The Chaperonin GroESL Facilitates Caulobacter crescentus Cell Division by Supporting the Functions of the Z-Ring Regulators FtsA and FzlA.

FtsA FzlA GroEL actin-like proteins bacterial cell division chaperonin peptidoglycan protein folding

Journal

mBio
ISSN: 2150-7511
Titre abrégé: mBio
Pays: United States
ID NLM: 101519231

Informations de publication

Date de publication:
04 05 2021
Historique:
entrez: 5 5 2021
pubmed: 6 5 2021
medline: 14 10 2021
Statut: epublish

Résumé

The highly conserved chaperonin GroESL performs a crucial role in protein folding; however, the essential cellular pathways that rely on this chaperone are underexplored. Loss of GroESL leads to severe septation defects in diverse bacteria, suggesting the folding function of GroESL may be integrated with the bacterial cell cycle at the point of cell division. Here, we describe new connections between GroESL and the bacterial cell cycle using the model organism

Identifiants

pubmed: 33947758
pii: mBio.03564-20
doi: 10.1128/mBio.03564-20
pmc: PMC8262945
pii:
doi:

Substances chimiques

Bacterial Proteins 0
FtsA protein, Bacteria 0
GroESL protein, Bacteria 0
Chaperonins EC 3.6.1.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

Copyright © 2021 Schroeder et al.

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Auteurs

Kristen Schroeder (K)

Science for Life Laboratory and Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Stockholm, Sweden.

Kristina Heinrich (K)

Science for Life Laboratory and Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Stockholm, Sweden.

Ines Neuwirth (I)

Science for Life Laboratory and Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Stockholm, Sweden.

Kristina Jonas (K)

Science for Life Laboratory and Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Stockholm, Sweden kristina.jonas@su.se.

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