The central domain of UNC-45 chaperone inhibits the myosin power stroke

Pawel Bujalowski, Paul Nicholls, Eleno Garza, Andres Oberhauser

Research output: Contribution to journalArticle

Abstract

The multidomain UNC-45B chaperone is crucial for the proper folding and function of sarcomeric myosin. We recently found that UNC-45B inhibits the translocation of actin by myosin. The main functions of the UCS and TPR domains are known but the role of the central domain remains obscure. Here, we show—using in vitro myosin motility and ATPase assays—that the central domain alone acts as an inhibitor of the myosin power stroke through a mechanism that allows ATP turnover. Hence, UNC-45B is a unique chaperone in which the TPR domain recruits Hsp90; the UCS domain possesses chaperone-like activities; and the central domain interacts with myosin and inhibits the actin translocation function of myosin. We hypothesize that the inhibitory function plays a critical role during the assembly of myofibrils under stress and during the sarcomere development process.

Original languageEnglish (US)
Pages (from-to)41-48
Number of pages8
JournalFEBS Open Bio
Volume8
Issue number1
DOIs
StatePublished - Jan 1 2018

Fingerprint

Myosins
Stroke
Actins
Sarcomeres
Myofibrils
Adenosine Triphosphatases
Adenosine Triphosphate

Keywords

  • chaperone
  • myosin
  • UNC-45

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

The central domain of UNC-45 chaperone inhibits the myosin power stroke. / Bujalowski, Pawel; Nicholls, Paul; Garza, Eleno; Oberhauser, Andres.

In: FEBS Open Bio, Vol. 8, No. 1, 01.01.2018, p. 41-48.

Research output: Contribution to journalArticle

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