Location of Repository

Cold denaturation of a repressor-operator complex: the role of entropy in protein-DNA recognition.

By D Foguel and J L Silva

Abstract

The mechanisms by which regulatory proteins recognize specific DNA sequences are not fully understood. Here we examine the basis for the stability of a protein-DNA complex, using hydrostatic pressure and low temperature. Pressure converts the DNA-binding Arc repressor protein from a native state to a denatured, molten-globule state. Our data show that the folding and dimerization of Arc repressor in the temperature range 0-20 degrees C are favored by a large positive entropy value, so that the reaction proceeds in spite of an unfavorable positive enthalpy. On binding operator DNA, Arc repressor becomes extremely stable against denaturation. However, the Arc repressor-operator DNA complex is cold-denatured at subzero temperatures under pressure, demonstrating that the favorable entropy increases greatly when Arc repressor binds tightly to its operator sequence but not a nonspecific sequence. We show how an increase in entropy may operate to provide the protein with a mechanism to distinguish between a specific and a nonspecific DNA sequence. It is postulated that the formation of the Arc-operator DNA complex is followed by an increase in apolar interactions and release of solvent which would explain its entropy-driven character, whereas this solvent would not be displaced in nonspecific complexes

Topics: Research Article
Year: 1994
OAI identifier: oai:pubmedcentral.nih.gov:44582
Provided by: PubMed Central
Sorry, our data provider has not provided any external links therefor we are unable to provide a PDF.

Suggested articles


To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.