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

@article{Hellerschmied2019MolecularFO,
  title={Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin},
  author={D. Hellerschmied and Anita Lehner and Nina Frani{\vc}evi{\'c} and Renato Arnese and Chloe A Johnson and Antonia Vogel and A. Meinhart and R. Kurzbauer and L. Deszcz and L. Gazda and M. Geeves and T. Clausen},
  journal={Nature Communications},
  year={2019},
  volume={10}
}
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… Expand
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The biophysical assays performed on purified proteins show that all of the mutations result in reduced myosin chaperone activity but not overall protein stability, suggesting that these mutations only cause protein instability in the in vivo setting and that these conserved regions may be involved in UNC-45 protein stability/ regulation via post translational modifications, protein-protein interactions, or some other unknown mechanism. Expand
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