Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway
Huanfeng Chen, Jinoh Kim, Debra A. Kendall
We have developed a system for examining the relative affinity of two different signal peptides for the protein secretion pathway in Escherichia coli. This system involves the expression of a modified alkaline phosphatase which possesses two signal peptides arranged in tandem. When both signal peptides have the wild-type sequence, cleavage after the first and cleavage after the second occur with nearly equal frequency. In both cases the remainder of the protein is transported to the periplasm. Thus both signal peptides effectively compete with each other fur entrance to the secretion pathway. When the hydrophobicity of the second signal peptide is altered by small increments, we find that the more hydrophobic signal peptide is preferentially utilized. Thus, a more hydrophobic signal peptide can outcompete even an efficient wild-type signal sequence. The crossover point, for utilization of the second to the first signal peptide, is marked and occurs over a very small change in hydrophobicity. Our results suggest that the small differences in the hydrophobicity of wild-type signal peptides may have critical consequences: preproteins with the more hydrophobic signals could dominate one pathway, leaving those with only slightly less hydrophobic signals to require additional factors such as chaperonins, SecB, and other binding proteins.
Fingerprint Dive into the research topics of 'Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway'. Together they form a unique fingerprint.
Secretory Pathway Medicine & Life Sciences
Protein Sorting Signals Medicine & Life Sciences
Hydrophobic and Hydrophilic Interactions Medicine & Life Sciences
Chaperonins Medicine & Life Sciences
Periplasm Medicine & Life Sciences
Alkaline Phosphatase Medicine & Life Sciences
Carrier Proteins Medicine & Life Sciences
Chen, H., Kim, J., & Kendall, D. A. (1996). Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway. Journal of Bacteriology, 178(23), 6658-6664.
Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway. / Chen, Huanfeng; Kim, Jinoh; Kendall, Debra A.
In: Journal of Bacteriology, Vol. 178, No. 23, 1996, p. 6658-6664.
Chen, H, Kim, J & Kendall, DA 1996, 'Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway', Journal of Bacteriology, vol. 178, no. 23, pp. 6658-6664.
Chen H, Kim J, Kendall DA. Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway. Journal of Bacteriology. 1996;178(23):6658-6664.
Chen, Huanfeng ; Kim, Jinoh ; Kendall, Debra A. / Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway. In: Journal of Bacteriology. 1996 ; Vol. 178, No. 23. pp. 6658-6664.
@article{e9bc5e8a8f8642918e16d16dafb7229e,
title = "Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway",
abstract = "We have developed a system for examining the relative affinity of two different signal peptides for the protein secretion pathway in Escherichia coli. This system involves the expression of a modified alkaline phosphatase which possesses two signal peptides arranged in tandem. When both signal peptides have the wild-type sequence, cleavage after the first and cleavage after the second occur with nearly equal frequency. In both cases the remainder of the protein is transported to the periplasm. Thus both signal peptides effectively compete with each other fur entrance to the secretion pathway. When the hydrophobicity of the second signal peptide is altered by small increments, we find that the more hydrophobic signal peptide is preferentially utilized. Thus, a more hydrophobic signal peptide can outcompete even an efficient wild-type signal sequence. The crossover point, for utilization of the second to the first signal peptide, is marked and occurs over a very small change in hydrophobicity. Our results suggest that the small differences in the hydrophobicity of wild-type signal peptides may have critical consequences: preproteins with the more hydrophobic signals could dominate one pathway, leaving those with only slightly less hydrophobic signals to require additional factors such as chaperonins, SecB, and other binding proteins.",
author = "Huanfeng Chen and Jinoh Kim and Kendall, {Debra A.}",
journal = "Journal of Bacteriology",
T1 - Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway
AU - Chen, Huanfeng
AU - Kim, Jinoh
AU - Kendall, Debra A.
N2 - We have developed a system for examining the relative affinity of two different signal peptides for the protein secretion pathway in Escherichia coli. This system involves the expression of a modified alkaline phosphatase which possesses two signal peptides arranged in tandem. When both signal peptides have the wild-type sequence, cleavage after the first and cleavage after the second occur with nearly equal frequency. In both cases the remainder of the protein is transported to the periplasm. Thus both signal peptides effectively compete with each other fur entrance to the secretion pathway. When the hydrophobicity of the second signal peptide is altered by small increments, we find that the more hydrophobic signal peptide is preferentially utilized. Thus, a more hydrophobic signal peptide can outcompete even an efficient wild-type signal sequence. The crossover point, for utilization of the second to the first signal peptide, is marked and occurs over a very small change in hydrophobicity. Our results suggest that the small differences in the hydrophobicity of wild-type signal peptides may have critical consequences: preproteins with the more hydrophobic signals could dominate one pathway, leaving those with only slightly less hydrophobic signals to require additional factors such as chaperonins, SecB, and other binding proteins.
AB - We have developed a system for examining the relative affinity of two different signal peptides for the protein secretion pathway in Escherichia coli. This system involves the expression of a modified alkaline phosphatase which possesses two signal peptides arranged in tandem. When both signal peptides have the wild-type sequence, cleavage after the first and cleavage after the second occur with nearly equal frequency. In both cases the remainder of the protein is transported to the periplasm. Thus both signal peptides effectively compete with each other fur entrance to the secretion pathway. When the hydrophobicity of the second signal peptide is altered by small increments, we find that the more hydrophobic signal peptide is preferentially utilized. Thus, a more hydrophobic signal peptide can outcompete even an efficient wild-type signal sequence. The crossover point, for utilization of the second to the first signal peptide, is marked and occurs over a very small change in hydrophobicity. Our results suggest that the small differences in the hydrophobicity of wild-type signal peptides may have critical consequences: preproteins with the more hydrophobic signals could dominate one pathway, leaving those with only slightly less hydrophobic signals to require additional factors such as chaperonins, SecB, and other binding proteins.
JO - Journal of Bacteriology
JF - Journal of Bacteriology