Hsc70/Hsp40 chaperone system mediates the Hsp90-dependent refolding of firefly luciferase

Genes to Cells

Volumn 4, Issue 12, 1999, Pages 721-729

  Minami, Yasufumi ^a   Minami, Michiko ^a  

^a OITA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; DNA; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; LUCIFERASE; THIOSULFATE SULFURTRANSFERASE;

ARTICLE; ENZYME DENATURATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; THERMAL INJURY;

ORYCTOLAGUS CUNICULUS;

EID: 0033369982     PISSN: 13569597     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2443.1999.00299.x     Document Type: Article

References (28)

1. Buchner, J. (1999) Hsp90 & Co. - a holding for folding. Trends Biochem. Sci. 24, 136-141.
2. Bukau, B., Hesterkamp, T. & Luirink, J. (1996) Growing up in a dangerous environment: a network of multiple targeting and folding pathways for nascent polypeptides in the cytosol. Trends Cell Biol. 6, 480-486.
3. Bukau, B. & Horwich, A.L. (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366.
4. Caplan, A.J. (1999) Hsp90s secrets unfold: new insights from structural and functional studies. Trends Cell Biol. 9, 262-268.
5. Chellaiah, A., Davis, A. & Mohanakumar, T. (1993) Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein. Biochim. Biophys. Acta 1174, 111-113.
6. Freeman, B.C., Myers, M.P., Schumacher, R. & Morimoto, R.I. (1995) Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J. 14, 2281-2292.
7. Freeman, B.C. & Morimoto, R.I. (1996) The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein folding. EMBO J. 15, 2969-2979.
8. Frydman, J. & Höhfeld, J. (1997) Chaperones get in touch: the Hip-Hop connection. Trends Biochem. Sci. 22, 87-92.
9. Frydman, J., Nimmesgern, E., Ohtsuka, K. & Hartl, F.U. (1994) Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370, 111-117.
10. Hartl, F.U. (1996) Molecular chaperones in cellular protein folding. Nature 381, 571-580.
11. Höhfeld, J., Minami, Y. & Hartl, F.-U. (1995) Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83, 589-598.
12. Höhfeld, J. & Jentsch, S. (1997) GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J. 16, 6209-6216.
13. Johnson, J.L. & Craig, E.A. (1997) Protein folding in vivo: unraveling complex pathways. Cell 90, 201-204.
14. Koyasu, S., Nishida, E., Kadowaki, T., et al. (1986) Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins. Proc. Natl. Acad. Sci. USA 83, 8054-8058.
15. Minami, Y.H., Höhfeld, J., Ohtsuka, K. & Hartl, F.-U. (1996) Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40. J. Biol. Chem. 271, 19617-19624.
16. Miyata, Y. & Yahara, I. (1995) Interaction between casein kinase II and the 90-kDa stress protein, HSP90. Biochemistry 34, 8123-8129.
17. Obermann, W.M.J., Sondermann, H., Russo, A.A., Pavletich, N.P. & Hartl, F.U. (1998) In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J. Cell Biol. 143, 901-910.
18. Oh, S., Iwahori, A. & Kato, S. (1993) Human cDNA encoding DnaJ protein homologue. Biochim. Biophys. Acta 1174, 114-116.
19. Panaretou, B., Prodromou, C., Roe, S.M., et al. (1998) ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17, 4829-4836.
20. Pelham, H.R.B. (1986) Speculation on the functions of the major heat shock protein and glucose-regulated proteins. Cell 46, 959-961.
21. Rassow, J., von Ahsen, O.B., Bömer, U. & Pfanner, N. (1997) Molecular chaperones: towards a characterization of the heat-shock protein 70 family. Trends Cell Biol. 7, 129-133.
22. Szabo, A., Korszun, R., Hartl, F.U. & Flanagan, J. (1996) A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. EMBO J. 15, 408-417.
23. Shue, G. & Kohtz, D.S. (1994) Structural and functional aspects of basic helix-loop-helix protein folding by heat-shock protein 90. J. Biol. Chem. 269, 2707-2711.
24. Takayama, S., Bimston, D.N., Matsuzawa, S., et al. (1997) BAG-1 modulates the chaperone activity of Hsp70/Hsc70. EMBO J. 16, 4887-4896.
25. Terada, K., Kanazawa, M., Bukau, B. & Mori, M. (1997) The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding. J. Cell Biol. 139, 1089-1095.
26. Wiech, H., Buchner, J., Zimmermann, R. & Jakob, U. (1992) Hsp90 chaperones protein folding in vitro. Nature 358, 169-170.
27. Yonehara, M., Minami, Y., Kawata, Y., Nagai, J. & Yahara, I. (1996) Heat-induced chaperone activity of HSP90. J. Biol. Chem. 271, 2641-2645.
28. Zeiner, M., Gebauer, M. & Gehring, U. (1997) Mammalian protein RAP46: an interaction partner and modulator of 70 kDa heat shock proteins. EMBO J. 16, 5483-5490.