Global jumping and domain-specific intersegment transfer between DNA cognate sites of the multidomain transcription factor Oct-1.

ABSTRACT: At high DNA concentration, as found in the nucleus, DNA-binding proteins search for specific binding sites by hopping between separate DNA strands. Here, we use (15)N(z)-exchange transverse relaxation optimized NMR spectroscopy to characterize the mechanistic details of intermolecular hopping for the multidomain transcription factor, human Oct-1. Oct-1 is a member of the POU family of transcription factors and contains two helix-turn-helix DNA-binding domains, POU(HD) and POU(S), connected by a relatively short flexible linker. The two domains were found to exchange between specific sites at significantly different rates. The cotranscription factor, Sox2, decreases the exchange rate and equilibrium dissociation constant for Oct-1 > or = 5-fold and approximately 20-fold, respectively, by sl

SUBMITTER: Doucleff M 

PROVIDER: S-EPMC2544546 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature