FlhF regulates the number and configuration of periplasmic flagella in Borrelia burgdorferi.


Journal

Molecular microbiology
ISSN: 1365-2958
Titre abrégé: Mol Microbiol
Pays: England
ID NLM: 8712028

Informations de publication

Date de publication:
06 2020
Historique:
received: 19 09 2019
revised: 03 02 2020
accepted: 04 02 2020
pubmed: 11 2 2020
medline: 27 4 2021
entrez: 11 2 2020
Statut: ppublish

Résumé

The Lyme disease bacterium Borrelia burgdorferi has 7-11 periplasmic flagella (PF) that arise from the cell poles and extend toward the midcell as a flat-ribbon, which is distinct from other bacteria. FlhF, a signal recognition particle (SRP)-like GTPase, has been found to regulate the flagellar number and polarity; however, its role in B. burgdorferi remains unknown. B. burgdorferi has an FlhF homolog (BB0270). Structural and biochemical analyses show that BB0270 has a similar structure and enzymatic activity as its counterparts from other bacteria. Genetics and cryo-electron tomography studies reveal that deletion of BB0270 leads to mutant cells that have less PF (4 ± 2 PF per cell tip) and fail to form a flat-ribbon, indicative of a role of BB0270 in the control of PF number and configuration. Mechanistically, we demonstrate that BB0270 localizes at the cell poles and controls the number and position of PF via regulating the flagellar protein stability and the polar localization of the MS-ring protein FliF. Our study not only provides the detailed characterizations of BB0270 and its profound impacts on flagellar assembly, morphology and motility in B. burgdorferi, but also unveils mechanistic insights into how spirochetes control their unique flagellar patterns.

Identifiants

pubmed: 32039533
doi: 10.1111/mmi.14482
pmc: PMC8085991
mid: NIHMS1681732
doi:

Substances chimiques

Bacterial Proteins 0
flhF protein, Bacteria 148970-49-4
Monomeric GTP-Binding Proteins EC 3.6.5.2

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

1122-1139

Subventions

Organisme : NIAID NIH HHS
ID : R01 AI078958
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI087946
Pays : United States
Organisme : NIDCR NIH HHS
ID : R01 DE023080
Pays : United States
Organisme : NIH HHS
ID : S10 OD023603
Pays : United States

Commentaires et corrections

Type : ErratumIn

Informations de copyright

© 2020 John Wiley & Sons Ltd.

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Auteurs

Kai Zhang (K)

Philips Institute for Oral Health Research, School of Dentistry, Virginia Commonwealth University, Richmond, VA, USA.

Jun He (J)

Department of Microbial Pathogenesis, Microbial Sciences Institute, Yale University School of Medicine, New Haven, CT, USA.

Claudio Cantalano (C)

Department of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, Richmond, VA, USA.
Institute for Structural Biology, Drug Discovery and Development, School of Pharmacy, Virginia Commonwealth University, Richmond, VA, USA.

Youzhong Guo (Y)

Department of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, Richmond, VA, USA.
Institute for Structural Biology, Drug Discovery and Development, School of Pharmacy, Virginia Commonwealth University, Richmond, VA, USA.

Jun Liu (J)

Department of Microbial Pathogenesis, Microbial Sciences Institute, Yale University School of Medicine, New Haven, CT, USA.

Chunhao Li (C)

Philips Institute for Oral Health Research, School of Dentistry, Virginia Commonwealth University, Richmond, VA, USA.
Department of Microbiology and Immunology, School of Medicine, Virginia Commonwealth University, Richmond, VA, USA.

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