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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1999-4-13
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pubmed:abstractText |
An ionizing radiation-induced DNA lesion, thymine glycol, is removed from DNA by a thymine glycol DNA glycosylase with an apurinic/apyrimidinic (AP) lyase activity encoded by the Escherichia coli endonuclease III ( nth ) gene and its homolog in humans. Cells from Cockayne syndrome patients with mutations in the XPG gene show approximately 2-fold reduced global repair of thymine glycol. Hence, I decided to investigate the molecular mechanism of the effect of XPG protein observed in vivo on thymine glycol removal by studying the interactions of XPG protein and human endonuclease III (HsNTH) protein in vitro and the effect of XPG protein on the activity of HsNTH protein on a substrate containing thymine glycol. The XPG protein stimulates the binding of HsNTH protein to its substrate and increases its glycosylase/AP lyase activity by a factor of approximately 2 through direct interaction between the two proteins. These results provide in vitro evidence for a second function of XPG protein in DNA repair and a mechanistic basis for its stimulatory activity on HsNTH protein.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA excision repair protein ERCC-5,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease (Pyrimidine Dimer),
http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Endonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NTH protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
27
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
979-83
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pubmed:dateRevised |
2008-11-20
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pubmed:meshHeading |
pubmed-meshheading:9927729-DNA,
pubmed-meshheading:9927729-DNA Repair,
pubmed-meshheading:9927729-DNA-Binding Proteins,
pubmed-meshheading:9927729-Deoxyribonuclease (Pyrimidine Dimer),
pubmed-meshheading:9927729-Endodeoxyribonucleases,
pubmed-meshheading:9927729-Endonucleases,
pubmed-meshheading:9927729-Escherichia coli Proteins,
pubmed-meshheading:9927729-Humans,
pubmed-meshheading:9927729-Nuclear Proteins,
pubmed-meshheading:9927729-Recombinant Fusion Proteins,
pubmed-meshheading:9927729-Substrate Specificity,
pubmed-meshheading:9927729-Transcription Factors
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pubmed:year |
1999
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pubmed:articleTitle |
Nucleotide excision repair 3' endonuclease XPG stimulates the activity of base excision repairenzyme thymine glycol DNA glycosylase.
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pubmed:affiliation |
Department of Biochemistry and Biophysics, Mary Ellen Jones Building, CB 7260, University of North CarolinaSchool of Medicine, Chapel Hill, NC 27599-7260, USA. tbess@med.unc.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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