Tol Energy-Driven Localization of Pal and Anchoring to the Peptidoglycan Promote Outer-Membrane Constriction.
OM invagination
Tol–Pal system
membrane vesicles
molecular motor
septum
Journal
Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R
Informations de publication
Date de publication:
09 08 2019
09 08 2019
Historique:
received:
09
04
2019
revised:
21
05
2019
accepted:
24
05
2019
pubmed:
4
6
2019
medline:
12
6
2020
entrez:
3
6
2019
Statut:
ppublish
Résumé
During cell division, gram-negative bacteria must coordinate inner-membrane invagination, peptidoglycan synthesis and cleavage and outer-membrane (OM) constriction. The OM constriction remains largely enigmatic, and the nature of this process, passive or active, is under debate. The proton-motive force-dependent Tol-Pal system performs a network of interactions within these three compartments. Here we confirm that the trans-envelope Tol-Pal complex accumulates at constriction site in Escherichia coli. We show that the inner-membrane complex composed of TolA, TolQ and TolR recruits the OM complex TolB-Pal to the septum, in an energy-dependent process. Pal recruitment then allows its binding to peptidoglycan and subsequently OM constriction. Our results provide evidence that the constriction of the OM is an energized process.
Identifiants
pubmed: 31153904
pii: S0022-2836(19)30323-7
doi: 10.1016/j.jmb.2019.05.039
pii:
doi:
Substances chimiques
Bacterial Outer Membrane Proteins
0
Escherichia coli Proteins
0
ExcC protein, E coli
0
Lipoproteins
0
Membrane Proteins
0
Peptidoglycan
0
tolA protein, E coli
0
tolQ protein, E coli
110736-92-0
tolR protein, E coli
110736-93-1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3275-3288Informations de copyright
Copyright © 2019. Published by Elsevier Ltd.