| The mechanics of FtsZ fibers. | |
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MedLine Citation:
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PMID: 22385843 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Inhibition of the Fts family of proteins causes the growth of long filamentous cells, indicating that they play some role in cell division. FtsZ polymerizes into protofilaments and assembles into the Z-ring at the future site of the septum of cell division. We analyze the rigidity of GTP-bound FtsZ protofilaments by using cryoelectron microscopy to sample their bending fluctuations. We find that the FtsZ-GTP filament rigidity is κ=4.7±1.0×10(-27) Nm(2), with a corresponding thermal persistence length of l(p)=1.15±0.25μm, much higher than previous estimates. In conjunction with other model studies, our new higher estimate for FtsZ rigidity suggests that contraction of the Z-ring may generate sufficient force to facilitate cell division. The good agreement between the measured mode amplitudes and that predicted by equipartition of energy supports our use of a simple mechanical model for FtsZ fibers. The study also provides evidence that the fibers have no intrinsic global or local curvatures, such as might be caused by partial hydrolysis of the GTP. |
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Authors:
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Daniel J Turner; Ian Portman; Timothy R Dafforn; Alison Rodger; David I Roper; Corinne J Smith; Matthew S Turner |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2012-02-21 |
Journal Detail:
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Title: Biophysical journal Volume: 102 ISSN: 1542-0086 ISO Abbreviation: Biophys. J. Publication Date: 2012 Feb |
Date Detail:
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Created Date: 2012-03-05 Completed Date: 2012-06-05 Revised Date: 2013-05-20 |
Medline Journal Info:
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Nlm Unique ID: 0370626 Medline TA: Biophys J Country: United States |
Other Details:
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Languages: eng Pagination: 731-8 Citation Subset: IM |
Copyright Information:
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Copyright © 2012 Biophysical Society. Published by Elsevier Inc. All rights reserved. |
Affiliation:
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Molecular Organisation and Assembly in Cells Doctoral Training Centre, University of Warwick, Coventry, United Kingdom. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Biomechanics Cryoelectron Microscopy Cytoskeletal Proteins / chemistry*, metabolism* Fourier Analysis Guanosine Triphosphate / metabolism Hydrolysis Protein Conformation Solutions Temperature Thermodynamics |
| Grant Support | |
ID/Acronym/Agency:
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055663/Z/98/Z//Wellcome Trust |
| Chemical | |
Reg. No./Substance:
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0/Cytoskeletal Proteins; 0/Solutions; 86-01-1/Guanosine Triphosphate |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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