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Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase

Author

Listed:
  • Oskar Berntsson

    (University of Gothenburg)

  • Ralph P. Diensthuber

    (Humboldt-Universität zu Berlin)

  • Matthijs R. Panman

    (University of Gothenburg)

  • Alexander Björling

    (University of Gothenburg)

  • Emil Gustavsson

    (University of Gothenburg)

  • Maria Hoernke

    (University of Gothenburg
    Albert-Ludwigs-Universität Freiburg)

  • Ashley J. Hughes

    (University of Gothenburg)

  • Léocadie Henry

    (University of Gothenburg)

  • Stephan Niebling

    (University of Gothenburg)

  • Heikki Takala

    (University of Gothenburg
    University of Jyväskylä
    University of Helsinki)

  • Janne A. Ihalainen

    (University of Jyväskylä)

  • Gemma Newby

    (European Synchrotron Radiation Facility)

  • Silke Kerruth

    (Freie Universität Berlin)

  • Joachim Heberle

    (Freie Universität Berlin)

  • Marianne Liebi

    (Paul ScherrerInstitut)

  • Andreas Menzel

    (Paul ScherrerInstitut)

  • Robert Henning

    (The University of Chicago)

  • Irina Kosheleva

    (The University of Chicago)

  • Andreas Möglich

    (Humboldt-Universität zu Berlin
    Universität Bayreuth)

  • Sebastian Westenhoff

    (University of Gothenburg)

Abstract

Sensor histidine kinases are central to sensing in bacteria and in plants. They usually contain sensor, linker, and kinase modules and the structure of many of these components is known. However, it is unclear how the kinase module is structurally regulated. Here, we use nano- to millisecond time-resolved X-ray scattering to visualize the solution structural changes that occur when the light-sensitive model histidine kinase YF1 is activated by blue light. We find that the coiled coil linker and the attached histidine kinase domains undergo a left handed rotation within microseconds. In a much slower second step, the kinase domains rearrange internally. This structural mechanism presents a template for signal transduction in sensor histidine kinases.

Suggested Citation

  • Oskar Berntsson & Ralph P. Diensthuber & Matthijs R. Panman & Alexander Björling & Emil Gustavsson & Maria Hoernke & Ashley J. Hughes & Léocadie Henry & Stephan Niebling & Heikki Takala & Janne A. Iha, 2017. "Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase," Nature Communications, Nature, vol. 8(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00300-5
    DOI: 10.1038/s41467-017-00300-5
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    Cited by:

    1. Stefanie S. M. Meier & Elina Multamäki & Américo T. Ranzani & Heikki Takala & Andreas Möglich, 2024. "Leveraging the histidine kinase-phosphatase duality to sculpt two-component signaling," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Julia Dietler & Renate Gelfert & Jennifer Kaiser & Veniamin Borin & Christian Renzl & Sebastian Pilsl & Américo Tavares Ranzani & Andrés García de Fuentes & Tobias Gleichmann & Ralph P. Diensthuber & , 2022. "Signal transduction in light-oxygen-voltage receptors lacking the active-site glutamine," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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