Hellerschmied, Doris, Lehner, Anita, Franicevic, Nina, Arnese, Renato, Johnson, Chloe, Vogel, Antonia, Meinhart, Anton, Kurzbauer, Robert, Deszcz, Luiza, Gazda, Linn, and others. (2019) Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin. Nature Communications, 10 (1). Article Number 4781. ISSN 2041-1723. (doi:10.1038/s41467-019-12667-8) (KAR id:77825)
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Official URL: https://doi.org/10.1038/s41467-019-12667-8 |
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.
Item Type: | Article |
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DOI/Identification number: | 10.1038/s41467-019-12667-8 |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Michael Geeves |
Date Deposited: | 25 Oct 2019 12:53 UTC |
Last Modified: | 10 Dec 2022 03:23 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/77825 (The current URI for this page, for reference purposes) |
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