English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/9577
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Citado 55 veces en Web of Knowledge®  |  Pub MebCentral Ver citas en PubMed Central  |  Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar otros formatos: Exportar EndNote (RIS)Exportar bibText (RIS)Exportar csv (RIS)
Título

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

AutorHuecas, Sonia ; Llorca, Óscar ; Boskovic, Jasminka; Martín-Benito, Jaime; Valpuesta, José M.; Andreu, José Manuel
Palabras claveCell division
FtsZ protein
Protofilaments
Protofilament accretion and cyclization
Polymerization
Fecha de publicación5-mar-2008
EditorRockefeller University Press
Elsevier
CitaciónBiophysical Journal 94(5): 1796-1806 (2008)
ResumenEssential 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.
Descripción11 pages, 5 figures.-- PMID: 18024502 [PubMed].-- Data Supplement available (6 pages, 10 figures).
Versión del editorhttp://dx.doi.org/10.1529/biophysj.107.115493
URIhttp://hdl.handle.net/10261/9577
DOI10.1529/biophysj.107.115493
ISSN0006-3495
Aparece en las colecciones: (CIB) Artículos
(CNB) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
Energetics_and_geometry.pdfMain text1,04 MBAdobe PDFVista previa
Visualizar/Abrir
Data_supplement_1.pdfSuppl. data106,89 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 



NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.