English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/9577
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Title

Energetics and Geometry of FtsZ Polymers: Nucleated Self-Assembly of Single Protofilaments

AuthorsHuecas, Sonia ; Llorca, Óscar ; Boskovic, Jasminka; Martín-Benito, Jaime; Valpuesta, José M.; Andreu, José Manuel
KeywordsCell division
FtsZ protein
Protofilaments
Protofilament accretion and cyclization
Polymerization
Issue Date5-Mar-2008
PublisherRockefeller University Press
Elsevier
CitationBiophysical Journal 94(5): 1796-1806 (2008)
AbstractEssential cell division protein FtsZ is an assembling GTPase which directs the cytokinetic ring formation in dividing bacterial cells. FtsZ shares the structural fold of eukaryotic tubulin and assembles forming tubulin-like protofilaments, but does not form microtubules. Two puzzling problems in FtsZ assembly are the nature of protofilament association and a possible mechanism for nucleated self-assembly of single-stranded protofilaments above a critical FtsZ concentration. We assembled two-dimensional arrays of FtsZ on carbon supports, studied linear polymers of FtsZ with cryo-electron microscopy of vitrified unsupported solutions, and formulated possible polymerization models. Nucleated self-assembly of FtsZ from Escherichia coli with GTP and magnesium produces flexible filaments 4–6 nm-wide, only compatible with a single protofilament. This agrees with previous scanning transmission electron microscopy results and is supported by recent cryo-electron tomography studies of two bacterial cells. Observations of double-stranded FtsZ filaments in negative stain may come from protofilament accretion on the carbon support. Preferential protofilament cyclization does not apply to FtsZ assembly. The apparently cooperative polymerization of a single protofilament with identical intermonomer contacts is explained by the switching of one inactive monomer into the active structure preceding association of the next, creating a dimer nucleus. FtsZ behaves as a cooperative linear assembly machine.
Description11 pages, 5 figures.-- PMID: 18024502 [PubMed].-- Data Supplement available (6 pages, 10 figures).
Publisher version (URL)http://dx.doi.org/10.1529/biophysj.107.115493
URIhttp://hdl.handle.net/10261/9577
DOI10.1529/biophysj.107.115493
ISSN0006-3495
Appears in Collections:(CIB) Artículos
(CNB) Artículos
Files in This Item:
File Description SizeFormat 
Energetics_and_geometry.pdfMain text1,04 MBAdobe PDFThumbnail
View/Open
Data_supplement_1.pdfSuppl. data106,89 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.