Cooperative DNA-protein interactions. Effects of changing the spacing between adjacent binding sites.

Abstract:

:Cooperative binding of specific DNA-binding proteins plays crucial roles in gene regulatory circuitry, and is a model system for interactions between proteins bound to DNA. We have studied coliphage HK022 repressor, which binds to two adjacent operators with a cooperativity parameter of approximately 2000. We examined the effect of changing the spacing between these two operators on cooperativity and on the conformation of the complex. Maximum cooperativity was seen with the wild-type spacing; considerable cooperativity was retained for most spacing variants, but was abolished when the operators lay on opposite faces of the DNA helix. Most spacing variants conferred changes in the conformation of the DNA-protein complex. Our data indicate that the pairwise cooperativity observed with the wild-type spacing results from a conformation that prevents protein-protein contacts with flanking bound dimers. We conclude that protein-DNA complexes involving the same specific binding sites and the same protein molecules can adopt many different conformations, depending on the spacing between the binding sites. This conclusion may be broadly applicable to protein-DNA interactions in other systems.

journal_name

J Mol Biol

authors

Mao C,Carlson NG,Little JW

doi

10.1006/jmbi.1994.1011

subject

Has Abstract

pub_date

1994-01-14 00:00:00

pages

532-44

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(84)71011-4

journal_volume

235

pub_type

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