Physical Sciences and Mathematics Commons^™

Tetratricopeptide Repeat Motif-Mediated Hsc70-Msti1 Interaction Molecular Characterization Of The Critical Contacts For Successful Binding And Specificity*, Odutayo O. Odunuge, Judith A. Hornby, Chrisiane Bies, Richard Zimmermann, David J. Pugh, Gregory L. Blatch

Faculty Publications

Murine stress-inducible protein 1 (mSTI1) is a cochaperone that is homologous with the human Hsp70/ Hsp90-organizing protein (Hop). Guided by Hop structural data and sequence alignment analyses, we have used site-directed mutagenesis, co-precipitation assays, circular dichroism spectroscopy, steady-state fluorescence, and surface plasmon resonance spectroscopy to both qualitatively and quantitatively characterize the contacts necessary for the N-terminal tetratricopeptide repeat domain (TPR1) of mSTI1 to bind to heat shock cognate protein 70 (Hsc70) and to discriminate between Hsc70 and Hsp90. We have shown that substitutions in the first TPR motif of Lys8 or Asn12 did not affect binding of mSTI1 to Hsc70, …