Nature Communications (Oct 2019)

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

  • Doris Hellerschmied,
  • Anita Lehner,
  • Nina Franicevic,
  • Renato Arnese,
  • Chloe Johnson,
  • Antonia Vogel,
  • Anton Meinhart,
  • Robert Kurzbauer,
  • Luiza Deszcz,
  • Linn Gazda,
  • Michael Geeves,
  • Tim Clausen

DOI
https://doi.org/10.1038/s41467-019-12667-8
Journal volume & issue
Vol. 10, no. 1
pp. 1 – 14

Abstract

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Myosin, a motor protein essential for intracellular transport to muscle contraction, requires a chaperone UNC-45 for folding and assembly. Here authors use in vitro reconstitution and structural biology to characterize the interplay between UNC-45 and muscle myosin MHC-B.