Similarity in the catalysis of DNA breakage and rejoining by type IA and IIA DNA topoisomerases

被引：60

作者：

Liu, QY ^{[1
]}

Wang, JC ^{[1
]}

机构：

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

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1999年 / 96卷 / 03期

关键词：

enzyme mechanism; DNA-protein transesterification; alanine substitution mutagenesis; quinolone binding pocket;

D O I：

10.1073/pnas.96.3.881

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：

Studies of yeast DNA topoisomerase II with various alanine substitution mutations provide strong biochemical support of a recent hypothesis that the type IA and IIA DNA topoisomerases act similarly in their cleavage and rejoining of DNA. DNA breakage and rejoining by either a type IA or a type IIA enzyme are shown to involve cooperation between a DNA-binding domain containing the active-site tyrosine and a Rossmann fold containing several highly conserved acidic residues. For a homodimeric type IIA enzyme, cooperation occurs in trans: the active-site tyrosine in the DNA-binding domain of one protomer cooperates with several residues in the Rossmann fold as well as other regions of the other protomer.

引用

页码：881 / 886

页数：6

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