Systematic identification of proteins binding to chromatin-embedded ubiquitylated H2B reveals recruitment of SWI/SNF to regulate transcription

Efrat Shema-Yaacoby, Miroslav Nikolov, Mahmood Haj-Yahya, Peter Siman, Eric Allemand, Yuki Yamaguchi, Christian Muchardt, Henning Urlaub, Ashraf Brik, Moshe Oren*, Wolfgang Fischle

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

53 Scopus citations

Abstract

Chromatin posttranslational modifications (PTMs), including monoubiquitylation of histone H2B on lysine 120 (H2Bub1), play a major role in regulating genome functions. To elucidate the molecular mechanisms of H2Bub1 activity, a chromatin template uniformly containing H2Bub1 was used as an affinity matrix to identify preferentially interacting human proteins. Over 90 such factors were found, including proteins and protein complexes associated with transcription, RNA posttranscriptional modifications, and DNA replication and repair. Notably, we found that the SWI/SNF chromatin remodeling complex associates preferentially with H2Bub1-rich chromatin. Moreover,SWI/SNF is required for optimal transcription of a subset of genes that are selectively dependent on H2Bub1. Our findings substantially expand the known H2Bub1 interactome and provide insights into the functions of this PTM in mammalian gene regulation

Original languageEnglish (US)
Pages (from-to)601-608
Number of pages8
JournalCell Reports
Volume4
Issue number3
DOIs
StatePublished - Aug 9 2013

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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