Redox-regulated cochaperone activity of the human DnaJ homolog Hdj2

Free Radical Biology and Medicine

Volumn 40, Issue 4, 2006, Pages 651-659

  Choi, Hoon In ^a,b   Lee, Sang Pil ^a,b   Kim, Kyung Soon ^a   Hwang, Chae Young ^a   Lee, Yu Ran ^a   Chae, Suhn Kee ^c   Kim, Yeon Soo ^d   Chae, Ho Zoon ^b   Kwon, Ki Sun ^a  

^a Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^b Chonnam National University   (South Korea)

^c PaiChai University   (South Korea)

^d Inje University   (South Korea)

Author keywords

Chaperone; Free radical; Oxidative stress; Protein folding; Thioredoxin; Zinc finger

Indexed keywords

CHAPERONE; CYSTEINE; HYDROGEN PEROXIDE; PROTEIN DNAJ; PROTEIN HDJ2; SERINE; THIOREDOXIN; UNCLASSIFIED DRUG; ZINC;

ARTICLE; ENZYME INACTIVATION; IMMUNOPRECIPITATION; OXIDATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; ZINC FINGER MOTIF;

MAMMALIA;

EID: 31644440524     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2005.09.018     Document Type: Article

References (46)

1. F.U. Hartl Molecular chaperones in cellular protein folding Nature 381 1996 571 579
2. B. Bukau, and A.L. Horwich The Hsp70 and Hsp60 chaperone machines Cell 92 1998 351 366
3. D.M. Cyr, T. Langer, and M.G. Douglas DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70 Trends. Biochem. Sci. 19 1994 176 181
4. A.W. Karzai, and R. McMacken A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein J. Biol. Chem. 271 1996 11236 11246
5. T. Laufen, M.P. Mayer, C. Beisel, D. Klostermeier, A. Mogk, J. Reinstein, and B. Bukau Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones Proc. Natl. Acad. Sci. USA 96 1999 5452 5457
6. J. Frydman, E. Nimmesgern, K. Ohtsuka, and F.U. Hartl Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones Nature 370 1994 111 117
7. D.R. Palleros, W.J. Welch, and A.L. Fink Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding Proc. Natl. Acad. Sci. USA 88 1991 5719 5723
8. K. Liberek, J. Marszalek, D. Ang, C. Georgopoulos, and M. Zylicz Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK Proc. Natl. Acad. Sci. USA 88 1991 2874 2878
9. T. Langer, C. Lu, H. Echols, J. Flanagan, M.K. Hayer, and F.U. Hartl Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding Nature 356 1992 683 689
10. Z. Lu, and D.M. Cyr Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1 J. Biol. Chem. 273 1998 27824 27830
11. J.L. Johnson, and E.A. Craig An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae J. Cell Biol. 152 2001 851 856
12. B. Banecki, K. Liberek, D. Wall, A. Wawrzynow, C. Georgopoulos, E. Bertoli, F. Tanfani, and M. Zylicz Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone J. Biol. Chem. 271 1996 14840 14848
13. A. Szabo, R. Korszun, F.U. Hartl, and J. Flanagan A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates EMBO J. 15 1996 408 417
14. Z. Lu, and D.M. Cyr The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding J. Biol. Chem. 273 1998 5970 5978
15. T. Finkel Oxidant signals and oxidative stress Curr. Opin. Cell Biol. 15 2003 247 254
16. A. Holmgren Thioredoxin. Annu. Rev. Biochem 54 1985 237 271
17. A. Holmgren Thioredoxin and glutaredoxin systems J. Biol. Chem. 264 1989 13963 13966
18. G. Powis, D. Mustacich, and A. Coon The role of the redox protein thioredoxin in cell growth and cancer Free Radic. Biol. Med. 29 2000 312 322
19. Y. Balmer, A. Koller, G. del Val, W. Manieri, P. Schurmann, and B.B. Buchanan Proteomics gives insight into the regulatory function of chloroplast thioredoxins Proc. Natl. Acad. Sci. USA 100 2003 370 375
20. K. Motohashi, A. Kondoh, M.T. Stumpp, and T. Hisabori Comprehensive survey of proteins targeted by chloroplast thioredoxin Proc. Natl. Acad. Sci. USA 98 2001 11224 11229
21. C.Y. Hwang, Y.S. Ryu, M.S. Chung, K.D. Kim, S.S. Park, S.K. Chae, H.Z. Chae, and K.S. Kwon Thioredoxin modulates activator protein 1 (AP-1) activity and p27Kip1 degradation through direct interaction with Jab1 Oncogene 23 2004 8868 8875
