| FtsZ fiber bundling is triggered by a conformational change in bound GTP. | |
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MedLine Citation:
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PMID: 15328358 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Rachel Marrington; Elaine Small; Alison Rodger; Timothy R Dafforn; Stephen G Addinall |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2004-08-23 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 279 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2004 Nov |
Date Detail:
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Created Date: 2004-11-15 Completed Date: 2005-01-11 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 48821-9 Citation Subset: IM |
Affiliation:
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Department of Chemistry, University of Warwick, Coventry CV4 7AL, School of Biological Sciences, Michael Smith Building, Oxford Road, Manchester M13 9PT, United Kingdom. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Bacterial Proteins
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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:
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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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