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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1995-2-24
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pubmed:abstractText |
The DNA-dependent protein kinase (DNA-PK) phosphorylates RNA polymerase II and a number of transcription factors. We now show that the activity of DNA-PK is directly stimulated by certain transcriptional activator proteins, including the human heat shock transcription factor 1 (HSF1) and a transcriptionally active N-terminal 147 amino acid GAL4 derivative. Stimulation of DNA-PK activity required specific sequences in the activator proteins outside the minimal DNA binding domains. The stimulation of DNA-PK activity also required DNA and was greater with DNA containing relevant activator binding sites. Comparison of different HSF binding fragments showed that optimal stimulation occurred when two HSF binding sites were present. Stimulation with HSF and GAL4 was synergistic with Ku protein, another regulator of DNA-PK activity. DNA-PK is tightly associated with the transcriptional template, and an increase in its activity could potentially influence transcription through the phosphorylation of proteins associated with the transcription complex.
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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/Antigens, Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Activated Protein Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GAL4 (1-147) protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Ku autoantigen,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PRKDC protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase II,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/XRCC5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/heat shock transcription factor
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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 |
20
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1449-54
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7836414-Antigens, Nuclear,
pubmed-meshheading:7836414-DNA Helicases,
pubmed-meshheading:7836414-DNA-Activated Protein Kinase,
pubmed-meshheading:7836414-DNA-Binding Proteins,
pubmed-meshheading:7836414-Enzyme Activation,
pubmed-meshheading:7836414-HeLa Cells,
pubmed-meshheading:7836414-Humans,
pubmed-meshheading:7836414-Nuclear Proteins,
pubmed-meshheading:7836414-Protein-Serine-Threonine Kinases,
pubmed-meshheading:7836414-RNA Polymerase II,
pubmed-meshheading:7836414-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:7836414-Substrate Specificity,
pubmed-meshheading:7836414-Trans-Activators,
pubmed-meshheading:7836414-Transcription Factors
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pubmed:year |
1995
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pubmed:articleTitle |
Stimulation of the DNA-dependent protein kinase by RNA polymerase II transcriptional activator proteins.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.
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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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