| pubmed-article:2247066 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2247066 | lifeskim:mentions | umls-concept:C0212694 | lld:lifeskim |
| pubmed-article:2247066 | lifeskim:mentions | umls-concept:C0018873 | lld:lifeskim |
| pubmed-article:2247066 | lifeskim:mentions | umls-concept:C0007610 | lld:lifeskim |
| pubmed-article:2247066 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:2247066 | pubmed:dateCreated | 1991-1-8 | lld:pubmed |
| pubmed-article:2247066 | pubmed:abstractText | A DNA-activated protein kinase (DNA-PK) was purified from nuclei of HeLa cells. Activity was associated with a single high-molecular-mass (approximately-300,000 Da) polypeptide when analyzed by gel filtration, denaturing polyacrylamide gel electrophoresis, and Western immunoblotting using a monoclonal antibody that also inhibits enzyme activity. Nuclear localization was indicated by subcellular fractionation and confirmed by immunofluorescence on whole cells. Double-stranded DNA stimulated phosphorylation of the 300-kDa polypeptide in purified preparations as well as phosphorylation of the exogenous substrates alpha-casein, simian virus 40 large T antigen, and the human heat shock protein hsp90. Autophosphorylation led to inactivation of the enzyme. The phosphorylation of casein was stimulated over 30-fold by DNA and was specific for serine and threonine residues. Bovine serum albumin and histone H1 were poor substrates for DNA-PK, and no phosphorylation of immunoglobulin G or histones other than H1 was observed. Supercoiled or heat-denatured DNA and synthetic double-stranded RNA or RNA-DNA copolymers did not stimulate casein phosphorylation by DNA-PK. Interaction of the enzyme with DNA in the absence of exogenous substrates was demonstrated by thermal inactivation and gel mobility shifts. These characteristics identify DNA-PK as distinct from other protein kinases described in the literature and suggest that activation by DNA is an important feature of the enzyme's in vivo function. | lld:pubmed |
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| pubmed-article:2247066 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2247066 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2247066 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2247066 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2247066 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:2247066 | pubmed:author | pubmed-author:SueFF | lld:pubmed |
| pubmed-article:2247066 | pubmed:author | pubmed-author:CarterTT | lld:pubmed |
| pubmed-article:2247066 | pubmed:author | pubmed-author:LouWW | lld:pubmed |
| pubmed-article:2247066 | pubmed:author | pubmed-author:VancurováII | lld:pubmed |
| pubmed-article:2247066 | pubmed:author | pubmed-author:DeLeonSS | lld:pubmed |
| pubmed-article:2247066 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2247066 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:2247066 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2247066 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2247066 | pubmed:pagination | 6460-71 | lld:pubmed |
| pubmed-article:2247066 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:2247066 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2247066 | pubmed:articleTitle | A DNA-activated protein kinase from HeLa cell nuclei. | lld:pubmed |
| pubmed-article:2247066 | pubmed:affiliation | Department of Biological Sciences, St. John's University, Jamaica, New York 11439. | lld:pubmed |
| pubmed-article:2247066 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2247066 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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