Document Detail


Force generation by a dynamic Z-ring in Escherichia coli cell division.
MedLine Citation:
PMID:  19114664     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
FtsZ, a bacterial homologue of tubulin, plays a central role in bacterial cell division. It is the first of many proteins recruited to the division site to form the Z-ring, a dynamic structure that recycles on the time scale of seconds and is required for division to proceed. FtsZ has been recently shown to form rings inside tubular liposomes and to constrict the liposome membrane without the presence of other proteins, particularly molecular motors that appear to be absent from the bacterial proteome. Here, we propose a mathematical model for the dynamic turnover of the Z-ring and for its ability to generate a constriction force. Force generation is assumed to derive from GTP hydrolysis, which is known to induce curvature in FtsZ filaments. We find that this transition to a curved state is capable of generating a sufficient force to drive cell-wall invagination in vivo and can also explain the constriction seen in the in vitro liposome experiments. Our observations resolve the question of how FtsZ might accomplish cell division despite the highly dynamic nature of the Z-ring and the lack of molecular motors.
Authors:
Jun F Allard; Eric N Cytrynbaum
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-12-29
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  106     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2009 Jan 
Date Detail:
Created Date:  2009-01-07     Completed Date:  2009-02-13     Revised Date:  2013-06-02    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  145-50     Citation Subset:  IM    
Affiliation:
Department of Mathematics, University of British Columbia, Vancouver, BC, Canada V6T 1Z2.
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MeSH Terms
Descriptor/Qualifier:
Bacterial Proteins / physiology*
Biomechanics
Cell Division*
Cytoskeletal Proteins / physiology*
Escherichia coli / cytology*
Escherichia coli Proteins / physiology
Guanosine Triphosphate / metabolism
Liposomes
Models, Biological
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Cytoskeletal Proteins; 0/Escherichia coli Proteins; 0/FtsZ protein, Bacteria; 0/Liposomes; 86-01-1/Guanosine Triphosphate
Comments/Corrections

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