Functional evidence for in vitro microtubule severing by the plant katanin homologue

被引：64
|
作者：
Stoppin-Mellet, V [1 ]
Gaillard, J [1 ]
Vantard, M [1 ]
机构：
[1] Univ Grenoble 1, UMR 5019 CNRS, CEA, Physiol Cellulaire Vegetale Lab, F-38054 Grenoble 9, France
来源：
BIOCHEMICAL JOURNAL | 2002年 / 365卷 / 02期
关键词：
AAA ATPase; ATPase activity; cytoskeleton; video microscopy;
D O I：
10.1042/BJ20020689
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：
Temporal and spatial assembly of microtubules in plant cells depends mainly on the activity of microtubule-interacting proteins, which either stabilize, destabilize or translocate microtubules. Recent data have revealed that the thale cress (Arabidopsis thaliana) contains a protein related to the p60 catalytic subunit of animal katanin, a microtubule-severing protein. However, effects of the plant p60 on microtubule assembly are not known. We report the first functional evidence that the recombinant A. thaliana p60 katanin subunit, Atp60, binds to microtubules and severs them in an ATP-dependent manner in vitro. ATPase activity of Atp60 is stimulated by low tubulin/katanin ratios, and is inhibited at higher ratios. Considering its properties in vitro, several functions of Atp60 in vivo are discussed.
引用
收藏
页码：337 / 342
页数：6
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