Abstract:
: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.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Bonizec M,Hérissant L,Pokrzywa W,Geng F,Wenzel S,Howard GC,Rodriguez P,Krause S,Tansey WP,Hoppe T,Dargemont Cdoi
10.1093/nar/gku786subject
Has Abstractpub_date
2014-01-01 00:00:00pages
10975-86issue
17eissn
0305-1048issn
1362-4962pii
gku786journal_volume
42pub_type
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