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The mammalian eukaryotic initiation factor 4GI (eIF4GI) may be divided into three roughly equal regions; an amino-terminal one-third (amino acids [aa] 1 to 634), which contains the poly(A) binding protein (PABP) and eIF4E binding sites; a middle third (aa 635 to 1039), which binds eIF4A and eIF3; and a carboxy-terminal third (aa 1040 to 1560), which harbors a second eIF4A binding site and a docking sequence for the Ser/Thr kinase Mnk1. Previous reports demonstrated that the middle one-third of eIF4GI is sufficient for cap-independent translation. To delineate the eIF4GI core sequence required for cap-dependent translation, various truncated versions of eIF4GI were examined in an in vitro ribosome binding assay with β-globin mRNA. A sequence of 540 aa encompassing aa 550 to 1090, which contains the eIF4E binding site and the middle region of eIF4GI, is the minimal sequence required for cap-dependent translation. In agreement with this, a point mutation in eIF4GI which abolished eIF4A binding in the middle region completely inhibited ribosomal binding. However, the eIF4GI C-terminal third region, which does not have a counterpart in yeast, modulates the activity of the core sequence. When the eIF4A binding site in the C-terminal region of eIF4GI was mutated, ribosome binding was decreased three- to fourfold. These data indicate that the interaction of eIF4A with the middle region of eIF4GI is necessary for translation, whereas the interaction of eIF4A with the C-terminal region plays a modulatory role.
All eukaryotic cellular (except organellar) mRNAs possess a cap structure (m7GpppN, where N is any nucleotide) at the 5′ end. The cap structure is bound by translation initiation factor 4F (eIF4F) as the first step of cap-dependent translation. eIF4F consists of three subunits, eIF4E, eIF4A, and eIF4G. eIF4E binds the cap structure directly and consequently is required for cap-dependent translation. eIF4A exhibits RNA-dependent ATPase activity and ATP-dependent RNA helicase activity. The helicase activity is though to be required for the melting of mRNA 5′ untranslated region secondary structure to facilitate ribosome binding (for reviews, see references 5, 19, and28). eIF4G is an adapter protein with a modular structure. It bridges the ribosome to the mRNA via eIF3 (for reviews, see references 20, 22, and 27). The human eIF4G may be divided into three distinct functional domains. The N-terminal one-third (amino acids [aa] 1 to 634) contains the eIF4E binding site (14, 18) and a recently described poly(A) binding protein (PABP) binding site (13). The middle third (aa 635 to 1039) possesses eIF3 and eIF4A binding sites (12) as well as an RNA binding site (6, 24). The C-terminal third (aa 1040 to 1560) contains a second eIF4A binding site (12, 14) and a Mnk1 binding site (26, 30). The middle third of eIF4G is sufficient for cap-independent binding of ribosomes to the encephalomyocarditis virus (EMCV) internal ribosomal entry site (IRES) (24) and for cap-independent but 5′-end-dependent translation (2). The function of the C-terminal region of human eIF4G is unclear.
The eIF4G-related mammalian protein p97/NAT1/DAP-5 (11, 16, 31), which is homologous to the carboxyl two-thirds of eIF4G, does not contain an eIF4A binding site in its C-terminal region (12). While the middle region is phylogenetically conserved, the C-terminal one-third is not. The wheat eIF4G homolog possesses a much shorter C terminus (1), and the Saccharomyces cerevisiae eIF4G homolog does not possess a sequence with homology to the mammalian C-terminal third (6).
In this study, using a toeprinting technique with the β-globin mRNA as a template (25), we define the region beginning at the eIF4E binding site and encompassing the middle third of eIF4G as the minimum sequence required for cap-dependent 40S ribosome binding. Our data provide evidence that the C-terminal region plays a modulatory role.
Construction of plasmids.Plasmids pcDNA3-HA (hemagglutinin), pcDNA3-FLAG, and pcDNA3-GST (glutathioneS-transferase) plasmids (13) were used as vectors for expression in HeLa cells. pBlueBacHis (Invitrogen) was used for generating recombinant baculoviruses expressing His-tagged eIF4GI and mutants in Sf9 cells. To construct pBlueBacFLAG, the His tag sequence in pBlueBacHis was replaced with the FLAG sequence. Deletion and point mutants of eIF4GI were generated using PCR with primers containingEcoRI (5′ primer) and XhoI (3′ primer) restriction enzyme sequences. All constructs were sequenced in their entirety.
Antibodies.Anti-hPrt1 (human Prt1), anti-eIF4GI(1–329), and anti-GST antisera were obtained by immunizing rabbits with GST-hPrt1(147–209), GST-eIF4GI(1–329), and GST, respectively. Anti-HA and anti-His6 monoclonal antibodies were obtained from BAbCo. Anti-Xpress and anti-FLAG monoclonal antibodies were obtained from Invitrogen and Sigma, respectively. Monoclonal anti-eIF4A was a kind gift from H. Trachsel.
Purification of recombinant proteins.His-eIF1, His-eIF1A, His-eIF4A, and His-eIF4E were expressed in Escherichia coliBL21(DE3) and purified by Ni-agarose (Qiagen) chromatography as described previously (23, 25). Baculoviruses expressing FLAG-eIF4B or His- or FLAG-eIF4GI proteins were generated by using the pBlueBac baculovirus expression system (Invitrogen). Log-phase Sf9 cells (200 ml of 2 × 106 cells/ml) were infected with a recombinant virus at multiplicity of infection of 5 and cultured for 40 h at 27°C. Expressed proteins were purified by Ni-agarose (Qiagen) or anti-FLAG-agarose (Sigma) chromatography. Concentrations of recombinant proteins were determined by comparison with standard bovine serum albumin (Ambion) following sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) and staining with Coomassie blue. Sf9 cell proteins copurified with His-tagged proteins were not considered to affect the functional analyses, because nickel resin-bound proteins purified from uninfected Sf9 cells did not inhibit or enhance ribosome binding activity or in vitro translation (data not shown).
40S ribosomal subunits, eIF2, eIF3, and eIF4F were purified from ribosomal pellets of Krebs cell extracts or rabbit reticulocyte lysate as described previously (23).
Assembly and toeprint analysis of 48S complexes.Reaction mixtures (40 μl) containing native α- and β-globin mRNA (Life Technologies) (0.3 μg), His-eIF1 (0.5 μg), His-eIF1A (0.5 μg), eIF2 (3 μg), eIF3 (7 μg), FLAG-eIF4B (1 μg), Met-tRNAi Met (4 pmol), 40S ribosomal subunits (4 pmol), His- or FLAG-eIF4GI (2 μg, unless indicated), His-eIF4E (0.3 μg), and His-eIF4A (3 μg) were incubated in buffer (2 mM dithiothreitol, 100 mM KCl, 20 mM Tris-HCl [pH 7.6], 2.5 mM magnesium acetate, 100 U of RNasin [Promega], 1 mM ATP, 0.4 mM guanylyl imidodiphosphate [GMP-PNP], 250 μM spermidine) for 5 min at 30°C. Following the addition of 4 pmol of oligonucleotide 5′-GCATTTGCAGAGGACAGG-3′ (complementary to β-globin positions 177 to 194), incubation was continued for 3 min at 30°C, and the mixture was then placed on ice. For reverse transcriptase reactions, the mixture was incubated for 40 min at 30°C after addition of 1 μl of magnesium acetate (320 mM), 4 μl of deoxynucleoside triphosphate mix solution (5 mM dCTP, dGTP, and dTTP; 1 mM dATP), 1 μl of [α-32P]dATP (6000 Ci/mmol; DuPont, NEN), and 15 U of avian myeloblastosis virus reverse transcriptase (Amersham Pharmacia Biotech Inc.). cDNA products were extracted with phenol-chloroform (1:1) and precipitated with ethanol (25). The same primer was used for sequencing of plasmid pBS−(β-globin), harboring β-globin cDNA (10). The products of primer extension and sequence products were resolved side by side on a sequencing gel. In the relevant figures, the full-length cDNA product and the toeprint product are marked "E" and "Complex II," respectively. The intensity of E and complex II was quantitated by BAS-2000 phosphorimager (Fuji). The relative efficiency of complex II formation was calculated as complex II/complex II + E. Values represent the means and standard errors of three independent experiments.
Protein immunoprecipitation.HeLa R19 cells (6-cm-diameter dish) were infected with vaccina virus vTF7-3 (3) for 1 h and then transfected with plasmids by using Lipofectin (Gibco BRL). Sixteen hours later, cells were lysed in 400 μl of buffer A (20 mM HEPES-KOH [pH 7.6], 100 mM KCl, 0.5 mM EDTA, 20% glycerol) containing 0.5% Triton X-100, 50 μg of RNase A per ml, and protease inhibitor cocktail (Boehringer Mannheim). After centrifugation, the supernatant was mixed with anti-HA or anti-FLAG antibody (2 μg) immobilized on protein G-Sepharose (10 μl) and incubated for 4 h at 4°C. After being washed with buffer A (400 μl, three times), bound proteins were dissolved in Laemmli buffer. The samples were resolved by SDS-PAGE and analyzed by Western blotting. Protein bands were visualized with an enhanced chemiluminescence detection system (Boehringer Mannheim).
To coprecipitate FLAG-Mnk1 with GST fusion proteins, cell extracts expressing FLAG-Mnk1 and a GST fusion protein were incubated with glutathione-Sepharose beads (15 μl; Amersham Pharmacia Biotech Inc.) for 4 h at 4°C. After being washed with buffer A containing 0.1% Triton X-100 (400 μl, three times), bound proteins were eluted with a buffer (40 μl) containing 20 mM reduced glutathione, 50 mM Tris-HCl (pH 8.0), and 100 mM KCl.
In vitro translation.Rabbit reticulocyte lysate (Promega) was treated with rhinovirus 2Apro (40 μg/ml) for 5 min at 30°C (7), followed by incubation for 10 min on ice with 0.8 mM elastatinal (Sigma). Aliquots (12.5 μl) were supplemented with eIF4E (0.2 μg) and/or wild-type or mutant eIF4GI (1 μg, unless indicated) and programmed for translation with 0.1 μg of capped bicistronic pGEMCAT/EMC/LUC mRNA (7) in the presence of [35S]methionine. Translation reaction mixtures were incubated at 30°C for 60 min and analyzed by SDS-PAGE (12.5% gel). Gels were fixed with 40% methanol–7% acetic acid, treated with En3Hance (Dupont, NEN) and processed for autoradiography. The intensity of the bands was determined with a BAS-2000 phosphorimager.
In vitro protein binding assay.A His-tagged protein (5 μg) was incubated with FLAG-eIF4A (4 μg or 8 μg) immobilized on anti-FLAG agarose resin in buffer A (50 μl) containing 0.1% Triton X-100 for 10 min on ice. The resin was washed with buffer A containing 0.1% Triton X-100 (400 μl, three times) and dissolved in Laemmli buffer. The sample was resolved by SDS-PAGE followed by Western blotting.
The eIF4E binding site and middle third of eIF4G are necessary and sufficient for cap-dependent translation.The toeprinting analysis has proven extremely useful for the study of translation initiation (23, 25). In the presence of β-globin mRNA (a typical cap-dependent mRNA), Met-tRNA, ATP, 40S ribosomal subunits, eIF1, eIF1A, eIF2, eIF3, eIF4B, eIF4A, and eIF4F, a 48S ribosomal complex is formed on the initiation codon of the mRNA. No signal was detected in the presence of mRNA, Met-tRNA, and ATP alone (Fig.1, lane 1). The ribosomal complex is detected by primer extension as a toeprint 15 to 17 nucleotides downstream from the initiation codon (25) (lane 2). This toeprint is termed complex II (25). To study the function of eIF4GI in cap-dependent translation, eIF4F was replaced by a combination of recombinant eIF4GI(157–1560), eIF4A, and eIF4E. Complex II was formed with these three recombinant proteins as efficiently as with eIF4F (compare lane 3 to lane 2). Control experiments in which eIF4A or eIF4E were omitted were performed. Complex II was not detectable in the absence of eIF4A (lane 4), confirming the importance of eIF4A for 48S ribosomal complex formation. However, the 48S complex was formed at the correct position in the absence of eIF4E (lane 5), albeit with much lower efficiency (compare lane 5 to lane 3). Complex II was not formed, however, when eIF4GI(157–1560) was omitted (lane 6). These results confirm that eIF4G is essential for 48S ribosomal complex formation, and they validate the use of recombinant eIF4G in this assay system.
Recently, the eIF4GI coding sequence was extended by 156 amino acids at the N terminus, to a total of 1560 amino acids (13). Because full-length eIF4GI(1–1560) is difficult to express in cells (13), a truncated protein (32), eIF4GI(157–1560), was the longest form used in this study and is referred to as full-length eIF4GI throughout this report. To delineate the minimal sequence of eIF4GI required for cap-dependent translation, several different fragments of eIF4GI were generated (Fig.2A), and tested for 48S ribosomal complex formation by the toeprint assay. eIF4GI(550–1560), which lacks a large part of the N-terminal region but retains the eIF4E binding site, functioned as efficiently as control eIF4GI(157–1560) (Fig. 2B, compare lanes 3 and 5). However, deletion of the eIF4E binding site markedly (80%) reduced cap-dependent 40S ribosomal binding (compare lanes 5 and 6). The residual activity (20%) is consistent with the background level of binding observed for control eIF4GI in the absence of eIF4E (Fig. 1). The reasons for the residual activity will be addressed in Discussion. eIF4GI(157–1090), which lacks the C-terminal third, retained ∼60% of the activity of control eIF4GI (compare lanes 3 and 4). Strikingly, efficient binding of 40S ribosomes (70% of control) was achieved by an eIF4GI protein possessing only the eIF4E binding site and the middle third (aa 550 to 1090), which contains binding sites for eIF3 and eIF4A (lane 7). In contrast to the results obtained for EMCV IRES RNA (24), the middle domain alone failed to support 40S ribosome binding to β-globin mRNA (lane 8). These results were reproducible with a wide concentration range (0.5 to 4 μg) of eIF4GI and its mutants (data not shown).
To further substantiate these conclusions, we extended the experiments to a rabbit reticulocyte lysate in vitro translation system. The lysate was pretreated with rhinovirus 2Apro to cleave the endogenous eIF4G. This treatment results in inhibition of cap-dependent translation and stimulation of IRES-dependent translation (7, 9). The 2Apro-treated lysate was programmed with a bicistronic mRNA in which translation of the first cistron (chloramphenicol acetyltransferase [CAT]) is cap dependent but translation of the second cistron (luciferase), which is preceded by the EMCV IRES, is cap independent (7). Treatment with 2Apro dramatically (85%) reduced cap-dependent translation, as expected (Fig. 2C, compare lane 2 to lane 1). While addition of eIF4E alone failed to enhance cap-dependent translation of the CAT cistron (lane 3), addition of eIF4E plus eIF4GI(157–1560) restored cap-dependent translation to 65% of the untreated control level (compare lane 4 to lane 1). The eIF4GI C-terminal third fragment is not critical for cap-dependent translation, because eIF4GI(157–1090) retained approximately half of the activity of control eIF4GI (compare lanes 4 and 5). In contrast, the eIF4E binding site is important for cap-dependent translation, because eIF4GI(613–1560) and eIF4GI(613–1090) were extremely feeble in stimulating cap-dependent translation (lanes 7 and 9). These results demonstrate that the minimal region required for cap-dependent translation is the eIF4GI(550–1090) fragment, which contains the eIF4E, eIF3, and one (the middle) eIF4A binding site. Thus, the eIF4A binding site in the C-terminal region (aa 1090 to 1560) of eIF4GI (12, 14) does not play a critical role in cap-dependent translation. In this regard, yeast eIF4Gs, which do not possess a region corresponding to the C-terminal third of human eIF4G, bind eIF4A (21). eIF4GI and deletion mutant proteins used in the above experiments were analyzed by SDS-PAGE followed by Western blotting (Fig. 2D) to indicate that similar amounts of the different proteins were utilized.
Point mutations which abolish eIF4A binding activity of the middle or C-terminal domain.To explore the possible function of the C-terminal eIF4A-binding site and to contrast it with that of the middle domain, we further delimited the middle and C-terminal regions of eIF4GI for eIF4A binding and generated point mutants (Fig.3 shows amino acid sequences). First, N-terminally truncated versions of the middle domain of eIF4GI were expressed as C-terminally FLAG-tagged proteins in HeLa cells and immunoprecipitated with anti-FLAG antibody. The immunoprecipitates were resolved by SDS-PAGE and analyzed by Western blotting with anti-FLAG, anti-hPrt1 (a subunit of eIF3), and anti-eIF4A antibodies (Fig.4A). The boundary of eIF4A and eIF3 binding region in eIF4GI resides between aa 672 and 702, because eIF4GI(672–1090) bound both proteins but eIF4GI(702–1090) bound neither (lanes 4 and 5). C-terminally truncated forms of the middle region of eIF4GI were expressed as N-terminally HA-tagged proteins for similar binding assays (Fig. 4B). The C-terminal boundary of eIF4A binding lies between aa 947 and 970, because eIF4GI(642–970) bound eIF4A but eIF4GI(642–947) did not (lanes 6 and 7). Interestingly, binding of eIF3 requires an extended C-terminal sequence compared to eIF4A binding: the C-terminal boundary of eIF3 binding resides between aa 1055 and 1065 (lanes 4 and 5). To show that eIF4GI(672–970) and eIF4GI(672–1065) are the minimal fragments that bind eIF4A or eIF3, HA-tagged fragments of eIF4GI were expressed for immunoprecipitation with anti-HA antibody followed by Western blotting (Fig. 4C). eIF4GI(672–970) bound eIF4A, while eIF4GI(702–970) did not (lanes 3 and 4). eIF4GI(672–1065) bound eIF3, while eIF4GI(672–970) did not (lanes 2 and 3). Thus, the minimal fragments of the eIF4GI middle region which are required for eIF4A and eIF3 binding comprise aa 672 to 970 and 672 to 1065, respectively.
