Source:http://linkedlifedata.com/resource/pubmed/id/10862773
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
36
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pubmed:dateCreated |
2000-10-13
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pubmed:abstractText |
8-Oxoguanine (G*), induced by reactive oxygen species, is mutagenic because it mispairs with A. The major G*-DNA glycosylase (OGG), namely, OGG1 in eukaryotes, or MutM in Escherichia coli, excises G* when paired in DNA with C, G, and T, but not A, presumably because removal of G* from a G*.A pair would be mutagenic. However, repair of G* will prevent mutation when it is incorporated in the nascent strand opposite A. This could be carried out by a second OGG, OGG2, identified in yeast and human cells. We have characterized a new OGG activity in E. coli and then identified it to be endonuclease VIII (Nei), discovered as a damaged pyrimidine-specific DNA glycosylase. Nei shares sequence homology and reaction mechanism with MutM and is similar to human OGG2 in being able to excise G* when paired with A (or G). Kinetic analysis of wild type Nei showed that it has significant activity for excising G* relative to dihydrouracil. The presence of OGG2 type enzyme in both E. coli and eukaryotes, which is at least as efficient in excising G* from a G*.A (or G) pair as from a G*.C pair, supports the possibility of G* repair in the nascent DNA strand.
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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/DNA-Formamidopyrimidine Glycosylase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-formamidopyrimidine...,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease (Pyrimidine Dimer),
http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Glycosyl Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27762-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10862773-DNA Damage,
pubmed-meshheading:10862773-DNA Repair,
pubmed-meshheading:10862773-DNA-Formamidopyrimidine Glycosylase,
pubmed-meshheading:10862773-Deoxyribonuclease (Pyrimidine Dimer),
pubmed-meshheading:10862773-Endodeoxyribonucleases,
pubmed-meshheading:10862773-Escherichia coli,
pubmed-meshheading:10862773-Escherichia coli Proteins,
pubmed-meshheading:10862773-Humans,
pubmed-meshheading:10862773-Kinetics,
pubmed-meshheading:10862773-N-Glycosyl Hydrolases,
pubmed-meshheading:10862773-Oligodeoxyribonucleotides,
pubmed-meshheading:10862773-Recombinant Proteins,
pubmed-meshheading:10862773-Saccharomyces cerevisiae,
pubmed-meshheading:10862773-Substrate Specificity
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pubmed:year |
2000
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pubmed:articleTitle |
Characterization of a novel 8-oxoguanine-DNA glycosylase activity in Escherichia coli and identification of the enzyme as endonuclease VIII.
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pubmed:affiliation |
Sealy Center for Molecular Science and Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, Texas 77555, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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