Base excision repair of oxidative DNA damage activated by XPG protein

被引：243

作者：

Klungland, A

Höss, M

Gunz, D

Constantinou, A

Clarkson, SG

Doetsch, PW

Bolton, PH

Wood, RD

Lindahl, T ^{[1
]}

机构：

[1] Imperial Canc Res Fund, Clare Hall Labs, S Mimms EN6 3LD, Herts, England

[2] Ctr Med Univ Geneva, Dept Genet & Microbiol, CH-1211 Geneva 4, Switzerland

[3] Emory Univ, Sch Med, Dept Biochem, Atlanta, GA 30322 USA

[4] Emory Univ, Sch Med, Div Canc Biol, Dept Radiat Oncol, Atlanta, GA 30322 USA

[5] Wesleyan Univ, Dept Chem, Middletown, CT 06459 USA

来源：

MOLECULAR CELL | 1999年 / 3卷 / 01期

关键词：

D O I：

10.1016/S1097-2765(00)80172-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：33 / 42

页数：10

共 57 条

[11] RETRACTED: Defective transcription-coupled repair of oxidative base damage in Cockayne syndrome patients from XP group G (Retracted Article. See vol 308, pg 1740, 2005)
Cooper, PK
Nouspikel, T
Clarkson, SG
Leadon, SA
[J]. SCIENCE, 1997, 275 (5302) : 990 - 993
[12] DEMPLE B, 1994, ANNU REV BIOCHEM, V63, P915, DOI 10.1146/annurev.biochem.63.1.915
[13] The helix-hairpin-helix DNA-binding motif: A structural basis for non-sequence-specific recognition of DNA
Doherty, AJ
Serpell, LC
Ponting, CP
[J]. NUCLEIC ACIDS RESEARCH, 1996, 24 (13) : 2488 - 2497
[14] Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein
Evans, E
Fellows, J
Coffer, A
Wood, RD
[J]. EMBO JOURNAL, 1997, 16 (03) : 625 - 638
[15] Mechanism of open complex and dual incision formation by human nucleotide excision repair factors
Evans, E
Moggs, JG
Hwang, JR
Egly, JM
Wood, RD
[J]. EMBO JOURNAL, 1997, 16 (21) : 6559 - 6573
[16] Two pathways for base excision repair in mammalian cells
Frosina, G
Fortini, P
Rossi, O
Carrozzino, F
Raspaglio, G
Cox, LS
Lane, DP
Abbondandolo, A
Dogliotti, E
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (16) : 9573 - 9578
[17] The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21
Gary, R
Ludwig, DL
Cornelius, HL
MacInnes, MA
Park, MS
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (39) : 24522 - 24529
[18] RETRACTED: BRCA1 required for transcription-coupled repair of oxidative DNA damage (Retracted article. See vol 300, pg 1657, June 13 2003)
Gowen, LC
Avrutskaya, AV
Latour, AM
Koller, BH
Leadon, SA
[J]. SCIENCE, 1998, 281 (5379) : 1009 - 1012
[19] OXIDATIVE DAMAGE IN DNA - LACK OF MUTAGENICITY BY THYMINE GLYCOL LESIONS
HAYES, RC
PETRULLO, LA
HUANG, H
WALLACE, SS
LECLERC, JE
[J]. JOURNAL OF MOLECULAR BIOLOGY, 1988, 201 (02) : 239 - 246
[20] Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III
Hilbert, TP
Chaung, WR
Boorstein, RJ
Cunningham, RP
Teebor, GW
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (10) : 6733 - 6740

← 1 2 3 4 5 6 →