Dynamic assembly of FtsZ regulated by GTP hydrolysis
Dynamic assembly of FtsZ regulated by GTP hydrolysis
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DOI：
10.1093/emboj/17.2.462
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发表时间：
1998-01-15
期刊：
影响因子：
11.4
通讯作者：
Lutkenhaus, J
中科院分区：
文献类型：
--
作者：
Mukherjee, A;Lutkenhaus, J
FtsZ形成细胞动力学环，称为Z环，其指导原核生物中的胞质分裂。它与真核微管蛋白的序列相似性有限，并且与微管蛋白一样，它具有GTPase活性以及组装成各种结构（包括原丝、束和细环）的能力。通过使用电子显微镜和沉降，我们证明了来自大肠杆菌的FtsZ经历了严格的依赖于GTP的聚合反应，并且聚合物随着GTP的消耗而消失。因此，FtsZ聚合，如微管蛋白，是动态的，并通过GTP水解调节。这些结果提供了Z环的动力学的基础，有利于模型，其中Z环形成的成核事件。
FtsZ forms a cytokinetic ring, designated the Z ring, that directs cytokinesis in prokaryotes. It has limited sequence similarity to eukaryotic tubulins and, like tubulin, it has GTPase activity and the ability to assemble into various structures including protofilaments, bundles and minirings, By using both electron microscopy and sedimentation, we demonstrate that FtsZ from Escherichia coli undergoes a strictly GTP-dependent polymerization and the polymers disappear as the GTP is consumed. Thus, FtsZ polymerization, like that of tubulin, is dynamic and regulated by GTP hydrolysis, These results provide the basis for the dynamics of the Z ring and favor a model in which the Z ring is formed by a nucleation event.