The tubulin ancester, FtsZ, draughtsman, designer and driving force for bacterial cytokinesis

被引：112

作者：

Addinall, SG

Holland, B

机构：

[1] Univ Paris 11, Inst Genet & Microbiol, F-91405 Orsay, France

[2] Univ Manchester, Sch Biol Sci, Manchester M13 9PT, Lancs, England

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2002年 / 318卷 / 02期

基金：

英国惠康基金;

关键词：

bacterial cytokinesis; Z ring; Min oscillation; FtsZ polymerization; division site selection;

D O I：

10.1016/S0022-2836(02)00024-4

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：

We discuss in this review the regulation of synthesis and action of FtsZ, its structure in relation to tubulin and microtubules, and the mechanism of polymerization and disassembly (contraction) of FtsZ rings from a specific nucleation site (NS) at mid cell. These topics are considered in the light of recent immunocytological studies, high resolution structures of some division proteins and results indicating how bacteria may measure their mid cell point. (C) 2002 Elsevier Science Ltd. All rights reserved.

引用

页码：219 / 236

页数：18

共 167 条

[1] Temperature shift experiments with ftsZ84(Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated [J].