The BAH domain of Rsc2 is a histone H3 binding domain

Anna L Chambers, Laurence H Pearl, Antony W Oliver, Jessica A Downs

Research output: Contribution to journalArticle (Academic Journal)

14 Citations (Scopus)

Abstract

Bromo-adjacent homology (BAH) domains are commonly found in chromatin-associated proteins and fall into two classes; Remodels the Structure of Chromatin (RSC)-like or Sir3-like. Although Sir3-like BAH domains bind nucleosomes, the binding partners of RSC-like BAH domains are currently unknown. The Rsc2 subunit of the RSC chromatin remodeling complex contains an RSC-like BAH domain and, like the Sir3-like BAH domains, we find Rsc2 BAH also interacts with nucleosomes. However, unlike Sir3-like BAH domains, we find that Rsc2 BAH can bind to recombinant purified H3 in vitro, suggesting that the mechanism of nucleosome binding is not conserved. To gain insight into the Rsc2 BAH domain, we determined its crystal structure at 2.4 Å resolution. We find that it differs substantially from Sir3-like BAH domains and lacks the motifs in these domains known to be critical for making contacts with histones. We then go on to identify a novel motif in Rsc2 BAH that is critical for efficient H3 binding in vitro and show that mutation of this motif results in defective Rsc2 function in vivo. Moreover, we find this interaction is conserved across Rsc2-related proteins. These data uncover a binding target of the Rsc2 family of BAH domains and identify a novel motif that mediates this interaction.

Original languageEnglish
Pages (from-to)9168-82
Number of pages15
JournalNucleic Acids Research
Volume41
Issue number19
DOIs
Publication statusPublished - Oct 2013

Keywords

  • Amino Acid Sequence
  • Chromatin
  • Chromosomal Proteins, Non-Histone
  • DNA, Ribosomal
  • Gene Silencing
  • Histones
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Protein Interaction Domains and Motifs
  • Saccharomyces cerevisiae Proteins

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