Browse > Article

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
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.
Tid1; mtHsp40; DnaJA3; J-domain; Secondary structure; HPD motif;
Citations & Related Records
Times Cited By KSCI : 2  (Citation Analysis)
연도 인용수 순위
1 B. Lu, N. Garrido, J. N. Spelbrink, C. K. Suzuki, J. Biol. Chem. 281, 13150 (2006).   DOI
2 O. Iosefson, S. Sharon, P. Goloubinoff, A. Azem, Cell. Stress Chaperones 17, 57 (2011).
3 L. N. Diane, A. N. Elwi, S.-W. Kim, Oncotaget 1, 396 (2010).   DOI
4 B. Y. Ahn, D. L. Zajchowski, B. Lee, A. N. Elwi, S. -W. Kim, Oncotarget 29, 1155 (2010).
5 O. Iosefson, A. Azem, FEBS Lett. 584, 1080 (2010).   DOI
6 H. -S. Won, S. -H. Park, H. -E. Kim, H. -E. Kim, B. Hyun, M. Kim, B. -J. Lee, B. -J. Kim, Eur. J. Biochem. 269, 4367 (2002).   DOI   ScienceOn
7 D. -W. Sim, H. -C. Ahn, H. -S. Won, J. Korean. Magn. Reson. Soc. 13, 108 (2009).   DOI
8 D. S. Wishart, B. D. Sykes, F. M. Richards, Biochemistry 31, 1647 (1992).   DOI   ScienceOn
9 D. S. Wishart, B. D. Sykes, J. Biomol. NMR 4, 171 (1994).
10 Y. Shen, F. Delaqlio, G. Cornilescu, A. Bax, J. Biomol. NMR 44, 213 (2009).   DOI   ScienceOn
11 Y. -S. Lee, K. -S. Ryu, Y. Lee, S. Kim, K. -W. Lee, H. -S. Won, J. Korean. Magn. Reson. Soc. 15,137 (2011).   DOI   ScienceOn
12 H. -S. Won, T. Yamazaki, T. -W. Lee, M. -K. Yoon, S. -H. Park, Y. Kyogoku, B. -J. Lee, Biochemistry 39, 13953 (2000).   DOI   ScienceOn
13 H. H. Kampinga, E. A. Elizabeth, Nat. Rev. Mol. Cell. Biol. 11, 579 (2010).   DOI
14 X. B. Qiu, Y. M. Shao, S. Miao, L. Wang, Cell. Mol. Life. Sci. 63, 2560 (2006).   DOI
15 F. Hennessy, W. S. Nicoll, R. Zimmermann, M. E. Cheetham, G. L. Blatch, Protein Sci. 14, 1697 (2005).   DOI
16 P. Genevaux, C. Georgopoulos, W.L. Kelley, Mol. Microbiol. 66, 840 (2007).   DOI
17 A. Ahmad, A. Bhattacharya, R.A. Mcdonald, M. Cordes, B. Ellington, E.B. Bertelsen, E.R. Zuiderweg, Proc. Natl. Acad. Sci. USA 108, 18966 (2011).   DOI
18 Li. Jingzhi, X. Quian, B. Sha, Protein Pept. Lett. 6, 606 (2009).
19 J. Syken, T. De-Medina, K. Münger, Proc. Natl. Acad. Sci. USA 96, 8499 (1999).   DOI
20 J. Proft, J. Faraji, J. C. Robbins, F. C. Zucchi, X. Zhao, G. A. Metz, J. E. Braun, PLoS One 6, e26045 (2011).   DOI