Base excision repair of oxidative DNA damage activated by XPG protein

Details

Serval ID
serval:BIB_5382566B2841
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Base excision repair of oxidative DNA damage activated by XPG protein
Journal
Molecular Cell
Author(s)
Klungland  A., Hoss  M., Gunz  D., Constantinou  A., Clarkson  S. G., Doetsch  P. W., Bolton  P. H., Wood  R. D., Lindahl  T.
ISSN
1097-2765 (Print)
Publication state
Published
Issued date
01/1999
Volume
3
Number
1
Pages
33-42
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S. --- Old month value: Jan
Abstract
Oxidized pyrimidines in DNA are removed by a distinct base excision repair pathway initiated by the DNA glycosylase--AP lyase hNth1 in human cells. We have reconstituted this single-residue replacement pathway with recombinant proteins, including the AP endonuclease HAP1/APE, DNA polymerase beta, and DNA ligase III-XRCC1 heterodimer. With these proteins, the nucleotide excision repair enzyme XPG serves as a cofactor for the efficient function of hNth1. XPG protein promotes binding of hNth1 to damaged DNA. The stimulation of hNth1 activity is retained in XPG catalytic site mutants inactive in nucleotide excision repair. The data support the model that development of Cockayne syndrome in XP-G patients is related to inefficient excision of endogenous oxidative DNA damage.
Keywords
Base Sequence Binding Sites/genetics Cockayne Syndrome/genetics DNA Damage/*genetics DNA Repair/*genetics DNA-Binding Proteins/*genetics *Deoxyribonuclease (Pyrimidine Dimer) Endodeoxyribonucleases Endonucleases Enzyme Activation/genetics *Escherichia coli Proteins Humans Molecular Sequence Data Mutation/genetics Nuclear Proteins Oxidative Stress/*genetics Pyrimidines/metabolism Recombinant Proteins/genetics Transcription Factors Uracil/analogs & derivatives/metabolism
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 14:50
Last modification date
20/08/2019 14:08
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