Source:http://linkedlifedata.com/resource/pubmed/id/16787914
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
33
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pubmed:dateCreated |
2006-8-14
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pubmed:abstractText |
Human DNA polymerase N (POLN or pol nu) is the most recently discovered nuclear DNA polymerase in the human genome. It is an A-family DNA polymerase related to Escherichia coli pol I, human POLQ, and Drosophila Mus308. We report the first purification of the recombinant enzyme and examination of its biochemical properties, as a step toward understanding the functions of POLN. Unusual for an A-family DNA polymerase, POLN is a low fidelity enzyme incorporating T opposite template G with a frequency of 0.45 and G opposite template T with a frequency of 0.021. The frequency of misincorporation of T opposite template G is higher than any other known DNA polymerase. POLN has a processivity of DNA synthesis (1-100 nucleotides) similar to the exonuclease-deficient Klenow fragment of E. coli pol I, is inhibited by dideoxynucleotides, and resistant to aphidicolin. The strand displacement activity of POLN was higher than exonuclease-deficient Klenow fragment. Furthermore, POLN can perform translesion synthesis past thymine glycol, a common endogenous and radiation-induced product of reactive oxygen species damage to DNA. Thymine glycol blocks DNA synthesis by most DNA polymerases, but POLN was particularly adept at efficient and accurate translesion synthesis past a 5S-thymine glycol.
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pubmed:grant | |
pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Polymerase I,
http://linkedlifedata.com/resource/pubmed/chemical/DNA polymerase theta,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed DNA Polymerase,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thymine,
http://linkedlifedata.com/resource/pubmed/chemical/thymine glycol
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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 |
18
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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 |
23445-55
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16787914-Amino Acid Sequence,
pubmed-meshheading:16787914-DNA Damage,
pubmed-meshheading:16787914-DNA Polymerase I,
pubmed-meshheading:16787914-DNA Replication,
pubmed-meshheading:16787914-DNA-Directed DNA Polymerase,
pubmed-meshheading:16787914-Humans,
pubmed-meshheading:16787914-Molecular Sequence Data,
pubmed-meshheading:16787914-Protein Processing, Post-Translational,
pubmed-meshheading:16787914-Recombinant Proteins,
pubmed-meshheading:16787914-Templates, Genetic,
pubmed-meshheading:16787914-Thymine
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pubmed:year |
2006
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pubmed:articleTitle |
Human DNA polymerase N (POLN) is a low fidelity enzyme capable of error-free bypass of 5S-thymine glycol.
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pubmed:affiliation |
Department of Pharmacology, Hillman Cancer Center, University of Pittsburgh Medical School, Pittsburgh, Pennsylvania 15213-1863, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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