where does the lac repressor bind to dna
Lac repressor The lac repressor (LacI) operates by a helix-turn-helix motif in its DNA binding domain binding base-specifically to the major groove of the operator region of the lac operon, with base contacts also made by residues of symmetry-related alpha helices, the "hinge" helices, which bind deeply in the minor groove.[1] This DNA binding causes the specific affinity of RNA polymerase for the promoter sequence to increase sufficiently that it cannot escape the promoter region and enter elongation, and so prevents transcription of the mRNA coding for the Lac proteins.[2] When lactose is present, allolactose binds to the lac repressor, causing an allosteric change in its shape. In its changed state, the lac repressor is unable to bind tightly to its cognate operator. This effect is referred to as induction, because it induces, rather than represses, expression of the metabolic genes. In vitro, Isopropyl β-D-1-thiogalactopyranoside (IPTG) is a commonly used allolactose mimic which can be used to induce transcription of genes being regulated by lac repressor.
DNA The two DNA strands are called polynucleotides since they are composed of simpler monomer units called nucleotides.[2][3] Each nucleotide is composed of one of four nitrogen-containing nucleobases (cytosine [C], guanine [G], adenine [A] or thymine [T]), a sugar called deoxyribose, and a phosphate group. The nucleotides are joined to one another in a chain by covalent bonds between the sugar of one nucleotide and the phosphate of the next, resulting in an alternating sugar-phosphate backbone. The nitrogenous bases of the two separate polynucleotide strands are bound together, according to base pairing rules (A with T and C with G), with hydrogen bonds to make double-stranded DNA.