Force-Generation by the Trans-Envelope Tol-Pal System.

Gram-negative bacteria Tol-Pal cell envelope force transduction outer membrane proton motive force

Journal

Frontiers in microbiology
ISSN: 1664-302X
Titre abrégé: Front Microbiol
Pays: Switzerland
ID NLM: 101548977

Informations de publication

Date de publication:
2022
Historique:
received: 10 01 2022
accepted: 26 01 2022
entrez: 21 3 2022
pubmed: 22 3 2022
medline: 22 3 2022
Statut: epublish

Résumé

The Tol-Pal system spans the cell envelope of Gram-negative bacteria, transducing the potential energy of the proton motive force (PMF) into dissociation of the TolB-Pal complex at the outer membrane (OM), freeing the lipoprotein Pal to bind the cell wall. The primary physiological role of Tol-Pal is to maintain OM integrity during cell division through accumulation of Pal molecules at division septa. How the protein complex couples the PMF at the inner membrane into work at the OM is unknown. The effectiveness of this trans-envelope energy transduction system is underscored by the fact that bacteriocins and bacteriophages co-opt Tol-Pal as part of their import/infection mechanisms. Mechanistic understanding of this process has been hindered by a lack of structural data for the inner membrane TolQ-TolR stator, of its complexes with peptidoglycan (PG) and TolA, and of how these elements combined power events at the OM. Recent studies on the homologous stators of Ton and Mot provide a starting point for understanding how Tol-Pal works. Here, we combine

Identifiants

pubmed: 35308353
doi: 10.3389/fmicb.2022.852176
pmc: PMC8928145
doi:

Types de publication

Journal Article Review

Langues

eng

Pagination

852176

Informations de copyright

Copyright © 2022 Webby, Williams-Jones, Press and Kleanthous.

Déclaration de conflit d'intérêts

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

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Auteurs

Melissa N Webby (MN)

Department of Biochemistry, University of Oxford, Oxford, United Kingdom.

Daniel P Williams-Jones (DP)

Department of Biochemistry, University of Oxford, Oxford, United Kingdom.

Cara Press (C)

Department of Biochemistry, University of Oxford, Oxford, United Kingdom.

Colin Kleanthous (C)

Department of Biochemistry, University of Oxford, Oxford, United Kingdom.

Classifications MeSH