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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0001483,
umls-concept:C0017428,
umls-concept:C0032136,
umls-concept:C0033684,
umls-concept:C0205088,
umls-concept:C0332256,
umls-concept:C0598312,
umls-concept:C0678713,
umls-concept:C1167395,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1880022,
umls-concept:C1998793
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pubmed:issue |
12
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pubmed:dateCreated |
1984-7-30
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pubmed:abstractText |
A host protein, which is required for the replication of a plasmid DNA (pLA1), has been purified from extracts of uninfected HeLa nuclei. This plasmid DNA contains the origin of adenovirus DNA replication but lacks the 55,000-dalton terminal proteins. The purified host protein has been designated factor pL. Factor pL is essential for the initiation of DNA replication of EcoRI-digested pLA1 DNA, which proceeds via the formation of a covalent complex between the 80,000-dalton adenovirus coded preterminal protein and 5' dCMP. Factor pL has been purified approximately 120-fold to greater than 75% homogeneity. It is a heat labile and N-ethylmaleimide-sensitive protein with a native Mr = 39,000 (+/- 2,000). Initiation of DNA replication using EcoRI-digested pLA1 DNA as the template requires the 80,000-dalton preterminal protein and the 140,000-dalton adenovirus DNA polymerase, in addition to factor pL, and is stimulated as much as 10-fold by nuclear factor I ( Nagata , K., Guggenheimer , R. A., Enomoto , T., Lichy , J. H., and Hurwitz , J. (1982) Proc. Natl. Acad. Sci. U. S. A. 79, 6438-6442). Factor pL has no effect on in vitro DNA replication when adenovirus DNA covalently linked to the 55,000-dalton terminal protein is used as the template, however the replication of adenovirus DNA treated with Pronase, becomes totally dependent upon the addition of factor pL.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Restriction Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease EcoRI,
http://linkedlifedata.com/resource/pubmed/chemical/Pronase,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
259
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7815-25
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6330083-Adenoviridae,
pubmed-meshheading:6330083-DNA, Viral,
pubmed-meshheading:6330083-DNA Replication,
pubmed-meshheading:6330083-DNA Restriction Enzymes,
pubmed-meshheading:6330083-Deoxyribonuclease EcoRI,
pubmed-meshheading:6330083-Models, Genetic,
pubmed-meshheading:6330083-Molecular Weight,
pubmed-meshheading:6330083-Plasmids,
pubmed-meshheading:6330083-Pronase,
pubmed-meshheading:6330083-Proteins,
pubmed-meshheading:6330083-Templates, Genetic
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pubmed:year |
1984
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pubmed:articleTitle |
Protein-primed replication of plasmids containing the terminus of the adenovirus genome. II. Purification and characterization of a host protein required for the replication of DNA templates devoid of the terminal protein.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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