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http://dx.doi.org/10.6564/JKMRS.2012.16.1.022

Structural Characterization of the J-domain of Tid1, a Mitochondrial Hsp40/DnaJ Protein  

Sim, Dae-Won (Department of Biotechnology, Konkuk University)
Jo, Ku-Sung (Department of Biotechnology, Konkuk University)
Ryu, Kyoung-Seok (Division of Magnetic Resonance, Korea Basic Science Institute)
Kim, Eun-Hee (Division of Magnetic Resonance, Korea Basic Science Institute)
Won, Hyung-Sik (Department of Biotechnology, Konkuk University)
Publication Information
Journal of the Korean Magnetic Resonance Society / v.16, no.1, 2012 , pp. 22-33 More about this Journal
Abstract
Tid1, belonging to the Hsp40/DnaJ family of proteins, functions as a cochaperone of cytosolic and mitochondrial Hsp70 proteins. In particular, the N-terminal J-domain of Tid1 (Tid1-JD) constitutes the major binding sites for proteinprotein 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 $[^{13}C/^{15}N]$-enriched protein. Far-UV CD result implied that Tid1-JD is an ${\alpha}$-helical protein and the secondary structure determined using chemical shift data sets indentified four ${\alpha}$-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.
Keywords
Tid1; mtHsp40; DnaJA3; J-domain; Secondary structure; HPD motif;
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