Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2009-8-3
pubmed:abstractText
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.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-11157774, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-15034139, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-15632065, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-15762987, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-16307923, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-16337599, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-16510875, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-17079134, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-17088385, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-17406230, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-17499042, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-17522673, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-18042462, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-18079404, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-18344985, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-18374642, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-18457900, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-18832071, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-18927579, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-19013272, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-19117995, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-2163669, http://linkedlifedata.com/resource/pubmed/commentcorrection/19575011-2576416
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 9, http://linkedlifedata.com/resource/pubmed/chemical/Dactinomycin, http://linkedlifedata.com/resource/pubmed/chemical/Dichlororibofuranosylbenzimidazole, http://linkedlifedata.com/resource/pubmed/chemical/Flavonoids, http://linkedlifedata.com/resource/pubmed/chemical/Histones, http://linkedlifedata.com/resource/pubmed/chemical/Nucleic Acid Synthesis Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Piperidines, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RNF20 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/RNF40 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases, http://linkedlifedata.com/resource/pubmed/chemical/flavopiridol
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1469-3178
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
894-900
pubmed:dateRevised
2010-9-27
pubmed:meshHeading
pubmed-meshheading:19575011-Animals, pubmed-meshheading:19575011-Blotting, Western, pubmed-meshheading:19575011-Cell Line, pubmed-meshheading:19575011-Cell Line, Tumor, pubmed-meshheading:19575011-Chromatin Immunoprecipitation, pubmed-meshheading:19575011-Cyclin-Dependent Kinase 9, pubmed-meshheading:19575011-Dactinomycin, pubmed-meshheading:19575011-Dichlororibofuranosylbenzimidazole, pubmed-meshheading:19575011-Flavonoids, pubmed-meshheading:19575011-Histones, pubmed-meshheading:19575011-Humans, pubmed-meshheading:19575011-Mice, pubmed-meshheading:19575011-Nucleic Acid Synthesis Inhibitors, pubmed-meshheading:19575011-Piperidines, pubmed-meshheading:19575011-RNA, Messenger, pubmed-meshheading:19575011-Transcription, Genetic, pubmed-meshheading:19575011-Ubiquitin-Protein Ligases, pubmed-meshheading:19575011-Ubiquitination
pubmed:year
2009
pubmed:articleTitle
CDK9 directs H2B monoubiquitination and controls replication-dependent histone mRNA 3'-end processing.
pubmed:affiliation
Department of Molecular Oncology, Göttingen Center for Molecular Biosciences, University of Göttingen, Göttingen, Germany.
pubmed:publicationType
Journal Article