Next, several amino acids in eIF4GI(672–970) which are conserved among eIF4GI, eIF4GII and p97 were mutated to alanines (Fig. 3). HA-tagged eIF4GI-middle third (aa 613 to 1090) fragments harboring the mutations were expressed in HeLa cells and immunoprecipitated with anti-HA antibody for Western blotting with anti-HA, anti-hPrt1, and anti-eIF4A antibodies (Fig. 4D). Mutations of tyrosine 776, phenylalanine 862, or phenylalanine 938 to alanines abolished eIF4A binding, yet the proteins retained eIF3 binding activity (lanes 4, 6 and 8). Other mutations, including phenylalanine 737, phenylalanine 812, or phenylalanine 920 to alanines, affected neither eIF3 nor eIF4A binding (lanes 3, 5 and 7). Thus, eIF3 binds to the middle domain of eIF4GI independently of eIF4A. These results also exclude the possibility that the mutations caused unfolding and denaturation of the proteins. An in vitro binding assay was carried out with the mutant Y776A, which retained 70% of the wild-type eIF3 binding, as determined by laser densitometry (Fig. 4D). Equal amounts of His-eIF4GI(157–1090) or His-eIF4GI(157–1090) Y776A were mixed with FLAG-eIF4A immobilized on anti-FLAG resin. After washing, proteins were eluted and subjected to SDS-PAGE, followed by Western blotting with anti-FLAG or with anti-His-tag. eIF4GI(157–1090) was bound to eIF4A (Fig. 4E, lane 1), while eIF4GI(157–1090) Y776A was not (lane 2), confirming that mutation Y776A abolishes eIF4A binding to the middle third fragment of eIF4GI.
To delimit the eIF4A binding site in the C-terminal region of eIF4GI, GST fusion fragments were expressed together with HA-tagged eIF4A in HeLa cells. Cell extract was immunoprecipitated with anti-HA antibody, and immunoprecipitates were resolved by SDS-PAGE followed by Western blotting with anti-HA antibody for eIF4A or anti-GST for eIF4GI fragments (Fig. 5A). The N-terminal boundary of eIF4A binding resides between aa 1201 and 1235, because eIF4GI(1201–1445) bound eIF4A but eIF4GI(1235–1445) did not (lanes 4 and 5). The C-terminal boundary resides between aa 1370 and 1411, because eIF4GI(1201–1411) bound eIF4A but eIF4GI(1201–1370) failed to bind (lanes 2 and 3). Thus, based on this analysis, eIF4GI(1201–1411) is the minimal region for eIF4A binding in the C-terminal region.
To create point mutations in the eIF4A binding region of the eIF4GI C-terminal third, three amino acid stretches of eIF4GI were mutated to alanines (FVR1239AAA, KKV1351AAA, and FEQ1377AAA [Fig. 3]). These amino acid stretches are conserved in eIF4GII but not in p97, whose C-terminal region does not bind eIF4A (12). HA-eIF4GI(1040–1560) or mutated fragments were expressed in HeLa cells and immunoprecipitated with anti-HA antibody (Fig. 5B). eIF4GI(1040–1560) FVR1239AAA did not bind eIF4A (lane 3), while the other two mutants, KKV1351AAA and FEQ1377AAA (lanes 4 and 5), bound eIF4A as well as wild-type protein (lane 2). To confirm that eIF4GI(1040–1560) FVR1239AAA was unable to bind eIF4A in vitro, equal amounts of His-tagged eIF4GI(1040–1560) or eIF4GI(1040–1560) FVR1239AAA were mixed with FLAG-eIF4A immobilized on anti-FLAG resin. After washing, proteins were analyzed by Western blotting for eIF4A or for His-tagged proteins (Fig. 5C). eIF4GI(1040–1560) bound eIF4A (lane 1), while eIF4GI(1040–1560) FVR1239AAA did not (lane 2). These binding assays suggest that either one or all of the amino acids FVR (aa 1239 to 1241) of eIF4GI are involved in eIF4A binding.
Distinct roles of the middle and C-terminal domains in eIF4A binding.To examine the physiological significance of eIF4A binding to the two binding sites in eIF4GI, recombinant full-length eIF4GI(157–1560) point mutants which abrogate eIF4A binding to either the middle or the C-terminal region were generated (Fig.6A; Western blotting shows that equal amounts of protein were used in the assay), and used in the ribosome toeprinting assay (Fig. 6B). Binding of eIF4A to the middle third of eIF4GI is essential for the 48S ribosomal complex formation, because no complex II was formed with full-length eIF4GI Y776A (compare lanes 3 and 4). Surprisingly, binding of eIF4A to the C-terminal region is also important for efficient 48S ribosomal complex formation, because ribosome complex II formation was decreased three- to fourfold when wild-type eIF4GI was replaced with eIF4GI FVR1239AAA (compare lanes 3 and 5). To substantiate these results, we performed a titration experiment whereby three different amounts of full-length wild type and mutant (FVR1239AAA) were tested in the toeprinting assay (Fig. 6C). At all concentrations, eIF4GI FVR1239AAA exhibited only 20 to 30% activity of wild-type eIF4GI in the ribosomal complex formation assay.
It could be argued that FVR1239AAA mutation causes partial denaturation of eIF4GI, which affects the functions of the other regions of eIF4GI. To address this possibility, the effects of the mutations in the middle and C-terminal regions in the context of full-length eIF4GI on eIF4A, eIF3, and eIF4E binding were determined. Coimmunoprecipitation was performed with anti-eIF4GI(1–329) antiserum following assembly of translation factors on β-globin mRNA (Fig. 6D). Mutation of either the middle (lane 3) or C-terminal (lane 4) eIF4A binding site dramatically decreased (10-fold, as determined by laser densitometry) the association of eIF4A with eIF4GI. In contrast, binding of eIF4E and eIF3 was not affected by either mutation. Thus, the defect of the mutant proteins in formation of the ribosomal complex is most probably due to their failure in eIF4A binding.
To further support these results, the mutants used for ribosome complex formation were examined in the 2Apro-treated rabbit reticulocyte lysate. 2Apro treatment dramatically reduced cap-dependent translation of CAT (Fig. 6E, compare lane 2 to lane 1). Addition of eIF4E by itself could not restore cap-dependent translation (lane 3), as shown above (Fig. 2C). However, addition of eIF4E together with eIF4G restored cap-dependent translation to 58% of the control level (compare lane 4 to lane 1). Addition of eIF4GI Y776A did not restore cap-dependent translation (lane 5), confirming that the binding of eIF4A to the middle domain of eIF4GI is essential for translation. Similarly, the importance of eIF4A binding to the C-terminal domain was corroborated, as eIF4GI FVR1239AAA stimulated translation to a much lesser extent than wild-type eIF4GI (24% of the wild-type level [compare lanes 4 and 6]). To substantiate this conclusion, we performed a titration experiment in which different amounts of full-length wild type and mutant (FVR1239AAA) were tested in in vitro translation (Fig. 6F). The capacity of eIF4GI FVR1239AAA to stimulate translation was four- to sixfold lower than the wild-type level within the range of the protein amounts examined.
The Mnk1 binding site does not overlap with the eIF4A binding site in the C-terminal region of eIF4GI.Recently, the serine/threonine kinase Mnk1 (4, 29) was shown to bind to the C-terminal region of eIF4G and to phosphorylate eIF4E (26, 30). However, it was not determined whether Mnk1 competes with eIF4A for binding to the C-terminal region. To address this question, progressive amino- or carboxy-terminal deletion mutants of the C-terminal region of eIF4GI were expressed as GST fusion proteins together with FLAG-Mnk1 in HeLa cells. Cell extracts were precipitated with glutathione-Sepharose, and bound proteins were eluted with glutathione (Fig.7A) or immunoprecipitated with anti-FLAG antibody (Fig. 7B). The N-terminal boundary for Mnk1 binding resides between aa 1411 and 1470, because eIF4GI(1411–1560) bound Mnk1 but eIF4GI(1470–1560) did not (Fig. 7A, lanes 3 and 4). The C-terminal boundary resides between aa 1545 and 1560, because eIF4GI(1411–1560) bound Mnk1 but eIF4GI(1235–1545) did not (Fig. 7B, lanes 3 and 4). Thus, the Mnk1 binding site, eIF4GI(1411–1560), does not overlap with the C-terminal eIF4A binding site (Fig.8, top).
In this report we demonstrate that a core sequence of 540 aa, comprising the middle third and eIF4E binding site of eIF4GI, is required and sufficient for cap-dependent translation. The middle third of eIF4GI binds two initiation factors, eIF4A and eIF3 (12), and possesses an RNA binding site (24). Owing to these features, this segment can mediate the internal entry of a 43S ribosome preinitiation complex on the EMCV IRES (24) and stimulate translation of uncapped RNAs in a reticulocyte lysate (2). However, all eukaryotic mRNAs possess a cap structure, and most are considered to be translated in a cap-dependent manner. Our present results demonstrate the importance of the middle region of eIF4GI for cap-dependent translation and further underscore the important role of the eIF4E-binding site for cap-dependent translation. We have also delimited the binding sites of eIF4A, eIF3, and Mnk1 on eIF4GI (Fig. 8, top).
Another important feature of eIF4GI characterized here is that binding of eIF4A to the C-terminal third region is required for robust translation, suggesting that the C-terminal region of eIF4GI plays a modulatory role. How does binding of eIF4A to the C-terminal region modulate the function of the core domain of eIF4GI? We consider two models, which are not necessarily mutually exclusive (Fig. 8). In model A, the C-terminal third folds over the middle region to inhibit its function in an autoinhibitory manner. eIF4A is sandwiched between the middle and C-terminal regions of eIF4GI, thus relieving the inhibition by the C-terminal region. Such a model may explain how eIF4AIII, a newly characterized translation modulator, functions (17). eIF4AIII, which exhibits 65% amino acid identity with eIF4AI, possesses RNA-dependent ATPase activity and ATP-dependent helicase activity, but it fails to substitute for eIF4AI in the ribosomal binding assay. In addition, eIF4AIII inhibits translation in a reticulocyte lysate (17). Interestingly, eIF4AIII binds eIFGI only through the middle region of eIF4GI. It is therefore conceivable that eIF4AIII fails to alleviate the inhibitory activity of the C-terminal part of eIF4G and instead forms an inactive eIF4F complex. The mechanism of action of a translation repressor protein, p97, may also be explained by this model. p97 is homologous to the C-terminal two-thirds segment of eIF4G, and it binds to eIF4A and eIF3 but not to eIF4E or PABP. p97 inhibits both cap-dependent and -independent translation, probably by sequestering eIF4A and eIF3 (11). Interestingly, the N-terminal half of p97, which corresponds to the middle region of eIF4G, binds eIF4A, but the C-terminal half, which corresponds to the C-terminal third of eIF4G, fails to bind eIF4A (12). Thus, the defect of p97 in stimulating translation might result from the inability of eIF4A to bind to the C-terminal half of p97, thus failing to counteract its autoinhibitory function.
An alternative model (Fig. 8, model B) for the function of the C-terminal region is that the middle region of eIF4GI is sterically hidden from free eIF4A by the C-terminal region. eIF4A binds first to the C-terminal region and is subsequently transferred to the middle region. This idea is consistent with another feature of eIF4AIII: while eIF4AIII strongly binds to the middle third of eIF4GI, it binds the full-length eIF4GI very poorly (17). To distinguish between these models, dissociation constants between eIF4A and each region or full-length of eIF4GI ought to be determined. Also, the number of eIF4A molecules that bind to eIF4GI at a given time will need to be established.
The C-terminal third of eIF4G also plays a role in the phosphorylation of eIF4E. The distal C-terminal region of eIF4GI contains a binding site for the serine/threonine kinase Mnk1 (Fig. 7). It has been shown that the C-terminal third of eIF4G recruits Mnk1 to phosphorylate eIF4E in vivo (26, 30), which is thought to stimulate cap-dependent translation. Phosphorylation of eIF4G itself may also affect translation. Interestingly, several serum-responsive phosphorylation sites are localized in the C-terminal third region of eIF4GI (B. Raught, A.-C. Gingras, S. P. Gygi, H. Imataka, S. Morino, A. Gradi, R. Aebersold, and N. Sonenberg, unpublished data).
What is the function of the N-terminal third of eIF4G? This region harbors the eIF4E and PABP binding sites and consequently engages the mRNA via both its 5′ and 3′ ends. While the critical role of the eIF4E-binding site for cap-dependent translation is confirmed in this study, our experiments did not address the importance of the PABP binding site in translation, because the recombinant eIF4GI which we used lacked this site. It should be very interesting, however, to examine how translation is affected when mRNA is circularized through the N terminus of eIF4G in a reconstituted translation system, using full-length eIF4G. However, current models state that the PABP interaction with eIF4G is not required for the first round of translation initiation, but only for subsequent rounds (28). The spacer region between the PABP and eIF4E binding sites (∼400 aa) is the least conserved region between eIF4GI and eIF4GII (7). We do not know the function of this region; no protein has been reported to bind this region, and its deletion had no effect on ribosomal binding (Fig. 2B) or on translation in the reticulocyte lysate (Fig. 2C).
Finally, using the in vitro ribosome binding assay, we demonstrated 48S ribosomal complex formation at the correct initiator AUG for the β-globin mRNA in the absence of eIF4E (Fig. 1) or with an eIF4GI mutant lacking the eIF4E binding site (Fig. 2B), albeit with low efficiency (20 to 24% of that of the complete system). The eIF4E-independent ribosome binding does not seem to represent aberrant ribosomes binding, since the ribosomal complex was not formed at the second AUG of β-globin mRNA (data not shown; the second AUG was out of the photograph in Fig. 1 and 2B). Thus, the binding represents cap-independent but 5′-end-dependent translation, which has been documented in a rabbit reticulocyte lysate (2) and in mammalian cells (8). The first AUG is still predominantly utilized as the translation initiator when the reticulocyte lysate is programmed with uncapped mRNA (2) or when uncapped mRNA is transcribed by RNA polymerase III in mammalian cells (8). These results are consistent with the idea that the cap structure dramatically enhances translation, rather than being absolutely required for translation in eukaryotes.
In summary, we have defined a minimal core sequence of eIF4GI which is required for ribosome binding and translation. The core sequence constitutes only one-third of the entire eIF4GI protein. The C-terminal third region, which does not have a counterpart in yeast, modulates eIF4GI activity. It is therefore of great importance to elucidate the mechanism by which the eIF4G C-terminal region controls translation in metazoan cells.
We thank W. C. Merrick for eIF2, eIF3, and eIF4F proteins used for a preliminary experiment, T. Skern for rhinovirus 2Apro, A. Gradi for the anti-eIF4GI antibody, and R. Fukunaga for the Mnk1 plasmid. We are indebted to C. Lister for excellent technical assistance. We thank B. Raught and A.-C. Gingras for sharing unpublished data and critically reading the manuscript.
S.M. was supported by research fellowships of the Japan Society for the Promotion of Science for Young Scientists. This work was supported by a grant from the Medical Research Council of Canada to N.S. N.S. is a Distinguished Scientist of the Medical Research Council of Canada and a Howard Hughes Medical Institute International Scholar.
Since the submission of this paper, a report by De Gregorio et al. (EMBO J. 18:4865–4874, 1999) also defined a conserved central domain (aa 642 to 1091) of eIF4G as an autonomous ribosome recruitment core in vivo.
- Received 30 August 1999.
- Accepted 6 October 1999.
- Copyright © 2000 American Society for Microbiology


