Base excision repair of oxidative DNA damage activated by XPG protein
Détails
ID Serval
serval:BIB_5382566B2841
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Base excision repair of oxidative DNA damage activated by XPG protein
Périodique
Molecular Cell
ISSN
1097-2765 (Print)
Statut éditorial
Publié
Date de publication
01/1999
Volume
3
Numéro
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
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S. --- Old month value: Jan
Résumé
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.
Mots-clé
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
Oui
Création de la notice
24/01/2008 14:50
Dernière modification de la notice
20/08/2019 14:08