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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
26
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pubmed:dateCreated |
1995-2-2
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pubmed:abstractText |
The 32-kDa subunit of replication protein A (RPA) is phosphorylated during the S phase of the cell cycle in vivo and during simian virus 40 DNA replication in vitro. To explore the functional significance of this modification, we purified a HeLa cell protein kinase that phosphorylates RPA in the presence of single-stranded DNA. By several criteria we identified the purified enzyme as a form of the DNA-activated protein kinase (DNA-PK), a previously described high molecular weight protein kinase that is capable of phosphorylating a number of nuclear DNA binding proteins. Phosphorylation of RPA by DNA-PK is stimulated by natural single-stranded DNAs but not by homopolymers lacking secondary structure. Studies with the simian virus 40 model system indicate that DNA-PK is required for DNA-replication-dependent RPA phosphorylation. Depletion of the kinase activity, however, has no effect on the extent of DNA replication in vitro. Our data support a model in which phosphorylation of RPA by DNA-PK is activated by formation of replication intermediates containing single- and double-stranded regions. This event may be involved in a signaling mechanism that coordinates DNA replication with the cell cycle.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-1318194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-1318195,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-1324186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-1406679,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-1465419,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-1976634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2050703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2159011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2200738,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2211668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2247066,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2247067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2406247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2457111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2536723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2557059,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2562399,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2833742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2841119,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2983081,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-2993858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-3031654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-3035543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-8187764,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-8206988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-8246944,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-8291090,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-8308077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-8397207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-8422676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7809070-8486698
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0027-8424
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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 |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12520-4
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7809070-DNA Repair,
pubmed-meshheading:7809070-DNA Replication,
pubmed-meshheading:7809070-DNA-Activated Protein Kinase,
pubmed-meshheading:7809070-DNA-Binding Proteins,
pubmed-meshheading:7809070-HeLa Cells,
pubmed-meshheading:7809070-Humans,
pubmed-meshheading:7809070-Nuclear Proteins,
pubmed-meshheading:7809070-Phosphorylation,
pubmed-meshheading:7809070-Protein-Serine-Threonine Kinases,
pubmed-meshheading:7809070-Replication Protein A,
pubmed-meshheading:7809070-S Phase,
pubmed-meshheading:7809070-Simian virus 40,
pubmed-meshheading:7809070-Virus Replication
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pubmed:year |
1994
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pubmed:articleTitle |
The DNA-activated protein kinase is required for the phosphorylation of replication protein A during simian virus 40 DNA replication.
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pubmed:affiliation |
Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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