Decoupling Filamentous Phage Uptake and Energy of the TolQRA Motor in Escherichia coli.
Tol-Pal system
Ton system
bacteriophage
bacteriophages
molecular motor
proton motive force
Journal
Journal of bacteriology
ISSN: 1098-5530
Titre abrégé: J Bacteriol
Pays: United States
ID NLM: 2985120R
Informations de publication
Date de publication:
02 01 2020
02 01 2020
Historique:
received:
25
06
2019
accepted:
18
10
2019
pubmed:
23
10
2019
medline:
8
9
2020
entrez:
23
10
2019
Statut:
epublish
Résumé
Filamentous phages are nonlytic viruses that specifically infect bacteria, establishing a persistent association with their host. The phage particle has no machinery for generating energy and parasitizes its host's existing structures in order to cross the bacterial envelope and deliver its genetic material. The import of filamentous phages across the bacterial periplasmic space requires some of the components of a macrocomplex of the envelope known as the Tol system. This complex uses the energy provided by the proton motive force (pmf) of the inner membrane to perform essential and highly energy-consuming functions of the cell, such as envelope integrity maintenance and cell division. It has been suggested that phages take advantage of pmf-driven conformational changes in the Tol system to transit across the periplasm. However, this hypothesis has not been formally tested. In order to decouple the role of the Tol system in cell physiology and during phage parasitism, we used mutations on conserved essential residues known for inactivating pmf-dependent functions of the Tol system. We identified impaired Tol complexes that remain fully efficient for filamentous phage uptake. We further demonstrate that the TolQ-TolR homologous motor ExbB-ExbD, normally operating with the TonB protein, is able to promote phage infection along with full-length TolA.
Identifiants
pubmed: 31636109
pii: JB.00428-19
doi: 10.1128/JB.00428-19
pmc: PMC6941534
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Escherichia coli Proteins
0
ExbB protein, E coli
0
Membrane Proteins
0
tolQ protein, E coli
110736-92-0
tolR protein, E coli
110736-93-1
exbD protein, E coli
123424-75-9
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2020 American Society for Microbiology.
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