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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
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pubmed:dateCreated |
1992-8-14
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pubmed:abstractText |
An initial step in the replication of simian virus (SV40) DNA is the ATP-dependent formation of a double hexamer of the SV40 large tumor (T) antigen at the SV40 DNA replication origin. In the absence of DNA, T antigen assembled into hexamers in the presence of magnesium and ATP. Hexameric T antigen was stable and could be isolated by glycerol gradient centrifugation. The ATPase activities of hexameric and monomeric T antigen isolated from parallel glycerol gradients were identical. However, while monomeric T antigen was active in the ATP-dependent binding, untwisting, unwinding, and replication of SV40 origin-containing DNA, hexameric T antigen was inactive in these reactions. Isolated hexamers incubated at 37 degrees C in the presence of ATP remained intact, but dissociated into monomers when incubated at 37 degrees C in the absence of ATP. This dissociation restored the activity of these preparations in the DNA replication reaction, indicating that hexameric T antigen is not permanently inactivated but merely assembled into a nonproductive structure. We propose that the two hexamers of T antigen at the SV40 origin assemble around the DNA from monomer T antigen in solution. This complex untwists the DNA at the origin, melting specific DNA sequences. The resulting single-stranded regions may be utilized by the T antigen helicase activity to initiate DNA unwinding bidirectionally from the origin.
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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/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Polyomavirus Transforming,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14129-37
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1321135-Adenosine Triphosphate,
pubmed-meshheading:1321135-Animals,
pubmed-meshheading:1321135-Antigens, Polyomavirus Transforming,
pubmed-meshheading:1321135-Baculoviridae,
pubmed-meshheading:1321135-DNA, Viral,
pubmed-meshheading:1321135-DNA Replication,
pubmed-meshheading:1321135-Insects,
pubmed-meshheading:1321135-Kinetics,
pubmed-meshheading:1321135-Macromolecular Substances,
pubmed-meshheading:1321135-Microscopy, Electron,
pubmed-meshheading:1321135-Models, Genetic,
pubmed-meshheading:1321135-Protein Binding,
pubmed-meshheading:1321135-Recombinant Proteins,
pubmed-meshheading:1321135-Simian virus 40,
pubmed-meshheading:1321135-Transfection
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pubmed:year |
1992
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pubmed:articleTitle |
The simian virus 40 T antigen double hexamer assembles around the DNA at the replication origin.
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pubmed:affiliation |
Program in Molecular Biology, Sloan-Kettering Cancer Center, New York, New York 10021.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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