REPAIR OF DNA METHYLPHOSPHOTRIESTERS THROUGH A METALLOACTIVATED CYSTEINE NUCLEOPHILE

被引：182

作者：

MYERS, LC

TERRANOVA, MP

FERENTZ, AE

WAGNER, G

VERDINE, GL

机构：

[1] HARVARD UNIV,PROGRAM HIGHER DEGREES BIOPHYS,CAMBRIDGE,MA 02138

[2] HARVARD UNIV,SCH MED,DEPT BIOL CHEM & MOLEC PHARMACOL,BOSTON,MA 02115

[3] HARVARD UNIV,DEPT CHEM,CAMBRIDGE,MA 02138

来源：

SCIENCE | 1993年 / 261卷 / 5125期

关键词：

D O I：

10.1126/science.8395079

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The Escherichia coli Ada protein repairs methylphosphotriesters in DNA by direct, irreversible methyl transfer to one of its own cysteines. Upon methyl transfer, Ada acquires the ability to bind specific DNA sequences and thereby to induce genes that confer resistance to methylating agents. The amino-terminal domain of Ada, which comprises the methylphosphotriester repair and sequence-specific DNA binding elements, contains a tightly bound zinc ion. Analysis of the zinc binding site by cadmium-113 nuclear magnetic resonance and site-directed mutagenesis revealed that zinc participates in the autocatalytic activation of the active site cysteine and may also function as a conformational switch.

引用

页码：1164 / 1167

页数：4

共 33 条

[1] ZINC-FINGER PROTEINS [J].