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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
51
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pubmed:dateCreated |
1997-1-23
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pubmed:abstractText |
We have previously shown that replication forks stall at a family of repeated sequences (FR) within the Epstein-Barr virus latent origin of replication oriP, both in a small plasmid and in the intact Epstein-Barr virus genome. Each of the 20 repeated sequences within the FR contains a binding site for Epstein-Barr nuclear antigen 1 (EBNA-1), the only viral protein required for latent replication. We showed that the EBNA-1 protein enhances the accumulation of paused replication forks at the FR. In this study, we have investigated a series of truncated EBNA-1 proteins to determine the portion of the EBNA-1 protein that is responsible for pausing of forks at the FR. Two-dimensional agarose gel electrophoresis was performed on the products of in vitro replication reactions in the presence of full-length EBNA-1 or proteins with various deletions to assess the extent of fork pausing at the FR. We conclude that a portion of the DNA binding domain is important for fork pausing. We also present evidence indicating that phosphorylation of the EBNA-1 protein or EBNA-1-truncated derivatives is not essential for pausing. To investigate the mechanism of EBNA-1-mediated pausing of replication forks, we asked whether EBNA-1 could inhibit the DNA unwinding activity of replicative helicases. We found that EBNA-1, when bound to the FR, inhibits DNA unwinding in vitro by SV40 T antigen and Escherichia coli dnaB helicases in an orientation-independent manner.
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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/Antigens, Polyomavirus Transforming,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DnaB Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Epstein-Barr Virus Nuclear Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
33009-17
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8955146-Antigens, Polyomavirus Transforming,
pubmed-meshheading:8955146-Bacterial Proteins,
pubmed-meshheading:8955146-Cell-Free System,
pubmed-meshheading:8955146-DNA, Viral,
pubmed-meshheading:8955146-DNA Helicases,
pubmed-meshheading:8955146-DNA Replication,
pubmed-meshheading:8955146-DnaB Helicases,
pubmed-meshheading:8955146-Epstein-Barr Virus Nuclear Antigens,
pubmed-meshheading:8955146-Herpesvirus 4, Human,
pubmed-meshheading:8955146-Macromolecular Substances,
pubmed-meshheading:8955146-Structure-Activity Relationship,
pubmed-meshheading:8955146-Virus Replication
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pubmed:year |
1996
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pubmed:articleTitle |
Role of the EBNA-1 protein in pausing of replication forks in the Epstein-Barr virus genome.
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pubmed:affiliation |
Department of Cell Biology, Albert Einstein College of Medicine, New York, New York 10461, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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