Structural Characterization of the J-domain of Tid1, a Mitochondrial Hsp40/DnaJ Protein
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Tid1, belonging to the Hsp40/DnaJ family of proteins, functions as a co-chaperone of cytosolic and mitochondrial Hsp70 proteins. In particular, the N-terminal J-domain of Tid1 (Tid1-JD) constitutes the major binding sites for protein-protein interactions with client proteins, including p53, as well as its partner chaperone, Hsp70. In the present study, soluble, recombinant protein of Tid1-JD could be obtained by using the pCold vector system, and backbone NMR assignments were completed using the isotope [13C/15N]-enriched protein. Far-UV CD result implied that Tid1-JD is an -helical protein and the secondary structure determined using chemical shift data sets indentified four -helices with a loop region containing the HPD (conserved tripeptide of His, Pro and Asp) motif. Additionally, NMR spectra under different conditions implied that the HPD motif, which is a critical region for protein-protein interactions of Tid1-JD, would possess dynamic properties.
Abstract
Tid1, belonging to the Hsp40/DnaJ family of proteins, functions as a co-chaperone of cytosolic and mitochondrial Hsp70 proteins. In particular, the N-terminal J-domain of Tid1 (Tid1-JD) constitutes the major binding sites for protein-protein interactions with client proteins, including p53, as well as its partner chaperone, Hsp70. In the present study, soluble, recombinant protein of Tid1-JD could be obtained by using the pCold vector system, and backbone NMR assignments were completed using the isotope [13C/15N]-enriched protein. Far-UV CD result implied that Tid1-JD is an -helical protein and the secondary structure determined using chemical shift data sets indentified four -helices with a loop region containing the HPD (conserved tripeptide of His, Pro and Asp) motif. Additionally, NMR spectra under different conditions implied that the HPD motif, which is a critical region for protein-protein interactions of Tid1-JD, would possess dynamic properties.
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