MUTM, A PROTEIN THAT PREVENTS G.C-]T.A TRANSVERSIONS, IS FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE

被引：218

作者：

MICHAELS, ML

PHAM, L

CRUZ, C

MILLER, JH

机构：

[1] UNIV CALIF LOS ANGELES, INST MOLEC BIOL, 405 HILGARD AVE, LOS ANGELES, CA 90024 USA

[2] UNIV CALIF LOS ANGELES, DEPT MICROBIOL, LOS ANGELES, CA 90024 USA

来源：

NUCLEIC ACIDS RESEARCH | 1991年 / 19卷 / 13期

关键词：

D O I：

10.1093/nar/19.13.3629

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：

We have cloned chromosomal DNA bordering an insert that inactivates mutM. Sequencing of this clone has revealed that the insertion element is located between the promoter and structural gene for formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase). An overproducing clone of Fapy-DNA glycosylase complements the original mutM strain that had been isolated after EMS mutagenesis. Thus, we conclude that MutM is actually Fapy-DNA glycosylase. mutM has previously been characterized as a mutator strain that leads specifically to G.C --> T.A transversions. This in vivo characterization correlates well with the mutagenic potential of one of the lesions Fapy-DNA glycosylase removes, 8-oxo-7,8-dihydro-2'-deoxyguanine (8-OxodG).

引用

页码：3629 / 3632

页数：4

共 30 条

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