Source:http://linkedlifedata.com/resource/pubmed/id/12953058
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 19
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pubmed:dateCreated |
2003-9-3
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pubmed:abstractText |
The sequential binding of the origin recognition complex (ORC), Cdc6p and the minichromosome maintenance proteins (MCM2-7) mediates replication competence at eukaryotic origins of DNA replication. The latent origin of Epstein-Barr virus, oriP, is a viral origin known to recruit ORC. OriP also binds EBNA1, a virally encoded protein that lacks any activity predicted to be required for replication initiation. Here, we used chromatin immunoprecipitation and chromatin binding to compare the cell-cycle-dependent binding of pre-RC components and EBNA1 to oriP and to global cellular chromatin. Prereplicative-complex components such as the Mcm2p-Mcm7p proteins and HsOrc1p are regulated in a cell-cycle-dependent fashion, whereas other HsOrc subunits and EBNA1 remain constantly bound. In addition, HsOrc1p becomes sensitive to the 26S proteasome after release from DNA during S phase. These results show that the complex protein-DNA dynamics at the viral oriP are synchronized with the cell division cycle. Chromatin-binding and chromatin-immunoprecipitation experiments on G0 arrested cells indicated that the ORC core complex (ORC2-5) and EBNA1 remain bound to chromatin and oriP. HsOrc6p and the MCM2-7 complex are released in resting cells. HsOrc1p is partly liberated from chromatin. Our data suggest that origins remain marked in resting cells by the ORC core complex to ensure a rapid and regulated reentry into the cell cycle. These findings indicate that HsOrc is a dynamic complex and that its DNA binding activity is regulated differently in the various stages of the cell cycle.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/EBV-encoded nuclear antigen 1,
http://linkedlifedata.com/resource/pubmed/chemical/Epstein-Barr Virus Nuclear Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/ORC2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Origin Recognition Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9533
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
116
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3971-84
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pubmed:dateRevised |
2011-10-28
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pubmed:meshHeading |
pubmed-meshheading:12953058-Animals,
pubmed-meshheading:12953058-Cell Cycle,
pubmed-meshheading:12953058-Cells, Cultured,
pubmed-meshheading:12953058-Chromatin,
pubmed-meshheading:12953058-DNA-Binding Proteins,
pubmed-meshheading:12953058-Epstein-Barr Virus Nuclear Antigens,
pubmed-meshheading:12953058-Flow Cytometry,
pubmed-meshheading:12953058-G0 Phase,
pubmed-meshheading:12953058-Herpesvirus 4, Human,
pubmed-meshheading:12953058-Humans,
pubmed-meshheading:12953058-Origin Recognition Complex,
pubmed-meshheading:12953058-Plasmids,
pubmed-meshheading:12953058-Protein Binding,
pubmed-meshheading:12953058-S Phase,
pubmed-meshheading:12953058-Viral Proteins,
pubmed-meshheading:12953058-Virus Replication
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pubmed:year |
2003
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pubmed:articleTitle |
Complex protein-DNA dynamics at the latent origin of DNA replication of Epstein-Barr virus.
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pubmed:affiliation |
Department of Gene Vectors, GSF-National Research Center for Environment and Health, Marchioninistrasse 25, 81377 München, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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