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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2002-1-21
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pubmed:abstractText |
Although the PITSLRE protein kinases are members of the cyclin-dependent kinase superfamily, their cellular function is unclear. Previously we demonstrated that the general RNA splicing factor RNPS1 is a specific PITSLRE p110 kinase interactor in vivo. This suggests that the PITSLRE family of protein kinases is involved in some aspect of RNA processing or transcription. Here we identify multiple transcriptional elongation factors, including ELL2, TFIIF(1), TFIIS, and FACT, as PITSLRE kinase-associated proteins. We demonstrate that PITSLRE p110 protein kinases co-immunoprecipitate and/or co-purify with these elongation factors as well as with RNA polymerase II. Antibody-mediated inhibition of PITSLRE kinase specifically suppressed RNA polymerase II-dependent in vitro transcription initiated at a GC-rich (adenosine deaminase) or TATA box-dependent (Ad2ML) promoter, and this suppression was rescued by readdition of purified PITSLRE p110 kinase. Together, these data strongly suggest that PITSLRE protein kinases participate in a signaling pathway that potentially regulates or links transcription and RNA processing events.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CDK11a protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GAL4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/High Mobility Group Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase I,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SSRP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, General,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, TFII,
http://linkedlifedata.com/resource/pubmed/chemical/Transcriptional Elongation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/transcription factor S-II,
http://linkedlifedata.com/resource/pubmed/chemical/transcription factor TFIIF
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2589-96
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pubmed:dateRevised |
2011-10-10
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pubmed:meshHeading |
pubmed-meshheading:11709559-Animals,
pubmed-meshheading:11709559-Cyclin-Dependent Kinases,
pubmed-meshheading:11709559-DNA-Binding Proteins,
pubmed-meshheading:11709559-Dose-Response Relationship, Drug,
pubmed-meshheading:11709559-Fungal Proteins,
pubmed-meshheading:11709559-Glutathione Transferase,
pubmed-meshheading:11709559-High Mobility Group Proteins,
pubmed-meshheading:11709559-Humans,
pubmed-meshheading:11709559-Jurkat Cells,
pubmed-meshheading:11709559-Mass Spectrometry,
pubmed-meshheading:11709559-Phosphorylation,
pubmed-meshheading:11709559-Phosphotransferases,
pubmed-meshheading:11709559-Precipitin Tests,
pubmed-meshheading:11709559-Protein Binding,
pubmed-meshheading:11709559-Protein Isoforms,
pubmed-meshheading:11709559-Protein Kinases,
pubmed-meshheading:11709559-Protein Structure, Tertiary,
pubmed-meshheading:11709559-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11709559-RNA,
pubmed-meshheading:11709559-RNA, Messenger,
pubmed-meshheading:11709559-RNA Polymerase I,
pubmed-meshheading:11709559-Recombinant Proteins,
pubmed-meshheading:11709559-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11709559-Transcription, Genetic,
pubmed-meshheading:11709559-Transcription Factors,
pubmed-meshheading:11709559-Transcription Factors, General,
pubmed-meshheading:11709559-Transcription Factors, TFII,
pubmed-meshheading:11709559-Transcriptional Elongation Factors,
pubmed-meshheading:11709559-Transfection,
pubmed-meshheading:11709559-Two-Hybrid System Techniques
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pubmed:year |
2002
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pubmed:articleTitle |
PITSLRE p110 protein kinases associate with transcription complexes and affect their activity.
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pubmed:affiliation |
Department of Tumor Cell Biology and the Hartwell Center for Bioinformatics and Biotechnology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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