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Residents of the Grand Bay area need a public library. There's no question about that, according to Citizens for a Better Grand Bay, whose statistics show 28,285 people with an average household income of $47,000 live in Grand Bay, Dawes, St. Elmo and Irvington. And Mobile Public Library data indicate the most frequent users of library services are in households with a $25,000 to $75,000 income, according to CBGB president Aleta Boudreaux.
Citizens for a Better Grand Bay are, and have been for several years, working toward the goal of providing a library for the area. And in the process, their plan is also to restore and use a couple of century-old buildings in the town's nationally recognized historic district.
The proposed Grand Bay Library will be housed in the two-story brick Grand Bay State Bank building at the corner of Dezauche Lane (Pottertract Road) and Freeland Avenue. When complete, in addition to being the Grand Bay Library and technology center, part of the building will be dedicated to historical and agricultural displays where residents can learn about the community's rich heritage of farming. The project also includes the renovation of the old Albert Freeland Store and a nearby area that will be used as a community park.
And all that takes money.
Boudreaux, coordinator for the Grand Bay Library Project, said the total amount needed to complete the library and museum is estimated at $656,000. As of the end of 2015, approximately 30 percent of the total building renovation had been completed. Funds have come from various grants, from local fundraisers and from individual donors.
Currently on the table is a $50,000 matching grant pledge from the Daniel Foundation. A total of $25,000 has been raised; the deadline to raise another $25,000 to get full credit from the grant is approaching in June.
About the need for a library in Grand Bay, Boudreaux said the nearest one is 13 miles away.
"And with no public transportation system, this creates a hardship on students and adults who need the resources of a local library for research and study and to apply for employment online," Boudreaux said. "By locating the library in a historic building, we are not only preserving our past, we are also preparing for the future growth of our rural area with a state-of-the-art modern library."
Boudreaux added, "More than just books and banks of computers, libraries are places where individuals gather to explore, interact and imagine. It is the goal that the Grand Bay Library will be a community-centered library, offering a space to meet the needs of our diverse population and become an essential part of our area's growth."
The Grand Bay Library will also be the focal point for a community redevelopment project that includes a second historic building, the Albert Freeland Grocery Store, with the adjacent land to be used as a park and recreation area and a pavilion on the site of the Old Grand Bay Depot. These open public areas will be used for market days, festivals, concerts and community gatherings, Boudreaux said.
The old brick building has an interesting past. Built in 1913, it served as the Grand Bay State Bank until 1929, the beginning of the Great Depression. From 1933-1975, the post office was located on the ground floor and, according to Boudreaux, "Many residents remember piano recitals and meetings held in the second-floor Masonic meeting hall."
Most recently, records show, the building was the site of the El Cazador Museum, where gold from a Spanish treasure ship found in the Gulf of Mexico was reclaimed and exhibited. A multimedia exhibit about the El Cazador is currently featured at GulfQuest National Maritime Museum in Mobile.
With the Daniel Foundation matching grant, this is a perfect time for those interested in seeing a Grand Bay Library complex come to fruition. They can make an outright donation, remember a loved one with a monetary memorial gift, contribute an honorarium to honor a living parent, family member, friend or beloved pet, or even set up a legacy fund from one's estate — or hold a fundraising event with proceeds to benefit the project.
Money can be sent online through gofundme.com/grandbaylibrary or through a PayPal account to email@example.com or simply donate by check, which should be mailed to CBGB-Grand Bay Library, P.O. Box 274, Grand Bay, AL 36541.
Donations are tax deductible and will directly benefit the community. For more information, call 251-656-4576.
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subset: commoncrawl


