Document Detail


FtsZ fiber bundling is triggered by a conformational change in bound GTP.
MedLine Citation:
PMID:  15328358     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Polymer formation by the essential FtsZ protein plays a crucial role in the cytokinesis of most prokaryotes. Lateral associations between these FtsZ polymers to form bundles or sheets are widely predicted to be extremely important for FtsZ function in vivo. We have carried out a study in vitro of FtsZ polymer formation and bundling using linear dichroism (LD) to assess structural properties of the polymers. We demonstrate proof-of-principle experiments to show that LD can be used as a technique to follow FtsZ polymerization, and we present the LD spectra of FtsZ polymers. Our subsequent examination of FtsZ polymer bundling induced by calcium reveals a substantial increase in the LD signal indicative of increased polymer length and rigidity. We also detect a specific conformational change in the guanine moiety associated with bundling, whereas the conformation and configuration of the FtsZ monomers within the polymer remain largely unchanged. We demonstrate that other divalent cations can induce this conformational change in FtsZ-bound GTP coincident with polymer bundling. Therefore, we present "flipping" of the guanine moiety in FtsZ-bound GTP as a mechanism that explains the link between reduced GTPase activity, increased polymer stability, and polymer bundling.
Authors:
Rachel Marrington; Elaine Small; Alison Rodger; Timothy R Dafforn; Stephen G Addinall
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2004-08-23
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  279     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2004 Nov 
Date Detail:
Created Date:  2004-11-15     Completed Date:  2005-01-11     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  48821-9     Citation Subset:  IM    
Affiliation:
Department of Chemistry, University of Warwick, Coventry CV4 7AL, School of Biological Sciences, Michael Smith Building, Oxford Road, Manchester M13 9PT, United Kingdom.
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MeSH Terms
Descriptor/Qualifier:
Bacterial Proteins / chemistry*
Calcium / chemistry
Calcium Chloride / pharmacology
Cations
Circular Dichroism
Cytoskeletal Proteins / chemistry*
Escherichia coli / metabolism
GTP Phosphohydrolases / chemistry
Guanine / chemistry
Guanosine Triphosphate / chemistry*
Kinetics
Light
Magnesium / chemistry
Magnesium Chloride / pharmacology
Models, Biological
Models, Chemical
Models, Molecular
Polymers / chemistry
Potassium Chloride / pharmacology
Protein Conformation
Scattering, Radiation
Spectrophotometry
Time Factors
Ultraviolet Rays
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Cations; 0/Cytoskeletal Proteins; 0/FtsZ protein, Bacteria; 0/Polymers; 10043-52-4/Calcium Chloride; 73-40-5/Guanine; 7439-95-4/Magnesium; 7440-70-2/Calcium; 7447-40-7/Potassium Chloride; 7786-30-3/Magnesium Chloride; 86-01-1/Guanosine Triphosphate; EC 3.6.1.-/GTP Phosphohydrolases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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