CDK9 directs H2B monoubiquitination and controls replication-dependent histone mRNA 3′-end processing

Judith Pirngruber, Andrei Shchebet, Lisa Schreiber, Efrat Shema, Neri Minsky, Rob D. Chapman, Dirk Eick, Yael Aylon, Moshe Oren, Steven A. Johnsen

Research output: Contribution to journalArticlepeer-review

121 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)894-900
Number of pages7
JournalEMBO Reports
Issue number8
StatePublished - 2009

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics


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