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Nov 19, 2013
It's a battle as old as time, the one between head and heart, primarily as it concerns romantic relationships. Luckily for me, I settled that particular battle a long time ago. When it comes to matters of romance neither organs have a say. I decide on using what really matters - a calculator and a checkbook.
Ha. Just kidding guys. I wish I had the wiring to be a gold-digger. Life would be void of love but filled with things! Oh, the glorious things!
Where the real fight between head and heart happens for me is in the tricky realm of future aspirations. Simply put, what is it that I want to do with my life? What will be my verb? "Hi, I'm Audrey and I'm a _______________." SEE MORE HERE.
Tags: life
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...are an electronica trio who have been around for a while now. They are pretty cool, here is their band profile page on their label's site (the label is aptly named Labels).
I didn't know about, ahem... their pornographic tendencies however, but they seem to do that with as much style and panache as they make music. Check out the following vids, they are awesomely cool and can be found lower down on that page where it says "LES CLIPS".
Plug Me In: Cute and peppy, woman-on-woman.
Metal Fingers In My Body: Appropriately more industrial-core, topic left to your imagination. Funny as hell.


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School Decorating Branksome
Every single pupil in your Branksome school must have at one point or the other paid some attention to their classroom walls. Yes, sometimes when they are bored in the middle of a lecture, they start to look around, other times they look around in search of tips related to topics they are learning or have learned in the past. Students are usually very grateful to have decorations up their classroom walls because wall decorations make learning more engaging.
Alternatively, blank, spartan classroom walls leave the students bored and uninterested in classroom topics, sometimes you find them falling asleep in the middle of their lessons, this is one reason many Branksome school owners nowadays insist on decorating their classrooms.
Sometimes the classrooms are decorated in such a way that the students can use the walls to their advantages, such as having amazing works of their fellow students put up on the walls or putting up class notes on the walls. School Decorations should not be done by just anybody. If they are you might find out that your classrooms are decorated in such a way that they distract or demotivate your pupils, that is why you need professional school Decorating job in your Branksome school.
Contact Us
Blakes Decorating Limited
Tel: 01202 873010
Mobile: 07828112538
Email: firstname.lastname@example.com
Send Enquiry
Blakes Decorating Limited
8 Milford Close
West Moors


