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Science 25 January 2002: Vol. 295. no. 5555, pp. 669 - 671 DOI: 10.1126/science.1066648
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Reports
Role of the Myosin Assembly Protein UNC-45 as a Molecular Chaperone for Myosin
José M. Barral,1*
Alex H. Hutagalung,1*
Achim Brinker,3
F. Ulrich Hartl,3
Henry F. Epstein12
The organization of myosin into motile cellular structures requires
precise temporal and spatial regulation. Proteins containing a UCS
(UNC-45/CRO1/She4p) domain are necessary for the incorporation of
myosin into the contractile ring during cytokinesis and into thick
filaments during muscle development. We report that the carboxyl-terminal regions of UNC-45 bound and exerted chaperone activity on the myosin head. The amino-terminal tetratricopeptide repeat domain of UNC-45 bound the molecular chaperone Hsp90. Thus, UNC-45 functions both as a molecular chaperone and as an Hsp90 co-chaperone for myosin, which can explain previous findings of altered
assembly and decreased accumulation of myosin in UNC-45 mutants of
Caenorhabditis elegans.
1 Department of Biochemistry and Molecular
Biology,
2 Department of Neurology, Baylor College
of Medicine, Houston, TX 77030, USA.
3 Max Planck
Institute for Biochemistry, D82152 Martinsried, Germany.
*
These authors contributed equally to this work.
Present address: Max Planck Institute for
Biochemistry, D82152 Martinsried, Germany.
To whom correspondence should be addressed. E-mail:
hepstein{at}bcm.tmc.edu
Read the Full Text
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