DNA glycosylase recognition and catalysis

被引：160

作者：

Fromme, JC

Banerjee, A

Verdine, GL

机构：

[1] Harvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA

[2] Harvard Univ, Dept Chem & Biol Chem, Cambridge, MA 02138 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2004年 / 14卷 / 01期

关键词：

D O I：

10.1016/j.sbi.2004.01.003

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：

DNA glycosylases are the enzymes responsible for recognizing base lesions in the genome and initiating base excision DNA repair. Recent structural and biochemical results have provided novel insights into DNA damage recognition and repair. The basis of the recognition of the oxidative lesion 8-oxoguanine by two structurally unrelated DNA glycosylases is now understood and has been revealed to involve surprisingly similar strategies. Work on MutM (Fpg) has produced structures representing three discrete reaction steps. The NMR structure of 3-methyladenine glycosylase I revealed its place among the structural families of DNA glycosylases and the X-ray structure of SMUG1 likewise confirmed that this protein is a member of the uracil DNA glycosylase superfamily. A novel disulfide cross-linking strategy was used to obtain the long-anticipated structure of MutY bound to DNA containing an A.oxoG mispair.

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收藏

页码：43 / 49

页数：7

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