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Marge Fenelon is a Catholic author, blogger, speaker, and award-winning journalist. She's a long-time correspondent for National Catholic Register, a columnist for the Milwaukee Catholic Herald and the author of several books on Marian devotion and
Catholic family life. She's also a weekly contributor to Relevant Radio's "Morning Air Show" and a popular guest on several other Catholic radio and television shows. Along with her husband, Mark, Marge also works as an educator in the Apostolic Movement of Schoenstatt. Together they have four grown children.
It will begin very soon.
We'll start to see Christmas trees on the curbsides or propped up against the back sheds. It usually starts the day after Christmas, with the number of discarded trees increasing until New Year's Day when it starts to taper off.
In the malls and on the city streets, the decorations are coming down, too. The After-Christmas sales are booming and the Return lines wind round and round the stores as folks come to exchange their unwanted Christmas presents.
For many, the Christmas season ends on December 26.
For faithful Catholics, the Christmas season begins at midnight on December 24 and continues well into January. While the rest of the world is winding down their Christmas celebrations, we're just gearing up for ours.
I feel so sad for those who miss out on the feasts and festivities that come after Christmas. They all have such deep meaning and are so rich with tradition that I wouldn't miss them for anything in the world. I look forward to every one of them and try to do something for home and family to make those days special.
We start with Christmas Octave.
Since the eighth century, the Church has observed octaves – eight days of celebration following a feast or solemnity. Christmas has its own octave, and so does Easter. For Christmas, the octave begins on Christmas Day and ends on January 1, the Solemnity of the Blessed Virgin Mary, Mother of God.
Both during and after the Octave of Christmas, there are number of feasts to commemorate and celebrate.
- December 26 – St. Stephen (the first martyr)
- December 27 – The Holy Family
- December 28 – Holy Innocents (children murdered by Herod's soldiers in the effort to destroy the Christ Child)
- January 1 – Holy Mary, Mother of God
- January 3 – The Epiphany of the Lord (visit of the Magi)
- January 10 – The Baptism of the Lord
Throughout those days, we hear in the daily readings the stories of the Nativity, but also of the prophecies of Simeon and Anna at the presentation and the finding of Jesus in the temple as well as the initiation of St. John the Baptist's ministry.
The Christmas season is filled with exciting scenes and happenings, all pointing to Jesus as the Christ. They all tell us about the magnificence and mission of the Infant born in Bethlehem that one day would be King.
That's the whole point of Christmas, isn't it?
The reason we have Christmas at all is because we are grateful and filled with joy that the God-Man has come to earth to bring salvation to all of mankind.
He is the Christ. That's worth celebrating for a good long time.
According to the to the Church, the Christmas season officially ends with the Baptism of the Lord, observed this year on January 10. That gives us 17 days to celebrate Christmas, and all of them begin and not end on Christmas Day.
I love that.
Every year our family becomes the counter-cultural ones on our street. We keep our decorations up and keep on celebrating throughout the entire Christmas season. I remember a few years that we kept our Christmas tree up until February 2 – the Feast of the Presentation of the Lord on the Roman calendar. We still laugh about the year our Christmas tree just couldn't hang in there. One or two days after Christmas as the kids were outside playing, they spotted a Christmas tree on the curbside that still was in great shape. So, they lugged it home and we put it up. Why let it go to waste?
I could say the same for the Christmas season. Why let it go to waste?
Marge Fenelon is a Catholic author, blogger, speaker, and award-winning journalist. She's a long-time correspondent for National Catholic Register, a columnist for the Milwaukee Catholic Herald and the author of several books on Marian devotion and


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Hi Loves So it is ay 3 of my Chambray Week! Here are 2 more looks from the YouTube video hope you all enjoy!
|Chambray Shirt J.Crew Factory Here
Shorts Forever 21 similar here
Moccasins Forever 21 here
Skirt Forever 21 similar here
Austin Cowboy boots Just Fab here
Chocolate Pearl Necklace similar here


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Roppongi 3K & Rocky Romero vs. SoCal Uncensored (Christopher Daniels, Frankie Kazarian & Scorpio Sky) – Winners: Roppongi 3K & Rocky Romero
Gedo & Hirooki Goto vs. Juice Robinson & David Finlay – Winners: Juice Robinson & David Finlay
Chuck Taylor & Toru Yano vs. Killer Elite Squad – Winners: Killer Elite Squad
Cody Rhodes & Marty Scurll vs. Guerrillas of Destiny – Winners: Cody Rhodes & Marty Scurll
Hiroshi Tanahashi, KUSHIDA, Dragon Lee & Rysuke Taguchi vs. Los Ingobernables de Japon (SANADA, Tetsuya Naito, BUSHI & Hiromu Takahashi) – Winners: Los Ingobernables de Japon
Rey Mysterio apologized for not being able to wrestle (Rey has a torn bicep) Jushin Thunder Liger. Mysterio promised that he will come back and wrestle in a NJPW ring.
Mysterio sat at ring side for the next match.
Jushin Thunder Liger vs. Will Ospreay – Winner: Will Ospreay
After the match, Ospreay issued a challenge to Mysterio. Marty Scurll ran in and hit Ospreay in the back with his umbrella. Mysterio tried to come in for the save but Scurll removed Mysterio's mask. Scurll stomped on Mysterio a few times before being chased off by Jushin Thunder Liger. Mysteruio got his mask back on and shook hands and embraced Liger and Ospreay.
Kazuchika Okada & Tomohiro Ishii vs. Zack Sabre Jr. & Minoru Suzuki – Winners: Zack Sabre Jr. & Minoru Suzuki – referee stoppage
It was announced that NJPW is returning to the United States on July 7 in San Francisco at the Cow Palace for a G1 Special.
IWGP United States Championship: (C) "Switchblade" Jay White vs. Hangman Page – Winner: Jay White
After the match, David Finlay ran in and took out White with a spear. Finlay challenged White to a Title match for April 24.
Golden Lovers (Kenny Omega & Kota Ibushi) vs. The Young Bucks – Winners: Golden Lovers
After the match, Cody came in and got in Matt Jackson's face yelling at him. Nick grabbed Cody and Cody shoved Nick to the mat. Omega came back in the ring and Cody fled the ring. Omega shook hand with Nick and offered his hand to Matt but Matt refused and walked away.
Omega got on the mic and said sometimes friends have to go to war and sometimes they are causalities. He wished he was more happy with the situation, but the silver lining is that the Golden Lovers are back and they are here to stay. He said he's going to beat Cody up in the very near future. They will up the ante at their next US show which will be bigger and better.


