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Structural insights into the mechanism of archaellar rotational switching

Author

Listed:
  • Florian Altegoer

    (Philipps-University Marburg, Center for Synthetic Microbiology (SYNMIKRO) & Faculty of Chemistry
    Heinrich-Heine University Düsseldorf, Institute of Microbiology)

  • Tessa E. F. Quax

    (University of Freiburg
    University of Groningen)

  • Paul Weiland

    (Philipps-University Marburg, Center for Synthetic Microbiology (SYNMIKRO) & Faculty of Chemistry)

  • Phillip Nußbaum

    (University of Freiburg)

  • Pietro I. Giammarinaro

    (Philipps-University Marburg, Center for Synthetic Microbiology (SYNMIKRO) & Faculty of Chemistry)

  • Megha Patro

    (University of Freiburg)

  • Zhengqun Li

    (University of Freiburg)

  • Dieter Oesterhelt

    (Max-Planck Institute for Biochemistry)

  • Martin Grininger

    (Goethe University Frankfurt, Institute of Organic Chemistry and Chemical Biology and Buchmann Institute for Molecular Life Sciences)

  • Sonja-Verena Albers

    (University of Freiburg)

  • Gert Bange

    (Philipps-University Marburg, Center for Synthetic Microbiology (SYNMIKRO) & Faculty of Chemistry
    Max-Planck Institute for terrestrial Microbiology)

Abstract

Signal transduction via phosphorylated CheY towards the flagellum and the archaellum involves a conserved mechanism of CheY phosphorylation and subsequent conformational changes within CheY. This mechanism is conserved among bacteria and archaea, despite substantial differences in the composition and architecture of archaellum and flagellum, respectively. Phosphorylated CheY has higher affinity towards the bacterial C-ring and its binding leads to conformational changes in the flagellar motor and subsequent rotational switching of the flagellum. In archaea, the adaptor protein CheF resides at the cytoplasmic face of the archaeal C-ring formed by the proteins ArlCDE and interacts with phosphorylated CheY. While the mechanism of CheY binding to the C-ring is well-studied in bacteria, the role of CheF in archaea remains enigmatic and mechanistic insights are absent. Here, we have determined the atomic structures of CheF alone and in complex with activated CheY by X-ray crystallography. CheF forms an elongated dimer with a twisted architecture. We show that CheY binds to the C-terminal tail domain of CheF leading to slight conformational changes within CheF. Our structural, biochemical and genetic analyses reveal the mechanistic basis for CheY binding to CheF and allow us to propose a model for rotational switching of the archaellum.

Suggested Citation

  • Florian Altegoer & Tessa E. F. Quax & Paul Weiland & Phillip Nußbaum & Pietro I. Giammarinaro & Megha Patro & Zhengqun Li & Dieter Oesterhelt & Martin Grininger & Sonja-Verena Albers & Gert Bange, 2022. "Structural insights into the mechanism of archaellar rotational switching," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-30358-9
    DOI: 10.1038/s41467-022-30358-9
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    References listed on IDEAS

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    1. Iain G. Duggin & Christopher H. S. Aylett & James C. Walsh & Katharine A. Michie & Qing Wang & Lynne Turnbull & Emma M. Dawson & Elizabeth J. Harry & Cynthia B. Whitchurch & Linda A. Amos & Jan Löwe, 2015. "CetZ tubulin-like proteins control archaeal cell shape," Nature, Nature, vol. 519(7543), pages 362-365, March.
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