| Literature DB >> 19575011 |
Judith Pirngruber1, Andrei Shchebet, Lisa Schreiber, Efrat Shema, Neri Minsky, Rob D Chapman, Dirk Eick, Yael Aylon, Moshe Oren, Steven A Johnsen.
Abstract
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.Entities:
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Year: 2009 PMID： 19575011 PMCID： PMC2726677 DOI： 10.1038/embor.2009.108
Source DB: PubMed Journal: EMBO Rep ISSN： 1469-221X Impact factor: 8.807