Structural Characterization of the SMRT Corepressor Interacting with Histone Deacetylase 7.

ABSTRACT: The 2525 amino acid SMRT corepressor is an intrinsically disordered hub protein responsible for binding and coordinating the activities of multiple transcription factors and chromatin modifying enzymes. Here we have studied its interaction with HDAC7, a class IIa deacetylase that interacts with the corepressor complex together with the highly active class I deacetylase HDAC3. The binding site of class IIa deacetylases was previously mapped to an approximate 500 amino acid region of SMRT, with recent implication of short glycine-serine-isoleucine (GSI) containing motifs. In order to characterize the interaction in detail, we applied a random library screening approach within this region and obtained a range of stable, soluble SMRT fragments. In agreement with an absence of predicted structu

SUBMITTER: Desravines DC 

PROVIDER: S-EPMC5473869 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature