Diversification of transcription factor paralogs via noncanonical modularity in C2H2 zinc finger DNA binding.

ABSTRACT: A major challenge in obtaining a full molecular description of evolutionary adaptation is to characterize how transcription factor (TF) DNA-binding specificity can change. To identify mechanisms of TF diversification, we performed detailed comparisons of yeast C2H2 ZF proteins with identical canonical recognition residues that are expected to bind the same DNA sequences. Unexpectedly, we found that ZF proteins can adapt to recognize new binding sites in a modular fashion whereby binding to common core sites remains unaffected. We identified two distinct mechanisms, conserved across multiple Ascomycota species, by which this molecular adaptation occurred. Our results suggest a route for TF evolution that alleviates negative pleiotropic effects by modularly gaining new binding sites. These f

SUBMITTER: Siggers T 

PROVIDER: S-EPMC4142112 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature