http://purl.uniprot.org/citations/21378166 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/21378166 | http://www.w3.org/2000/01/rdf-schema#comment | "Actin is a key regulator of RNA polymerase (Pol) II-dependent transcription. Positive transcription elongation factor b (P-TEFb), a Cdk9/cyclin T1 heterodimer, has been reported to play a critical role in transcription elongation. However, the relationship between actin and P-TEFb is still not clear. In this study, actin was found to interact with Cdk9, a catalytic subunit of P-TEFb, in elongation complexes. Using immunofluorescence and immunoprecipitation assays, Cdk9 was found to bind to G-actin through the conserved Thr-186 in the T-loop. Overexpression and in vitro kinase assays showed that G-actin promotes P-TEFb-dependent phosphorylation of the Pol II C-terminal domain. An in vitro transcription experiment revealed that the interaction between G-actin and Cdk9 stimulated Pol II transcription elongation. ChIP and immobilized template assays indicated that actin recruited Cdk9 to a transcriptional template in vivo and in vitro. Using cytokine IL-6-inducible p21 gene expression system, we revealed that actin recruited Cdk9 to endogenous gene. Moreover, overexpression of actin and Cdk9 increased histone H3 acetylation and acetylized histone H3 binding to a transcriptional template through the interaction with histone acetyltransferase, p300. Taken together, our results suggested that actin participates in transcription elongation by recruiting Cdk9 for phosphorylation of the Pol II C-terminal domain, and the actin-Cdk9 interaction promotes chromatin remodeling."xsd:string |
http://purl.uniprot.org/citations/21378166 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.184374"xsd:string |
http://purl.uniprot.org/citations/21378166 | http://purl.uniprot.org/core/author | "Guo L."xsd:string |
http://purl.uniprot.org/citations/21378166 | http://purl.uniprot.org/core/author | "Tang W."xsd:string |
http://purl.uniprot.org/citations/21378166 | http://purl.uniprot.org/core/author | "Qi T."xsd:string |
http://purl.uniprot.org/citations/21378166 | http://purl.uniprot.org/core/author | "Wang L."xsd:string |
http://purl.uniprot.org/citations/21378166 | http://purl.uniprot.org/core/author | "Zeng X."xsd:string |
http://purl.uniprot.org/citations/21378166 | http://purl.uniprot.org/core/author | "Zhai L."xsd:string |
http://purl.uniprot.org/citations/21378166 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
http://purl.uniprot.org/citations/21378166 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/21378166 | http://purl.uniprot.org/core/pages | "15171-15181"xsd:string |
http://purl.uniprot.org/citations/21378166 | http://purl.uniprot.org/core/title | "G-actin participates in RNA polymerase II-dependent transcription elongation by recruiting positive transcription elongation factor b (P-TEFb)."xsd:string |
http://purl.uniprot.org/citations/21378166 | http://purl.uniprot.org/core/volume | "286"xsd:string |
http://purl.uniprot.org/citations/21378166 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21378166 |
http://purl.uniprot.org/citations/21378166 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/21378166 |
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http://purl.uniprot.org/uniprot/#_Q562L9-mappedCitation-21378166 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21378166 |
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http://purl.uniprot.org/uniprot/#_Q562M5-mappedCitation-21378166 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21378166 |