期刊
NUCLEIC ACIDS RESEARCH
卷 42, 期 17, 页码 10975-10986出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gku786
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资金
- French National Research Agency [2010 BLAN1227-01]
- Who am I? laboratory of excellence - 'Investments for the Future' program [ANR-11-LABX-0071, ANR-11-IDEX-0005-01]
- Ligue Nationale contre le Cancer. Deutsche Forschungsgemeinschaft [CECAD] [FOR885, SFB635, KFO286, DIP8, 2014376]
- Centre National pour la Recherche Scientifique
- Association pour la Recherche Contre le Cancer
- National Institute of General Medical Sciences [GM067728]
- Vanderbilt Ingram Cancer Center Support [P30CA68485]
- Ligue Nationale contre le Cancer
Cdc48/p97 is an evolutionary conserved ubiquitin-dependent chaperone involved in a broad array of cellular functions due to its ability to associate with multiple cofactors. Aside from its role in removing RNA polymerase II from chromatin after DNA damage, little is known about how this AAA-ATPase is involved in the transcriptional process. Here, we show that yeast Cdc48 is recruited to chromatin in a transcription-coupled manner and modulates gene expression. Cdc48, together with its cofactor Ubx3 controls monoubiquitylation of histone H2B, a conserved modification regulating nucleosome dynamics and chromatin organization. Mechanistically, Cdc48 facilitates the recruitment of Lge1, a cofactor of the H2B ubiquitin ligase Bre1. The function of Cdc48 in controlling H2B ubiquitylation appears conserved in human cells because disease-related mutations or chemical inhibition of p97 function affected the amount of ubiquitylated H2B in muscle cells. Together, these results suggest a prominent role of Cdc48/p97 in the coordination of chromatin remodeling with gene transcription to define cellular differentiation processes.
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