TY - JOUR
T1 - Recognition of a DNA operator by the repressor of phage 434
T2 - A view at high resolution
AU - Aggarwal, Aneel K.
AU - Rodgers, David W.
AU - Drottar, Marie
AU - Ptashne, Mark
AU - Harrison, Stephen C.
PY - 1988
Y1 - 1988
N2 - The repressors of temperate bacteriophages such as 434 and lambda control transcription by binding to a set of DNA operator sites. The different affinity of repressor for each of these sites ensures efficient regulation. High-resolution x-ray crystallography was used to study the DNA-binding domain of phage 434 repressor in complex with a synthetic DNA operator. The structure shows recognition of the operator by direct interactions with base pairs in the ma or groove, combined with the sequence-dependent ability of DNA to adopt the required conformation on binding repressor. In particular, a network of three-centered bifurcated hydrogen bonds among base pairs in the operator helps explain why 434 repressor prefers certain sites over others. These bonds, which stabilize the conformation of the bound DNA, can form only with certain sequences.
AB - The repressors of temperate bacteriophages such as 434 and lambda control transcription by binding to a set of DNA operator sites. The different affinity of repressor for each of these sites ensures efficient regulation. High-resolution x-ray crystallography was used to study the DNA-binding domain of phage 434 repressor in complex with a synthetic DNA operator. The structure shows recognition of the operator by direct interactions with base pairs in the ma or groove, combined with the sequence-dependent ability of DNA to adopt the required conformation on binding repressor. In particular, a network of three-centered bifurcated hydrogen bonds among base pairs in the operator helps explain why 434 repressor prefers certain sites over others. These bonds, which stabilize the conformation of the bound DNA, can form only with certain sequences.
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U2 - 10.1126/science.3187531
DO - 10.1126/science.3187531
M3 - Article
C2 - 3187531
AN - SCOPUS:0024284650
SN - 0036-8075
VL - 242
SP - 899
EP - 907
JO - Science
JF - Science
IS - 4880
ER -