DNA transport by a type II topoisomerase: Direct evidence for a two-gate mechanism

被引：171

作者：

Roca, J ^{[1
]}

Berger, JM ^{[1
]}

Harrison, SC ^{[1
]}

Wang, JC ^{[1
]}

机构：

[1] HARVARD UNIV, HOWARD HUGHES MED INST, CAMBRIDGE, MA 02138 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1996年 / 93卷 / 09期

关键词：

protein engineering; disulfide crosslinking; enzyme mechanism; DNA topology;

D O I：

10.1073/pnas.93.9.4057

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：

Recent biochemical and crystallographic results suggest that a type II DNA topoisomerase acts as an ATP-modulated clamp with two sets of jaws at opposite ends: a DNA-bound enzyme can admit a second DNA through one set of jaws; upon binding ATP, this DNA is passed through an enzyme-mediated opening in the first DNA and expelled from the enzyme through the other set of jaws. Experiments based on the introduction of reversible disulfide links across one dimer interface of yeast DNA topoisomerase II have confirmed this mechanism. The second DNA is found to enter the enzyme through the gate formed by the N-terminal parts of the enzyme and leave it through the gate dose to the C termini.

引用

页码：4057 / 4062

页数：6

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