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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
1992-8-28
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pubmed:abstractText |
Mammalian DNA ligase I has been shown to be a phosphoprotein. Dephosphorylation of purified DNA ligase I causes inactivation, an effect dependent on the presence of the N-terminal region of the protein. Expression of full-length human DNA ligase I in Escherichia coli yielded soluble but catalytically inactive enzyme whereas an N-terminally truncated form expressed activity. Incubation of the full-length preparation from E. coli with purified casein kinase II (CKII) resulted in phosphorylation of the N-terminal region and was accompanied by activation of the DNA ligase. Of a variety of purified protein kinases tested, only CKII stimulated the activity of calf thymus DNA ligase I. Tryptic phosphopeptide analysis of DNA ligase I revealed that CKII specifically phosphorylated a major peptide also apparently phosphorylated in cells, implying that CKII is a protein kinase acting on DNA ligase I in the cell nucleus. These data suggest that DNA ligase I is negatively regulated by its N-terminal region and that this inhibition can be relieved by post-translational modification.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-1264233,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-13567776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-1547771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-1581963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-1659651,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-1694965,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-1695631,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-1730748,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-1740119,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-1902230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-1939197,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-1943760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-1956768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-1988940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2017356,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2154252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2157164,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2169868,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2196445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2197279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2204063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2204827,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2238044,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2383569,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2471642,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2531073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2584181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2842338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-2987912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-3076090,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-378985,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-4346342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-6191328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-6447694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1639065-6802840
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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 |
Aug
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2925-33
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1639065-Amino Acids,
pubmed-meshheading:1639065-Animals,
pubmed-meshheading:1639065-Binding Sites,
pubmed-meshheading:1639065-Casein Kinase II,
pubmed-meshheading:1639065-Cattle,
pubmed-meshheading:1639065-Cell Line,
pubmed-meshheading:1639065-Cloning, Molecular,
pubmed-meshheading:1639065-DNA Ligases,
pubmed-meshheading:1639065-Enzyme Activation,
pubmed-meshheading:1639065-Escherichia coli,
pubmed-meshheading:1639065-Humans,
pubmed-meshheading:1639065-Models, Structural,
pubmed-meshheading:1639065-Muscles,
pubmed-meshheading:1639065-Phosphopeptides,
pubmed-meshheading:1639065-Phosphorylation,
pubmed-meshheading:1639065-Protein-Serine-Threonine Kinases,
pubmed-meshheading:1639065-Rabbits,
pubmed-meshheading:1639065-Recombinant Proteins,
pubmed-meshheading:1639065-Thymus Gland
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pubmed:year |
1992
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pubmed:articleTitle |
Activation of mammalian DNA ligase I through phosphorylation by casein kinase II.
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pubmed:affiliation |
Imperial Cancer Research Fund, Clare Hall Laboratories, South Mimms, Herts, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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