Physical limits on cooperative protein-DNA binding and the kinetics of combinatorial transcription regulation.

ABSTRACT: Much of the complexity observed in gene regulation originates from cooperative protein-DNA binding. Although studies of the target search of proteins for their specific binding sites on the DNA have revealed design principles for the quantitative characteristics of protein-DNA interactions, no such principles are known for the cooperative interactions between DNA-binding proteins. We consider a simple theoretical model for two interacting transcription factor (TF) species, searching for and binding to two adjacent target sites hidden in the genomic background. We study the kinetic competition of a dimer search pathway and a monomer search pathway, as well as the steady-state regulation function mediated by the two TFs over a broad range of TF-TF interaction strengths. Using a transcription

SUBMITTER: Geisel N 

PROVIDER: S-EPMC3183818 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature