A REPAIR SYSTEM FOR 8-OXO-7,8-DIHYDRODEOXYGUANINE

被引：311

作者：

MICHAELS, ML

TCHOU, J

GROLLMAN, AP

MILLER, JH

机构：

[1] UNIV CALIF LOS ANGELES,DEPT MICROBIOL & MOLEC GENET,LOS ANGELES,CA 90024

[2] UNIV CALIF LOS ANGELES,INST MOLEC BIOL,LOS ANGELES,CA 90024

[3] SUNY STONY BROOK,DEPT PHARMACOL SCI,STONY BROOK,NY 11794

来源：

BIOCHEMISTRY | 1992年 / 31卷 / 45期

关键词：

D O I：

10.1021/bi00160a004

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：

Active oxygen species can damage DNA and may play a role in aging and carcinogenesis. We have tested MutY glycosylase for activity on undamaged mispairs as well as mispairs formed with the oxidatively damaged substrates, 8-oxo-7,8-dihydrodeoxyguanine (GO) or 8-oxo-7,8-dihydrodeoxyadenine (AO). MutY acts as a glycosylase on four of the heteroduplexes tested, A/G, A/GO, A/C, and A/AO, removing the undamaged adenine from each substrate. Genetic data suggest that the primary substrate for MutY glycosylase in vivo is the A/GO mispair. We present biochemical evidence demonstrating that MutY glycosylase is an important part of a repair system that includes the MutM and MutT proteins. The GO repair system is dedicated to the repair of the oxidatively damaged guanine and the mutations it can induce.

引用

页码：10964 / 10968

页数：5

共 21 条

[1] ESCHERICHIA-COLI MUTY GENE ENCODES AN ADENINE GLYCOSYLASE ACTIVE ON G-A MISPAIRS [J].