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PMID: 9430638 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

The EMBO journal ·Vol. 17 ·No. 2 ·1998-01-15 ·Pages 462-9

Mukherjee A, Lutkenhaus J

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.

MeSH Terms
Bacterial Proteins/analysis,drug effects,metabolism,ultrastructure Cytoskeletal Proteins GTP-Binding Proteins/metabolism Guanosine Triphosphate/metabolism,pharmacology Hydrolysis Microscopy, Electron Polymers/analysis,metabolism Ultracentrifugation
Chemicals
Bacterial Proteins Cytoskeletal Proteins FtsZ protein, Bacteria Polymers Guanosine Triphosphate GTP-Binding Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Mukherjee A
Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City 66160, USA.
Lutkenhaus J
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28 references, click to expand
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
DOI
10.1093/emboj/17.2.462
Published
1998-01-15
Pages
462-9
Language
English
Region
England
NLM ID
8208664
PMCID
PMC1170397
Subset
IM
Grants
NIGMS NIH HHS · GM29764 · United States
External Links
PubMed source DOI: 10.1093/emboj/17.2.462 PMC Full Text View journal details
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