Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
50
pubmed:dateCreated
2004-12-14
pubmed:abstractText
Human proliferating cell nuclear antigen (hPCNA) containing a single amino acid substitution at position 85, that of lysine for glutamate (E85K), was compared to wild-type (wt) hPCNA for its ability to promote DNA synthesis by purified DNA polymerase delta (pol delta) both on unmodified templates and past chemically defined template base lesions (translesion synthesis; TLS). Significant enhancement (up to 4-5-fold or greater) was seen but depended both on the exact PCNA/pol delta ratio tested and on the specific nature of the template (e.g., unmodified versus lesion-containing; chemical nature of the template base lesion). These results suggest that human PCNA, either mutated to contain lysine (K) at position 85 or bearing similar primary mutations, would promote more secondary mutagenesis in cells and/or tissues where PCNA is normally expressed at low levels relative to pol delta. Over an entire lifetime, such secondary mutagenesis could be biomedically significant.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15915-21
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
A single amino acid change (E85K) in human PCNA that leads, relative to wild type, to enhanced DNA synthesis by DNA polymerase delta past nucleotide base lesions (TLS) as well as on unmodified templates.
pubmed:affiliation
Department of Pharmacological Sciences, University Medical Center, State University of New York, Stony Brook, New York 11794-8651, USA. paul@pharm.sunysb.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.