Source:http://linkedlifedata.com/resource/pubmed/id/16803901
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
34
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pubmed:dateCreated |
2006-8-21
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pubmed:abstractText |
Cellular functions of the REV1 gene have been conserved in evolution and appear important for maintaining genetic integrity through translesion DNA synthesis. This study documents a novel biochemical activity of human REV1 protein, due to higher affinity for single-stranded DNA (ssDNA) than the primer terminus. Preferential binding to long ssDNA regions of the template strand means that REV1 is targeted specifically to the included primer termini, a property not shared by other DNA polymerases, including human DNA polymerases alpha, beta, and eta. Furthermore, a mutant REV1 lacking N- and C-terminal domains, but catalytically active, lost this function, indicating that control is not due to the catalytic core. The novel activity of REV1 protein might imply a role for ssDNA in the regulation of translesion DNA synthesis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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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 |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
24314-21
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:16803901-Binding Sites,
pubmed-meshheading:16803901-Catalysis,
pubmed-meshheading:16803901-DNA, Single-Stranded,
pubmed-meshheading:16803901-DNA Replication,
pubmed-meshheading:16803901-Escherichia coli,
pubmed-meshheading:16803901-Humans,
pubmed-meshheading:16803901-Mutation,
pubmed-meshheading:16803901-Nuclear Proteins,
pubmed-meshheading:16803901-Nucleotidyltransferases,
pubmed-meshheading:16803901-Protein Binding,
pubmed-meshheading:16803901-Protein Structure, Tertiary,
pubmed-meshheading:16803901-Substrate Specificity
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pubmed:year |
2006
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pubmed:articleTitle |
Role of single-stranded DNA in targeting REV1 to primer termini.
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pubmed:affiliation |
Research Institute for Radiation Biology and Medicine, Hiroshima University, Hiroshima 734-8553, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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