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Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin

Author

Listed:
  • Doris Hellerschmied

    (Vienna BioCenter
    University Duisburg-Essen)

  • Anita Lehner

    (Vienna BioCenter Facilities)

  • Nina Franicevic

    (Vienna BioCenter)

  • Renato Arnese

    (Vienna BioCenter)

  • Chloe Johnson

    (University of Kent)

  • Antonia Vogel

    (Vienna BioCenter)

  • Anton Meinhart

    (Vienna BioCenter)

  • Robert Kurzbauer

    (Vienna BioCenter)

  • Luiza Deszcz

    (Vienna BioCenter)

  • Linn Gazda

    (Vienna BioCenter)

  • Michael Geeves

    (University of Kent)

  • Tim Clausen

    (Vienna BioCenter
    Medical University Vienna)

Abstract

Myosin is a motor protein that is essential for a variety of processes ranging from intracellular transport to muscle contraction. Folding and assembly of myosin relies on a specific chaperone, UNC-45. To address its substrate-targeting mechanism, we reconstitute the interplay between Caenorhabditis elegans UNC-45 and muscle myosin MHC-B in insect cells. In addition to providing a cellular chaperone assay, the established system enabled us to produce large amounts of functional muscle myosin, as evidenced by a biochemical and structural characterization, and to directly monitor substrate binding to UNC-45. Data from in vitro and cellular chaperone assays, together with crystal structures of binding-deficient UNC-45 mutants, highlight the importance of utilizing a flexible myosin-binding domain. This so-called UCS domain can adopt discrete conformations to efficiently bind and fold substrate. Moreover, our data uncover the molecular basis of temperature-sensitive UNC-45 mutations underlying one of the most prominent motility defects in C. elegans.

Suggested Citation

  • Doris Hellerschmied & Anita Lehner & Nina Franicevic & Renato Arnese & Chloe Johnson & Antonia Vogel & Anton Meinhart & Robert Kurzbauer & Luiza Deszcz & Linn Gazda & Michael Geeves & Tim Clausen, 2019. "Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin," Nature Communications, Nature, vol. 10(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12667-8
    DOI: 10.1038/s41467-019-12667-8
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    Cited by:

    1. Antonia Vogel & Renato Arnese & Ricardo M. Gudino Carrillo & Daria Sehr & Luiza Deszcz & Andrzej Bylicki & Anton Meinhart & Tim Clausen, 2024. "UNC-45 assisted myosin folding depends on a conserved FX3HY motif implicated in Freeman Sheldon Syndrome," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Carl Elias Kutzner & Karen Carolyn Bauer & Jan-Wilm Lackmann & Richard James Acton & Anwesha Sarkar & Wojciech Pokrzywa & Thorsten Hoppe, 2024. "Optogenetic induction of mechanical muscle stress identifies myosin regulatory ubiquitin ligase NHL-1 in C. elegans," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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