Mukherjee A, Lutkenhaus J
Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City 66160, USA.
EMBO J. 1998 Jan 15;17(2):462-9. doi: 10.1093/emboj/17.2.462.
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.
FtsZ形成一个细胞分裂环,称为Z环,它指导原核生物的细胞分裂。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GTP酶活性以及组装成各种结构的能力,包括原丝、束和微环。通过使用电子显微镜和沉降法,我们证明来自大肠杆菌的FtsZ经历严格的GTP依赖性聚合,并且随着GTP的消耗聚合物消失。因此,FtsZ聚合,与微管蛋白一样,是动态的并且受GTP水解调节。这些结果为Z环的动态变化提供了基础,并支持Z环由成核事件形成的模型。