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Mutational analysis of the structure and function of the chaperone domain of UNC-45B

biorxiv. 2020; 
I. Gaziova,  T. Moncrief,  C. J. Christian,  M. White,  M. Villarreal,  S. Powell,  H. Qadota,  G. M. Benian,  A. F. Oberhauser
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Molecular Biology Reagents The UCS domain constructs (wild-type and mutants) of UNC-45B (residues 501- 931) from Homo sapiens were codon optimized for expression in Escherichia coli, synthesized (GenScript, Piscataway, NJ) and subcloned into a pET-28 vector (EMD Millipore, Billerica, MA) or pET30A (Novagen) respectively. Get A Quote

摘要

UNC-45B is a multidomain molecular chaperone that is essential for the proper folding and assembly of myosin into muscle thick filaments in vivo. We have previously demonstrated that its UCS domain is responsible for the chaperone-like properties of UNC-45B. In order to better understand the chaperoning function of the UCS domain we engineered mutations designed to: i) disrupt chaperone-client interactions by removing and altering the structure of the putative client-interacting loop and ii) disrupt chaperone-client interactions by changing highly conserved residues in the putative client-binding groove. We tested the effect of these mutations by using a novel combination of complementary biophysical (circular ... More

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