Journal of the Korean Magnetic Resonance Society (한국자기공명학회논문지)

Korean Magnetic Resonance Society (한국자기공명학회)
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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)
  • Received : 2012.05.07
  • Accepted : 2012.06.08
  • Published : 2012.06.20
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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.

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