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CDK9 directs H2B monoubiquitination and controls replication-dependent histone mRNA 3'-end processing.
EMBO Rep. 10, 894-900 (2009)
Post-translational histone modifications have essential roles in controlling nuclear processes; however, the specific mechanisms regulating these modifications and their combinatorial activities remain elusive. Cyclin-dependent kinase 9 (CDK9) regulates gene expression by phosphorylating transcriptional regulatory proteins, including the RNA polymerase II carboxy-terminal domain. Here, we show that CDK9 activity is essential for maintaining global and gene-associated levels of histone H2B monoubiquitination (H2Bub1). Furthermore, CDK9 activity and H2Bub1 help to maintain correct replication-dependent histone messenger RNA (mRNA) 3'-end processing. CDK9 knockdown consistently resulted in inefficient recognition of the correct mRNA 3'-end cleavage site and led to increased read-through of RNA polymerase II to an alternative downstream polyadenylation signal. Thus, CDK9 acts to integrate phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
cyclin-dependent kinase; histone; mRNA processing; monoubiquitination; RNA polymerase II C-terminal domain; gene-expression; polymerase-ii; breast-cancer; transcription; chromatin; carcinomas
ISSN (print) / ISBN
1469-221X
e-ISSN
1469-3178
Journal
EMBO Reports
Quellenangaben
Volume: 10,
Issue: 8,
Pages: 894-900
Publisher
EMBO Press
Reviewing status
Peer reviewed