English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/162445
COMPARTIR / IMPACTO:
Estadísticas
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:
Título

Visualization of single Escherichia coli FtsZ filament dynamics with atomic force microscopy

AutorMingorance, Jesús; Tadros, Michael; Vicente, Miguel; González-Izquierdo, José Manuel; Rivas, Germán ; Vélez, Marisela
Fecha de publicación27-may-2005
EditorAmerican Society for Biochemistry and Molecular Biology
CitaciónJ Biol Chem 280(21):20909-14 (2005)
ResumenFtsZ, the prokaryotic homologue of tubulin, is an essential cell division protein. In the cell, it localizes at the center, forming a ring that constricts during division. In vitro, it binds and hydrolyzes GTP and polymerizes in a GTP-dependent manner. We have used atomic force microscopy to study the structure and dynamics of FtsZ polymer assembly on a mica surface under buffer solution. The polymers were highly dynamic and flexible, and they continuously rearranged over the surface. End-to-end joining of filaments and depolymerization from internal zones were observed, suggesting that fragmentation and reannealing may contribute significantly to the dynamics of FtsZ assembly. The shape evolution of the restructured polymers manifested a strong inherent tendency to curve. Polymers formed in the presence of non-hydrolyzable nucleotide analogues or in the presence of GDP and AlF(3) were structurally similar but showed a slower dynamic behavior. These results provide experimental evidence supporting the model of single-strand polymerization plus cyclization recently proposed to explain the hydrodynamic behavior of the polymers in solution.
Descripción6 p.-5 fig.
Versión del editorhttp://dx.doi.org/10.1074/jbc.M503059200
URIhttp://hdl.handle.net/10261/162445
DOI10.1074/jbc.M503059200
ISSN0021-9258
E-ISSN1083-351X
Aparece en las colecciones: (CIB) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
J. Biol. Chem.-2005-Mingorance-20909-14.pdfArtículo principal609,3 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 

Artículos relacionados:


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