ZomB is essential for chemotaxis of Vibrio alginolyticus by the rotational direction control of the polar flagellar motor.


Journal

Genes to cells : devoted to molecular & cellular mechanisms
ISSN: 1365-2443
Titre abrégé: Genes Cells
Pays: England
ID NLM: 9607379

Informations de publication

Date de publication:
Nov 2021
Historique:
revised: 30 08 2021
received: 05 08 2021
accepted: 01 09 2021
pubmed: 7 9 2021
medline: 14 1 2022
entrez: 6 9 2021
Statut: ppublish

Résumé

Bacteria exhibit chemotaxis by controlling flagellar rotation to move toward preferred places or away from nonpreferred places. The change in rotation is triggered by the binding of the chemotaxis signaling protein CheY-phosphate (CheY-P) to the C-ring in the flagellar motor. Some specific bacteria, including Vibrio spp. and Shewanella spp., have a single transmembrane protein called ZomB. ZomB is essential for controlling the flagellar rotational direction in Shewanella putrefaciens and Vibrio parahaemolyticus. In this study, we confirmed that the zomB deletion results only in the counterclockwise (CCW) rotation of the motor in Vibrio alginolyticus as previously reported in other bacteria. We found that ZomB is not required for a clockwise-locked phenotype caused by mutations in fliG and fliM, and that ZomB is essential for CW rotation induced by overproduction of CheY-P. Purified ZomB proteins form multimers, suggesting that ZomB may function as a homo-oligomer. These observations imply that ZomB interacts with protein(s) involved in either flagellar motor rotation, chemotaxis, or both. We provide the evidence that ZomB is a new player in chemotaxis and is required for the rotational control in addition to CheY in Vibrio alginolyticus.

Identifiants

pubmed: 34487583
doi: 10.1111/gtc.12895
doi:

Substances chimiques

Bacterial Proteins 0
Escherichia coli Proteins 0
Membrane Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

927-937

Subventions

Organisme : JSPS KAKENHI
ID : JP16J01859
Organisme : JSPS KAKENHI
ID : JP20J00329
Organisme : JSPS KAKENHI
ID : JP20H03220

Informations de copyright

© 2021 Molecular Biology Society of Japan and John Wiley & Sons Australia, Ltd.

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Auteurs

Norihiro Takekawa (N)

Department of Macromolecular Science, Graduate School of Science, Osaka University, Toyonaka, Japan.

Tatsuro Nishikino (T)

Research Center for Next-Generation Protein Sciences, Institute for Protein Research, Osaka University, Suita, Japan.

Kiyoshiro Hori (K)

Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan.

Seiji Kojima (S)

Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan.

Katsumi Imada (K)

Department of Macromolecular Science, Graduate School of Science, Osaka University, Toyonaka, Japan.

Michio Homma (M)

Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan.

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