Article
- The EMBO Journal (1998) 17, 462 - 469
- doi:10.1093/emboj/17.2.462
Dynamic assembly of FtsZ regulated by GTP hydrolysis
Amit Mukherjee1 and Joe Lutkenhaus1
- Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, KS 66160, USA
Correspondence to:
Joe Lutkenhaus, E-mail: jlutkenh@kumc.edu
Received 1 August 1997; Accepted 7 November 1997; Revised 30 September 1997
Abstract
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.
Keywords:
- cytokinesis,
- cytoskeleton,
- FtsZ,
- GTPase,
- tubulin