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This user has not added any information to their profile yet.
Rider info! Keep it updated prior to the event!
Next of Kin info! Keep it updated prior to the event!
I used to dream of #Fjellimellom, a month long MTB-ride across all the mountains in southern Norway. Now #Fjellimellom is temporarily dead. But #Fjellimellom is also ressurected. Now I dream of #Fjellimellom as taking part in and finishing #AroundNorway in 10–12 days.
56 years old


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If there is one word to describe Amber Gray, it's tenacious. After all, the 31-year-old College of Charleston student's path to a degree has been both uncharted in her family and an uphill battle, given the many demands on her time and attention.
Thanks to her impressive will, as well as philanthropic support, Gray today trains her tenacity on juggling a job, raising two young children and pursuing an undergraduate degree in the School of Professional Studies at the College of Charleston North Campus.
"In my family on my mom's side, I was the second person to finish high school," says the North Charleston native, whose degree was preceded only by one uncle. In her father's entire extended family, she was the third family member to do so, following two cousins who graduated before her. And she did so in the midst of considerable family turmoil.
"My parents were in and out of prison my whole life," says Gray. "They unfortunately got into drugs when they were 20 years old."
Because of this, Gray was raised by both her grandmothers, who took care of her starting at the age of 2 after her father was incarcerated until she was 10. Similarly, her mother spent more than 15 years cycling in and out of prison during Gray's early life.
"She would get in trouble and go back," says Gray. "It was always stealing and just things related to trying to get drugs."
Having since overcome those challenges, each parent has now cultivated a friendship with their daughter. However, there were challenges still for Gray. After having a child with an abusive former partner, she eventually found new happiness in a supportive husband, and the couple and her 5-year-old son this July welcomed a second baby boy to the family.
Of course, the demands of family and employment results in a particularly full plate as Gray pursues a college degree, which builds upon a two-year degree she earned from Trident Technical College. This was initiated while she was still in high school through the help of a guidance counselor, with 17-year-old Gray securing the necessary financial aid on her own to complete her associate's degree.
However, it was not until few years later, after joining the workforce, that she realized the lack of a full four-year undergraduate degree was holding her back professionally. With the encouragement of her husband, an attorney, Gray began her studies at the College in 2016.
All of her 60 Trident credits transferred, and she was able to start as a junior. After spending a few hours with a guidance counselor at the College and taking tests like the Myers-Briggs Type Indicator, she elected to major in project management.
"We realized how much I love organizing and planning," says Gray. "That really made sense for me."
It was around this time that Gray also discovered that the logistics of getting to the downtown campus from her home in Beaufort County were causing her undue stress, so it made sense that she should pursue a degree in her major through the College of Charleston's North Campus.
Today, Gray manages to balance caring for two young children, managing customer service concerns for Dunkin' Donuts from home and steadfastly gaining credits – many through online courses – to get that coveted degree.
A good deal of pressure in her hectic life has been relieved by the financial support she has received for her studies. Gray is a 2018–19 recipient of the School of Professional Studies scholarship fund and of various other grants and scholarships.
While alleviating the financial burden on her family, she says the support also relieves those small daily stressors by allowing her to afford to pick up a quick meal when course loads constrain her time. And, while there are certainly many demands on her time with all that is in play, Gray knows that, together, those components have created a meaningful, full life.
As a child, she had been urged by her grandmother to set her sights simply on succeeding by way of a good marriage. Gray has done that and is pursuing more.
"My grandmother always said, 'You have to marry a doctor or a lawyer,'" she recalls. "So it so happened to have worked out that way, but I'm also doing my thing, too."
With her trademark drive and commitment, she is certain to do so for years to come, empowered by a degree from the College of Charleston.
To support the School of Professional Studies, visit https://giving.cofc.edu/SPS


text:
- Learn to Row | Learn to Scull
- >
- Learn to Row
Learn to Row
per item
Learn to Row is a continuation of the Introduction to Rowing. The goal is to carry forward with the basic skills, to develop a solid foundationn in prepration for membership in Orlando Rowing Club and partitication in the Novice Sweep Rowing Programs. Whether your goals are to row competitively in your future or row for the recreational enjoyment of the sport, Learn to Row is a fundamental learning experience.


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SOME/IP analysing tool
The someIpAnalyzer is a analysing tool for SOME/IP and Service-Discovery. Based on a standard PC with Ethernet interface and WinPcap as an intermediate layer, the data is displayed in a web interface. A web interface is a local browser, such as Firefox, or a tablet.
There are different views for SOME/IP and Service-Discovery messages:
- Message counter
- Message view. In this view, SOME / IP and Service-Discovery messages with names and payload are displayed.
- Signal view. This view shows the physical values of individual signals.
- Diagram view. This view contains charts signals.
Bus systems supported:
- Service-Discovery
System requirements:
- Windows™ 7, Windows™ 10, Linux on request


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As summer comes to a close and everything below 14th street is infiltrated by confused students toting around pop-up New York City maps and attempting to ditch their Midwest roots, we've compiled a "back to school" themed throwback to the good ole days of slide-rules and Trapper Keepers. So rummage through your closet to find your favorite scrunchies and sticker books—school is in session!
Above, clockwise from upper left:
This tiny tin robot sharpener may not be able to bust down walls, but he sure bring your pencil to a point.
A classic must-have, this black leather Coach planner would keep us on track as we jet between first period Math and margaritas on the quad.
For hours of mathematical fun, pick up this snazzy retro calculator. After all, you forgot how to multiply as soon as they handed you that High School diploma.
Above, clockwise from upper left:
This nifty vintage suede-and-leather backpack can hold your lunch, crayon set, and make-up kit with ease and élan.


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#Debtline blog: More than 7 million people have been sucked in to their bank's or card provider's sales pitch that they 'needed' CPP insurance (card and ID protection insurance).
CPP's card protection product was sold as Card Guard by HSBC, Card Safe by M&S Money, Barclaycard Card Protection, Barclays Cardholder Protection, NatWest Card Protection, Egg Emergency Cover and Card Protection Plus and Commercial Card Protection by CPP and a number of its business partners.
Customers were told that they should take out card protection, which provided cover for fraud of up to £100,000. However, this was not really necessary as banks have to cover fraud as a matter of course. So if your bank account is defrauded by criminals, your bank will reimburse the money, unless they can prove the customer was grossly negligent.
The Financial Conduct Authority ("FCA") has confirmed that the major banks and credit card providers, together with CPP, have agreed to set up a central redress system to compensate customers. Compensation will be available for all customers who took out the insurance after 2005.
CPP should have written to all policyholders with more information about the compensation scheme and what to do next. If they haven't written to you, contact them if you had a policy you won't need to prove that the insurance was mis-sold to you as simply claiming guarantees your money back.
If you need more advice on any type of debt contact us at Twinpier


