Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/243514
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | FtsZ induces membrane deformations via torsional stress upon GTP hydrolysis |
Autor: | Ramirez-Diaz, Diego A.; Merino- Salomón, Adrián; Meyer, Fabian; Heymann, Michael; Rivas, Germán CSIC ORCID CVN ; Bramkamp, Marc; Schwille, Petra | Fecha de publicación: | 3-jun-2021 | Editor: | Springer Nature | Citación: | Nature Communications 12: 3310 (2021) | Resumen: | FtsZ is a key component in bacterial cell division, being the primary protein of the presumably contractile Z ring. In vivo and in vitro, it shows two distinctive features that could so far, however, not be mechanistically linked: self-organization into directionally treadmilling vortices on solid supported membranes, and shape deformation of flexible liposomes. In cells, circumferential treadmilling of FtsZ was shown to recruit septum-building enzymes, but an active force production remains elusive. To gain mechanistic understanding of FtsZ dependent membrane deformations and constriction, we design an in vitro assay based on soft lipid tubes pulled from FtsZ decorated giant lipid vesicles (GUVs) by optical tweezers. FtsZ filaments actively transform these tubes into spring-like structures, where GTPase activity promotes spring compression. Operating the optical tweezers in lateral vibration mode and assigning spring constants to FtsZ coated tubes, the directional forces that FtsZ-YFP-mts rings exert upon GTP hydrolysis can be estimated to be in the pN range. They are sufficient to induce membrane budding with constricting necks on both, giant vesicles and E.coli cells devoid of their cell walls. We hypothesize that these forces result from torsional stress in a GTPase activity dependent manner. | Descripción: | 11 p.-6 fig. | Versión del editor: | https://doi.org/10.1038/s41467-021-23387-3 | URI: | http://hdl.handle.net/10261/243514 | DOI: | 10.1038/s41467-021-23387-3 | E-ISSN: | 2041-1723 |
Aparece en las colecciones: | (CIB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
Nature Communications_Ramirez_Diaz_2021.pdf | 6,21 MB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
PubMed Central
Citations
11
checked on 14-abr-2024
SCOPUSTM
Citations
24
checked on 28-abr-2024
WEB OF SCIENCETM
Citations
21
checked on 29-feb-2024
Page view(s)
68
checked on 01-may-2024
Download(s)
75
checked on 01-may-2024