Kinesin's second step

被引：90

作者：

Klumpp, LM

Hoenger, A

Gilbert, SP

机构：

[1] Univ Pittsburgh, Dept Biol Sci, Pittsburgh, PA 15260 USA

[2] European Mol Biol Lab, D-69012 Heidelberg, Germany

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2004年 / 101卷 / 10期

关键词：

D O I：

10.1073/pnas.0307691101

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：

We have identified dimeric kinesin mutants that become stalled on the microtubule after one ATIP turnover, unable to bind and hydrolyze ATP at their second site. We have used these mutants to determine the regulatory signal that allows ATP to bind to the forward head, such that processive movement can continue. The results show that phosphate release occurs from the rearward head before detachment, and detachment triggers active-site accessibility for ATP binding at the forward head. This mechanism, in which the rearward head controls the behavior of the forward head, may be conserved among processive motors.

引用

收藏

页码：3444 / 3449

页数：6

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