By Mark Ptashne
The 1st variation of Mark Ptashne's 1986 ebook describing the foundations of gene legislation in phage lambda grew to become a vintage in either content material and shape, surroundings a customary of readability and designated prose that has infrequently been bettered. This variation is a reprint of the unique textual content, including a brand new bankruptcy updating the tale to 2004. one of the amazing new advancements are fresh findings on long-range interactions among proteins absolute to largely separated websites at the phage genome, and a close description of ways gene activation works.
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Additional info for A Genetic Switch: Phage Lambda Revisited
10. Cro bound to an operator site. A Cro dimer docks with DNA in much the same way as does a repressor dimer. 11. This is not surprising. In each case, one surface (the “inside”) of the helix fits against the body of the protein, and the “outside” surface fits into the DNA’s major groove to make specific contacts. The inside surfaces of the recognition helices differ because the bodies of the proteins with which they interact are different in repressor and Cro. The sequences along the outsides of the recognition helices are similar but not identical—although repressor and Cro bind to the same operator sites, they do so with different relative affinities.
N protein turns on the early genes to the left of N and to the right of cro. The pyramid representing N protein is shown hovering near the beginning of the leftward mRNA, but further downstream in the case of the rightward mRNA. This is explained in the text. How N works is not known in detail. We do know that it recognizes a specific sequence called Nut (for N utilization); as polymerase passes over this sequence it is evidently modified by N so that it ignores certain (but not all) further termination signals.
As the repressor binds the operator, its arms wrap around and make specific contacts on the backside of the DNA in the major groove. 8 may be an example of a less widely used sequence-reading device. 9 shows Cro’s structure. It includes three α-helices and, in addition, three regions that form so-called λ-sheets. (The λ-sheet is a second common structural motif found in many proteins. 9. Cro. The three flattened arrows represent the segments of a λ-sheet that, in addition to its three α-helices, form Cro’s structure.