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The Board of Regents of the State of Iowa were tasked with finding a suitable replacement for outgoing University of Iowa President and, according to many faculty and graduate students, walking disaster, Sally Mason. Today they made their decision. This guy: Bruce Harreld.
(Image courtesy of KCRG)
President Harreld is certainly not a traditional choice for president of a major research university. For starters, his highest degree is an MBA and the extent of his experience in higher education is as adjunct faculty at Harvard Business School. Moreover, he displays a stunning ignorance of the responsibilities of the position as well as of how little he understands about what a university is.
Some examples of his answers to questions:
He revealed he has no idea what "contact hours" or "touch time" means in the context of "as graduate students 70% of undergraduate contact hours are with graduate assistants."
He apparently said in his speech he'd like the University of Iowa to become a public ivy, to which someone took issue and pointed out that it already is and questioned how he could possibly be qualified if he couldn't even properly research the institution. He said he got the information from Wikipedia (revealing he managed to misread Wikipedia, which does say it is a public ivy) and countered by asking the woman where she got her information from, and she said "I'm a lawyer. I don't read Wikipedia!" and cited Greene's Guides book on public ivies.
I got to him after question time was over and asked what he would be willing to do to make for a more amicable relationship between the administration and COGS (the union representing the graduate students employed at the university. He gave a non-answer and said that he would want to address specific issues that he doesn't know the full extent of but from what he heard from us today seems to be a number of things, rather than do a bunch of - and I quote directly - "kumbaya crap."
Harreld takes over the job on Nov. 2. That said, the above observations I made should be supplemented by others so we can get a full picture of what's going on.
The Iowa City Press-Citizen provides further evidence of Harreld's extreme unpopularity among faculty, staff, and students, as well as his lack of qualifications:
In addition to airing concerns about J. Bruce Harreld's personal business history, several University of Iowa questioners Tuesday noted they are more concerned at how his inclusion among the four finalists fits into a long-term trend they see among colleges, universities and their governing boards: Looking to the corporate sector to for leaders to turn around institutions of higher education.
Ed Wasserman, a professor of psychology, suggested in his question that providing a businessman with no university leadership experience was the equivalent of "giving the fox the key to henhouse" when it comes to transforming UI into a bottom-line business rather than an institution of higher learning.
"(The graduate employee union, COGS) believes that the three most important tasks of the president are to make sure that our university is fully funded by the state, that we address the issue of sexual assault on campus and that we address the needs of our growing international students.
None of these issue came up in his initial remarks.
He did address a specific sexual assault question in the Q&A period, and it seemed like he was committed to avoiding victim blaming and willing to deal with the cultural issues.
However, our remaining two points were unaddressed or, in the case of funding for the university, he seemed to be taking the opposite stance of where we think funding should be going."
— Bailey Kelley, a UI graduate student and trustee of COGS, UE Local 896.
"For somebody who is apparently made one of four finalists after a national search on grounds that they have business experience, at a minimum, they need to put their business experience on the table for examination. And I'm not confident that what he offers is very spectacular in terms of his business history.
But it's really troublesome that there is absolutely no experience at any level of education administration. ... .Nor has he been in a position to understand and implement the values of higher education ... in terms of culture (or) in terms of improving quality of life beyond what the university does for the economy of its state."
— Nicholas Johnson, retired UI adjunct faculty member in law.
"I don't know why he wants the job because he doesn't know any of the details about the finances.
When asked about any specific proposals, he would always go back out to very vague generalities. So I was very unimpressed.
And I'm also worried [he] wants to cut us out of existence because he's still open for cutting graduate and (teaching assistant) lines. He wants us to do research, but he won't say how we're going to be funded if we're not going to be teaching."
— Landon Elkind, a third year graduate student in philosophy [and financial officer for COGS] at UI.
The most bizarre aspect of his candidacy was certainly his CV. I have this saved in the event that the University of Iowa removes it from their online files like they did the video of his public forum job talk and Q&A. There are two very large oddities about this CV. The first is the last - his personal section, which appear to be things he believes qualify him personally for the position:
Married to Mary Gillilan Harreld for 42 years; BS Purdue University, Juris Doctorate Boston College
Four adult children who all have advanced degrees
Six grandchildren
Ordained Elder, Presbyterian Church
Reared in Midwest USA
Outside interests include traveling, reading, jogging, hiking
It reads like a dating site ad. One that would get no attention. Because it sucks.
The second, much more distressing part of his CV is his entry for most recent employment.
Executing Strategy, LLC Avon, Colorado 2014 - present
Managing Principal
Confidentially advise several public, private, and military organizations on leadership, organic growth and strategic renewal.
Here's the problem. There is no "Executing Strategy, LLC" in Avon Colorado or anywhere else in Colorado. There's a company by that name in Florida, but that is not this one. Harreld lists as his most recent job a position in a company which does not exist. The Press-Citizen reports:
On the resume available on the University of Iowa website, J. Bruce Harreld listed his current job as the managing principal for the Colorado-based Executing Strategy, LLC — a company that "confidentially (advises) several public, private and military organization on leadership, organic growth and strategic renewal."
The Colorado secretary of state, however, has no listing for a company of that name.
Harreld explained during Tuesday's public forum that the listing had been a mistake. He used the name of a limited liability company that he had been using in Massachusetts but no longer needed now that his clients wanted to work with him to assume liability directly. He allowed that company to lapse.
"So that's 'shame on me,'"Harreld said. "There is no Colorado corporation. That's my company. … It's me personally working."
The Massachusetts company does appear to exist, and is still listed as "Active" rather than lapsed.
Suffice to say, the appointment of Harreld to the presidency signals a move toward a more business-oriented approach to the governance of the University of Iowa. Given that all nine members of the board of regents have been appointed by Governor Branstad, that they are happy to seek new state funds for Iowa State University and University of Northern Iowa but not University of Iowa, and that Johnson County (where the University of Iowa is located) is the only county to have voted against Branstad in the last gubernatorial election it would appear that Harreld's selection by the Board of Regents may be a move calculated to punish the university.
Below you may watch the job talk and Q&A with Harreld via youtube, hopefully far beyond the reach of the Board of Regents's erasing grasp.
There are dark days ahead for the faculty and graduate students at the University of Iowa and real concern what Harreld's tenure could mean for the reputation and success of the University of Iowa as an educational and research institution.
A reminder: Harreld would not be qualified to even apply for an entry-level tenure-track job at the university he is now president of. A microcosm of what is happening to higher education at large in this country.


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FIFA SOCCER GAMEPLAY BETA Unreleased v11.5 APK Get a first take a gander at the new interactivity motor new to FIFA Mobile! This is your opportunity to experience, test, and even give criticism to our designers. This encourages us change our amusement to guarantee we're conveying the most ideal experience to the pitch, and to players around the world. Since this is a beta form, it would be ideal if you take note of that your advancement won't persist to the new season or add to your center diversion Ultimate Team. Beneath you'll discover an outline of what you can expect in the beta. Much obliged for your help!
We're presenting to you a little section of our up and coming refresh which will include energizing ongoing interaction, more legitimate and reasonable illustrations, and better approaches to play the soccer match you adore all determined by our interactivity motor new to FIFA Mobile.
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Fight it out, Head-to-Head, continuously with rivalry from around the globe. We're conveying our most asked for highlight to you, so get ready to provoke yourself, and domiate.
Construct YOUR ULTIMATE TEAM
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This application: Requires a persevering Internet association (arrange charges may apply). Requires acknowledgment of EA's Privacy and Cookie Policy and User Agreement. Incorporates into diversion publicizing. Contains guide connects to the Internet and informal communication destinations planned for a crowd of people more than 13. The application utilizes Google Play Game Services. Log out of Google Play Game Services previously establishment in the event that you would prefer not to impart your amusement play to companions.


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July 21, Colombo: A lawmaker of Sri Lanka's main opposition United National Party (UNP) says fishermen in the Chilaw area of the North West are being extorted by a group.
UNP Puttalam District parliamentarian Palitha Range Bandara has said a certain group in Chilaw was extorting monies from the fishermen by terrorizing them.
Range Bandara has told parliament that certain government politicians supported this group.
The fishermen, therefore, have to pay the extortionists on top of the three types of taxes imposed by the government, he has said.
The parliamentarian has said that monies were being extorted from the fishermen during weighing fish in the market using false weighing scales.
Range Bandara has added that false weighing scales were being used to weigh the fish after locking up a new weighing scale given by a group of fishermen and a priest in the area.
He has called on Fisheries Minister Dr. Rajitha Senaratne to visit the area and meet the fishermen to resolve the issue.


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For many baby boomers, retirees and seniors, winding down a career, or having an empty nest can be a shock. The quiet, and lack of daily demands can take some getting used to; and it is common to feel a lack of purpose. Studies show that NOT having a purpose in life can increase illness and reduce longevity.
With 10,000 people turning 65 per day, the aging population is growing, and with greater health and vitality, a new era of "active aging" is underway. The "Third Age" of life can be one of renewed purpose via encore careers, volunteering, caring for children or meaningful travel. Science shows the best gift we can give ourselves is to have an upbeat and positive attitude about the future- whatever comes.
"It is time to expand our perceptions of aging," said Paul Irving, president of the Milken Institute. "Having a sense of purpose literally changes everything."
Irving went on to offer four astounding statistics on the power of positive perceptions of aging and having a purpose:
- Yale University research has shown that older individuals with positive self-perceptions of aging lived 7.5 years longer.
- Rush University Medical Center found individuals with a high level of purpose were 2.4 times more likely to remain free of Alzheimer's disease.
- Older adults with positive perceptions of aging were 44% more likely to recover from severe disability than those with a negative perception of aging.
- Having a sense of purpose in life was associated with a 19% reduced risk for both heart disease and stroke.
"Having a sense of purpose is not just 'nice,' it is as important to our society as good nutrition, smoking cessation or exercise and should be a public health mandate."
At Silvernest, we have found that active aging extends into our perceptions of our homes. An empty house is a lonely house; and bringing in a roommate creates a positive vibe. Many homeowners say they are more motivated to take on little projects, cook meals, turn the music up and actually look forward to coming home seeing the lights on for a change!
Silvernest boldly breaks the rules of aging so you can share your home on your own terms. We're creating the next generation of roommates. A more modern kind. A well-matched kind. A kind that's just your style. Because around here, the details are totally up to you.


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Herculaneum | Panoramic view
View towards northeast. Excavated area in the town of Ercolano. Unlike Pompeii, Herculaneum was not destroyed by ash falls due to the 23 November 79 AD eruption of Mount Vesuvius (1281 m, right central background), but was deeply covered by pyroclastic surges during the following night. Many structures were preserved and then excavated since the 18th Century. At the time the pyroclastic flows occurred, the inhabitants had already fled towards the coast, but those who had not been evacuated by boats on time died through the intense heat. Since 1981, may skeletons have been found in the boat houses and along the former beach (central foreground of the photo).
- Keywords
- hazard impact, historic place, mirror of the past, mountaintop, ruin, stratovolcano, volcanism
- Created
- Saturday 18 June 2016 by Martin Mergili in Europe / Italy (2111 visits)


