期刊
CELL REPORTS
卷 4, 期 3, 页码 601-608出版社
CELL PRESS
DOI: 10.1016/j.celrep.2013.07.014
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资金
- European Research Council [293438]
- National Cancer Institute [R37 CA40099]
- Dr. Miriam and Sheldon G. Adelson Medical Research Foundation
- Edmond J. Safra Foundation
- Lower Saxony-Israeli Association
- Max Planck Society
- Mina and James Heinemann Foundation
- Adams Fellowship Program of the Israel Academy of Sciences and Humanities
- MSc/PhD program Molecular Biology International Max Planck Research School at the Georg August University, Gottingen
- NATIONAL CANCER INSTITUTE [R37CA040099] Funding Source: NIH RePORTER
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.
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