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Cited by 37Bacterial Genetics and BiotechnologyATP Synthase and ATPases ResearchAdvanced Electron Microscopy Techniques and Applications

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Ion selectivity and rotor coupling of the Vibrio flagellar sodium-driven stator unit

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Hu, Haidai, Popp, Philipp F., Santiveri, Mònica, Roa-Eguiara, Aritz, Yan, Yumeng, Martin, Freddie J. O., Liu, Zheyi, Wadhwa, Navish, Wang, Yong, Erhardt, Marc, Taylor, Nicholas M. I.·2023·Nature Communications
DOI 10.1038/s41467-023-39899-zPMC PMC10374538

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Abstract

Bacteria swim using a flagellar motor that is powered by stator units. Vibrio spp. are highly motile bacteria responsible for various human diseases, the polar flagella of which are exclusively driven by sodium-dependent stator units (PomAB). However, how ion selectivity is attained, how ion transport triggers the directional rotation of the stator unit, and how the stator unit is incorporated into the flagellar rotor remained largely unclear. Here, we have determined by cryo-electron microscopy the structure of Vibrio PomAB. The electrostatic potential map uncovers sodium binding sites, which together with functional experiments and molecular dynamics simulations, reveal a mechanism for ion translocation and selectivity. Bulky hydrophobic residues from PomA prime PomA for clockwise rotation. We propose that a dynamic helical motif in PomA regulates the distance between PomA subunit cytoplasmic domains, stator unit activation, and torque transmission. Together, our study provides mechanistic insights for understanding ion selectivity and rotor incorporation of the stator unit of the bacterial flagellum.

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Metadata

Authors
Hu, H., Popp, P. F., Santiveri, M., Roa-Eguiara, A., Yan, Y., Martin, F. J. O., Liu, Z., Wadhwa, N., Wang, Y., Erhardt, M., & Taylor, N. M. I.
Affiliations
  • University of Copenhagen (DK)
  • Humboldt-Universität zu Berlin (DE)
  • Zhejiang University (CN)
  • Arizona State University (US)
Corresponding author
Taylor, Nicholas M. I.
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2023-07-27
Volume
14
Issue
1
Pages
4411-4411
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-023-39899-z
PMC
PMC10374538
OpenAlex
W4385330728
Cited by
37
References
2
Citations by year
2026: 7 · 2025: 13 · 2024: 12 · 2023: 5
FWCI
6.07
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • Research Square (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, cc-by)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • European Commission (HORIZON2020)
  • Lundbeckfonden (NNF14CC0001, R347-2020-2429)
  • Novo Nordisk (NNF14CC0001)
  • Zhejiang University
  • Novo Nordisk Fonden (NNF 14CC0001, NNF18OC0031006, NNF17OC0031006)
  • H. Lundbeck A/S
  • National Key Research and Development Program of China (2021YFF1200404)
  • Fundamental Research Funds for the Central Universities (K20220228)
  • National Institute of General Medical Sciences (R00GM134124)
  • H2020 European Research Council (864971)
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
ion selectivity, bacterial flagellum, cryo-EM structure, electrostatic potential mapping, hydrophobic residues, helical motifs, torque transmission, clockwise rotation
MeSH terms
Bacterial Proteins, Flagella, Humans, Polymethacrylic Acids, Sodium, Cryoelectron Microscopy, Molecular Motor Proteins, Vibrio alginolyticus

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