A coproofreading Zn2+-dependent exonuclease within a bacterial replicase

被引：40

作者：

Stano, NM ^{[1
]}

Chen, J ^{[1
]}

McHenry, CS ^{[1
]}

机构：

[1] Univ Colorado, Hlth Sci Ctr, Dept Biochem & Mol Biol, Denver, CO 80262 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2006年 / 13卷 / 05期

关键词：

D O I：

10.1038/nsmb1078

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：

The proofreading exonucleases of all DNA replicases contain acidic residues that chelate two Mg2+ ions that participate in catalysis. DNA polymerase III holoenzymes contain their proofreading activity in a separate subunit, epsilon, which binds the polymerase subunit, alpha, through alpha's N-terminal php domain. Here we demonstrate that the a php domain contains a novel Zn2+-dependent 3'-> 5' exonuclease that preferentially removes mispaired nucleotides, providing the first example of a coediting nuclease.

引用

页码：458 / 459

页数：2

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