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Finland Middle School
1825 Finland Avenue | Columbus, Ohio 43223
Phone: (614) 801-3600 | Fax: (614) 278-6334 | Attendance: (614) 801-8874
Lori Balough, Principal | Jason Phillips, Assistant Principal | Erin Harris, School Counselor
To leave a voicemail in a teachers mailbox :
1. Call (614) 801-3190.
2. Enter the teacher's mailbox number.
If you don't know the mailbox number, you can search the directory by the teacher's last name. Click the blue bar above entitled "Teacher Telephone Extensions" to access the directory.
Dinner Grab and Go Pick-up
3:30pm - 4:30pm
Westland High School
Wednesday, March 25th
Thursday, March 26th
Friday, March 27th
Finland Middle School
1825 Finland Avenue
Columbus, Ohio 43223
(614) 801-3600
Fax: (614) 278-6334
March 17, 2020
Dear Finland Middle School Families,
There is a phrase, 'May you live in interesting times.' We think it is fair to say that we are living in interesting times right now. The purpose of this letter is two-fold: 1) sharing resources with parents on talking with their children about the Coronavirus; and 2) communicating the processes we will be using to continue education.
In times of crisis, parents may have difficulty knowing what to say when talking to their children. This is normal. As things seem to change on a day-to-day basis, concern can make both children and adults anxious.
1) We would like to offer some things to think about in case your child appears to be struggling with the current situation:
- Children look to adults for how to respond in times of crisis and will mirror the reactions of adults. The words we use and the actions we take will frame how children view this new circumstance. Remaining calm ourselves helps reassure our children to do the same.
- Routines are our friend. Routines bring familiarity and comfort to our lives. When we know what to expect and feel some level of control, we are better able to adapt to changing circumstances. Regular bed, meal, study, art, and play times are some of the ways to embed routines into our daily lives. Unpredictability and loss of control can leave us feeling stressed and anxious.
- Regardless of the logic, it is important to listen to children's feelings and answer their questions as best we can. Fear is an extremely contagious and powerful emotion. For some children fear can lead to irrational conclusions that cloud their every thought and action. Being able to verbalize these fears allows caregivers the opportunity to add a touch of realism, practicality, and being proactive. It also helps us reframe their concerns, so these fears can be significantly reduced.
- Finally, communicate hope. While children are very good at sensing insincerity, they are also influenced by aspirational thoughts and behaviors. Hope for better days and better outcomes can be more powerful than fear. Communicating that hard work, good decisions, and ingenuity will lead to a better tomorrow is an empowering thought.
- For tips and expert guidance, please consider exploring the following links:
- Talking to Children About COVID-19 ( from the National Association of School Psychologists) https://www.nasponline.org/resources-and-publications/resources-and-podcasts/school-climate-safety-and-crisis/health-crisis-resources/talking-to-children-about-covid-19-(coronavirus)-a-parent-resource
- The National Institute for Trauma and Loss in Children (TLC Institute – part of STARR Global) https://starr.org/covid-19-school-cancellation-and-trauma/
2) We will be educating students remotely for a period of time. Below are answers to some of the questions we have received about this process:
- What about Devices and Internet access?
- Almost any device that supports Internet browsing will work. Your child does not need to have a 'Chromebook' to access the lessons from their teachers. Any computer, tablet, phone or other internet capable device will work for this purpose.
- Last Friday, we made our first attempt to ensure that every home has access to a personal computing device. Many families already had their own device(s) and some students borrowed a device from school. If your student did not borrow a device or an additional device is needed because your household has multiple students attending the South-Western City School District and one is not sufficient, please contact your child's school attendance line leaving your child's name, grade, and homeroom/first period teacher's name, and a call back phone number. We will make arrangements with you to secure a device.
- We are in the process of securing an extremely limited number of wireless access points. These requests will be based on financial need beginning with the senior class and working downward through grade levels. Follow the procedure above if you have this need and we will try to assist you to the best of our ability. For requests that can't be met, please consider exploring places near your residence that offer this service for free or consider accessing district WiFi from common areas outside of our school buildings. Please remember that social distancing (6 feet) is a best practice and congregating on school property is currently prohibited.
- One final note: the district will not be filtering devices or access points while students are working remotely. While the district acceptable use policy remains in full effect, we are counting on caregivers to monitor the use, search activity, and social interactions in which students engage through these devices.
- If you encounter any technical problems with your child's Chromebook, please contact our Helpdesk for Chromebook assistance by calling (614) 801-3014 or emailing email@example.com
- How will learning activities and submitting assignments work?
- Email will be the primary method of communication during this time period. Every student has been issued a district email/account address.
- Assignment and learning activities will be distributed through email or another learning platform that have already been used in the classroom (such as Google classroom and iReady). These activities should take your child a regular class period to complete (25-50 minutes). Please remember some students work more quickly than others so times may vary. Videos, text, links to Websites, and downloadable PDFs will be among the most common materials with which students interact. While some activities will be completed in a single sitting, others could take several days. Students should expect to submit three items per subject per week that will receive teacher feedback. This will likely take the form of a graded activity. This could happen automatically as a normal course of the lesson, they may require uploading a pdf, it could be in the form of an email to the teacher, OR printed/created to submit in a physical form.
- What is the best way to communicate with staff?
- All staff have email addresses and phone extensions. Staff will communicate these directly to students. The format of email addresses in our district is email@example.com. Please be patient as our staff members work through their email and phone messages. Between student and parent communication, creating lessons in a new way, providing students feedback, and taking care of their own families, they will be stretched very thin at times. Many staff will be working remotely, therefore we encourage the use of email to communicate with staff members.
- How will the end of the grading period be handled?
- March 20 marks the end of the grading period. Recognizing the unexpected way this grading period has ended, students are encouraged to communicate with teachers sooner rather than later so that grades can be calculated for the quarter.
- Teachers have been asked to finalize third quarter grades no later than March 30, 2020.
- All assignments given beginning March 24 will be considered part of the final grading period.
- How will the district be distributing food to those in need?
- Our building will be used to distribute 'Grab-n-Go' breakfast and lunch meals for students who need food assistance. Meals will be available from 10:00 a.m. till noon, Monday through Friday, beginning Monday, March 23. A list of locations will also be available on our district Website at www.swcsd.us.
- For families with more immediate food needs, please visit our Website for additional resources.
- Assignments and other materials can also be returned during food pick up times. Please include the building and teacher name on any assignments/materials.
- How do I get the medication(s) my child left at school?
- If your child has medication in the clinic that you need to have returned, please contact the school phone number at (614) 801-3600.
We are grateful for our families who partner with us to make this community stronger for our children. Thank you for your patience over the past few days as we worked through our plans to close school, finalized our remote learning options, and provide families with the tools to help support their children's learning at home.
Sincerely, Ms. Balough Principal
The most recent information regarding school closings, and electronic teaching and learning can be found on the homepage of our district Website at www.swcsd.us. Thank you for your patience as we work to keep our students safe and learning.
Infinite Campus (IC) is the District's Internet-based student information system. Important features of IC are the Parent Portal and NEW Mobile App. Through the IC tools parents are able to access their child's information, such as class schedules, attendance, academic reports, transportation information, coursework, and put funds in their child's food service account online. Parents can also designate how and where they wish to receive emergency communications, attendance calls, general announcement messages, and e-mail messages from teachers, the school, and the school district.
To create an IC account, please go to: https://sites.google.com/swcsd.us/parentresources/infinite-campus/parent-portal-mobile-app
If you already have an IC account, please update your emergency contact information at: https://sites.google.com/swcsd.us/parentresources/infinite-campus/online-emergency-information-submission


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Tips For Caring For Extension
Hair extensions are a great way to change up your look or lengthen your hair. Extensions blend in with your hair for a natural look that can be styled the same as real hair. Proper care and maintenance of your extensions will keep them looking great! Here are some tips for care for extensions.
1. Remember, your extensions are a high maintenance product and as such you should expect to spend 20-30 minutes a day to care for and style them.
2. Extensions may be uncomfortable to sleep on the first few nights.
3. Your scalp may be slightly itchy the first few days after getting the extensions.
Above the three tips, you can take good care of your extensions.


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Thinking of bringing your garden back to life using less water this year? Always wanted to install a drip irrigation system and just don't know where to start?
Join us this weekend, May 14-15th from 9AM – 3PM for our DIG Drip Irrigation Demo Days. Manufacturer representatives will be on had to answer your questions and help you find the right products for your needs. Come on down and enter to win a FREE Drip Starter Kit.


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Same Day Flower Delivery Throughout NYC
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Green Gab Podcast | Helping Builders Build Green Homes
Gabbing with Michelle Foster of Home Innovation Research Labs, the VP of Innovation Services. Michelle speaks a lot with the housing financial industry to help them see the impact of an NGBS (National Green Building Standard) green certified home or project. Taking the lower expenses of a better built home into account in the financial process can allow more money to be spent on the asset of the home.
Home buyers can think holistically about where they will be most comfortable, what is the smartest investment for them and will make them happiest going forward. As we spend a lot of time indoors in our homes – our refuge, it only makes sense that our homes be comfortable and support our needs. An NGBS Green Certified Home can do just this.
Green homes are just a better place to call home!
Listen to the podcast and read the podcast notes.
Subscribe on iTunes and get the show notes on The Green Gab Podcast. Get the gab with us as we share what we've done, as well as tips for greening up your home, your job, your family and your life! Get in on the gab for why green matters.
Get Marla's book Living Green Effortlessly: Simple Choices to a Better Home. I'd love to speak at your next event – for ideas check out my speaking information. Thank you and have a blessed day.
For more information about the show, Marla at [email protected] or Tony at [email protected]
Marla Esser Cloos Marla inspires and educates about what makes a green home green and how to do it – a bit at a time or all at once. Her work creating an online owners' manual for green and greener homes, HomeNav.com, and work in national and local businesses, groups and associations, provides her a unique perspective to help people realize the true values of green homes as safer, healthier and more comfortable homes. Marla founded and co-hosts the Green Gab Podcast, on iTunes, 2 Guys Talking Podcast Network and GreenHomeCoach.com. She blogs on Green Home Coach and Proud Green Home. Her articles have appeared in Green Home Builder, Building Women and The Healthy Planet and she is the author of Living Green Effortlessly: Simple Choices to a Better Home from NAHB Builder Books. www
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