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PreprintCited by 4Bacterial Genetics and BiotechnologyATP Synthase and ATPases ResearchAdvanced Electron Microscopy Techniques and Applications

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Hybrid Exb/Mot stators require substitutions distant from the chimeric pore to power flagellar rotation

Open access
Ridone, Pietro, Baker, Matthew AB·2024·Journal of Bacteriology
DOI 10.1101/2024.03.12.584617PMC PMC11500575

Preprint — published as 10.1128/jb.00140-24

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Abstract

Powered by ion transport across the cell membrane, conserved ion-powered rotary motors (IRMs) drive bacterial motility by generating torque on the rotor of the bacterial flagellar motor. Homologous heteroheptameric IRMs have been structurally characterized in ion channels such as Tol/Ton/Exb/Gld, and most recently in phage defense systems such as Zor. Functional stator complexes synthesized from chimeras of PomB/MotB (PotB) have been used to study flagellar rotation at low ion-motive force achieved via reduced external sodium concentration. The function of such chimeras is highly sensitive to the location of the fusion site, and these hybrid proteins have thus far been arbitrarily designed. To date, no chimeras have been constructed using interchange of components from Tol/Ton/Exb/Gld and other ion powered motors with more distant homology. Here we synthesised chimeras of MotAB, PomAPotB and ExbBD to assess their capacity for cross-compatibility. We generated motile strains powered by stator complexes with B-subunit chimeras. This motility was further optimised by directed evolution. Whole genome sequencing of these strains revealed that motility-enhancing residue changes occurred in the A-subunit and at the peptidoglycan binding domain of the B-unit, which could improve motility. Overall, our work highlights the complexity of stator architecture and identifies the challenges associated with rational design of chimeric IRMs.

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Metadata

Authors
Ridone, P., & Baker, M. A.
Affiliations
UNSW Sydney (AU)
Corresponding author
Baker, Matthew AB
ORCID
Venue
Journal of Bacteriology
Publisher
openRxiv
Published
2024-03-12
Volume
206
Issue
10
Pages
e0014024-e0014024
ISSN
0021-9193 (ISSN-L)
DOI
10.1101/2024.03.12.584617
PMC
PMC11500575
OpenAlex
W4402581863
Cited by
4
References
1
Citations by year
2025: 2 · 2024: 2
FWCI
1.06
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Bacteriology (publishedVersion)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • University of New South Wales
  • Department of Education and Training (DP190100497)
  • U.S. Navy
  • Office of Naval Research
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
Keywords
flagellar motor, bacterial motility, directed evolution, peptidoglycan-binding domain, ion transport
MeSH terms
Bacterial Proteins, Escherichia coli, Flagella, Recombinant Fusion Proteins, Rotation, Molecular Motor Proteins

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