22. Y. Minami, J. Hohfeld, K. Ohtsuka, and F.U. Hartl Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40 J. Biol. Chem. 271 1996 19617 19624
23. A.A. Michels, B. Kanon, A.W. Konings, K. Ohtsuka, O. Bensaude, and H.H. Kampinga Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells J. Biol. Chem. 272 1997 33283 33289
24. J.B. Hunt, S.H. Neece, and A. Ginsburg The use of 4-(2-pyridylazo) resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase Anal. Biochem. 146 1985 150 157
25. H.K. Brandes, F.W. Larimer, M.K. Geck, C.D. Stringer, P. Schurmann, and F.C. Hartman Direct identification of the primary nucleophile of thioredoxin f J. Biol. Chem. 268 1993 18411 18414
26. K. Terada, M. Kanazawa, B. Bukau, and M. Mori The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding J. Cell. Biol. 139 1997 1089 1095
27. J.R. Kim, H.W. Yoon, K.S. Kwon, S.R. Lee, and S.G. Rhee Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH Anal. Biochem. 283 2000 214 221
28. M. Martinez-Yamout, G.B. Legge, O. Zhang, P.E. Wright, and H.J. Dyson Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ J. Mol. Biol. 300 2000 805 818
29. K. Linke, T. Wolfram, J. Bussemer, and U. Jakob The roles of the two zinc binding sites in DnaJ J. Biol. Chem. 278 2003 44457 44466
30. B. Biteau, J. Labarre, and M.B. Toledano ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin Nature 425 2003 980 984
31. A.V. Budanov, A.A. Sablina, E. Feinstein, E.V. Koonin, and P.M. Chumakov Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD Science 304 2004 596 600
32. W. Tang, and C.C. Wang Zinc fingers and thiol-disulfide oxidoreductase activities of chaperone DnaJ Biochemistry 40 2001 14985 14994
33. E.R. Stadtman Protein oxidation in aging and age-related diseases Ann. N. Y. Acad. Sci. 928 2001 22 38
34. C.J. Cummings, M.A. Mancini, B. Antalffy, D.B. DeFranco, H.T. Orr, and H.Y. Zoghbi Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1 Nat. Genet. 19 1998 148 154
35. D.L. Stenoien, C.J. Cummings, H.P. Adams, M.G. Mancini, K. Patel, G.N. DeMartino, M. Marcelli, N.L. Weigel, and M.A. Mancini Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone Hum. Mol. Genet. 8 1999 731 741
36. Y. Kobayashi, A. Kume, M. Li, M. Doyu, M. Hata, K. Ohtsuka, and G. Sobue Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract J. Biol. Chem. 275 2000 8772 8778
37. A. Wyttenbach, O. Sauvageot, J. Carmichael, C. Diaz-Latoud, A.P. Arrigo, and D.C. Rubinsztein Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin Hum. Mol. Genet. 11 2002 1137 1151
38. S.J. Kim, T.S. Kim, S. Hong, H. Rhim, I.Y. Kim, and S. Kang Oxidative stimuli affect polyglutamine aggregation and cell death in human mutant ataxin-1-expressing cells Neurosci. Lett. 348 2003 21 24
39. U. Jakob, W. Muse, M. Eser, and J.C. Bardwell Chaperone activity with a redox switch Cell 96 1999 341 352
40. K.D. Kroncke, H. Haase, D. Beyersmann, V. Kolb-Bachofen, and M.K. Hayer-Hartl Nitric oxide inhibits the cochaperone activity of the RING finger-like protein DnaJ Nitric Oxide 5 2001 289 295
41. J. Yodoi, H. Masutani, and H. Nakamura Redox regulation by the human thioredoxin system Biofactors 15 2001 107 111
42. J.R. Matthews, N. Wakasugi, J.L. Virelizier, J. Yodoi, and R.T. Hay Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62 Nucleic Acids Res. 20 1992 3821 3830
43. Y. Makino, N. Yoshikawa, K. Okamoto, K. Hirota, J. Yodoi, I. Makino, and H. Tanaka Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function J. Biol. Chem. 274 1999 3182 3188
44. S.R. Lee, K.S. Kwon, S.R. Kim, and S.G. Rhee Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor J. Biol. Chem. 273 1998 15366 15372
45. S.R. Lee, K.S. Yang, J. Kwon, C. Lee, W. Jeong, and S.G. Rhee Reversible inactivation of the tumor suppressor PTEN by H2O2 J. Biol. Chem. 277 2002 20336 20342
46. M. Saitoh, H. Nishitoh, M. Fujii, K. Takeda, K. Tobiume, Y. Sawada, M. Kawabata, K. Miyazono, and H. Ichijo Mammalian thioredoxin is a direct inhibitor of apoptosis signal- regulating kinase (ASK) 1 EMBO J. 17 1998 2596 2606