Oligomerization of the 17-kDa peptide-binding domain of the molecular chaperone HSC70

European Journal of Biochemistry

Volumn 259, Issue 1-2, 1999, Pages 379-384

  Fouchaq, Benoît ^a   Benaroudj, Nadia ^a   Ebel, Christine ^b   Ladjimi, Moncef M ^a  

^a CNRS   (France)

^b CEA GRENOBLE   (France)

Author keywords

Analytical ultracentrifugation; Heat shock proteins; HSC70; Molecular chaperones; Self association

Indexed keywords

CHAPERONE;

ARTICLE; CRYSTAL STRUCTURE; MOLECULAR DYNAMICS; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; ULTRACENTRIFUGATION;

ADENOSINE TRIPHOSPHATASES; APOPROTEINS; BINDING SITES; CARRIER PROTEINS; CHROMATOGRAPHY, GEL; CYTOCHROME C GROUP; CYTOCHROMES C; HSC70 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MODELS, THEORETICAL; MUTATION; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; ULTRACENTRIFUGATION;

EID: 0033556248     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00053.x     Document Type: Article

References (33)

1. Hartl, F.U. (1996) Molecular chaperones in cellular protein folding. Nature 381, 571-579.
2. Schatz, G. & Dobberstein, B. (1996) Common principles of protein translocation across membranes. Science 271, 1519-1526.
3. Bukau, B. & Horwich, A.L. (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366.
4. Chappell, T.G., Konforti, B.B., Schmid, S.L. & Rothman, J.E. (1987) The ATPase core of a clathrin uncoating protein. J. Biol. Chem 262, 746-751.
5. Wang, T.F., Chang, J.H. & Wang, C. (1993) Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding. J. Biol. Chem 268, 26049-26051.
6. Zhu, X., Zhao, X., Burkholder, W.F., Gragerov, A., Ogata, C.M., Gottesman, M.E. & Hendrickson, W.A. (1996) Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272, 1606-1614.
7. Flaherty, K.M., DeLuca-Flaherty, C. & McKay, D.B. (1990) Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein [see comments]. Nature 346, 623-628.
8. Takenaka, I.M., Leung, S.M., McAndrew, S.J., Brown, J.P. & Hightower, L.E. (1995) Hsc70-binding peptides selected from a phage display peptide library that resemble organellar targeting sequences. J. Biol. Chem 270, 19839-19844.
9. Palleros, D.R., Welch, W.J. & Fink, A.L. (1991) Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Proc. Natl. Acad. Sci. USA 88, 5719-5723.
10. Flynn, G.C., Chappell, T.G. & Rothman, J.E. (1989) Peptide binding and release by proteins implicated as catalysts of protein assembly. Science-245, 385-390.
11. Sadis, S. & Hightower, L.E. (1992) Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange. Biochemistry, 31, 9406-9412.
12. Cheetham, M.E., Jackson, A.P. & Anderton, B.H. (1994) Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b. Eur J. Biochem. 226, 99-107.
13. Freeman, B.C., Myers, M.P., Schumacher, R. & Morimoto, R.L (1995) Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. Embo J. 14, 2281-2292.
14. 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 refolding. Embo J. 15, 2969-2979.
15. Greene, L.E., Zinner, R., Naficy, S. & Eisenberg, E. (1995) Effect of nucleotide on the binding of peptides to 70-kDa heat shock protein. J. Biol. Chem 270, 2967-2973.
16. Hohfeld, J., Minami, Y. & Hartl, F.U. (1995) Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83, 589-598.
17. Gross, M. & Hessefort, S. (1996) Purification and characterization of a 66-kDa protein from rabbit reticulocyte lysate which promotes the recycling of hsp 70. J. Biol. Chem 271, 16833-16841.
18. Hohfeld, J. & Jentsch, S. (1997) GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1. Embo J. 16, 6209-6216.
19. Schonfeld, H.J., Schmidt, D., Schroder, H. & Bukau, B. (1995) The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components. J. Biol. Chem 270, 2183-2189.
20. Schlossman, D.M., Schmid, S.L., Braell, W.A. & Rothman, J.E. (1984) An enzyme that removes clathrin coats: purification of an uncoating ATPase. J. Cell Biol. 99, 723-733.
21. Benaroudj, N., Fang, B., Triniolles, F., Ghelis, C. & Ladjimi, M.M. (1994) Overexpression in Escherichia coli, purification and characterization of the molecular chaperone HSC70. Eur J. Biochem. 221, 121-128.
22. Velazquez, J.M. & Lindquist, S. (1984) hsp70: nuclear concentration during environmental stress and cytoplasmic storage during recovery. Cell 36, 655-662.
23. Brown, C.R., Martin, R.L., Hansen, W.J., Beckmann, R.P. & Welch, W.J. (1993) The constitutive and stress inducible forms of hsp 70 exhibit functional similarities and interact with one another in an ATP-dependent fashion. J. Cell Biol. 120, 1101-1112.
24. Freiden, P.J., Gaut, J.R. & Hendershot, L.M. (1992) Interconversion of three differentially modified and assembled forms of BiP. Embo J. 11, 63-70.
25. Benaroudj, N., Triniolles, F. & Ladjimi, M.M. (1996) Effect of nucleotides, peptides, and unfolded proteins on the self-association of the molecular chaperone HSC70. J. Biol. Chem 271, 18471-18476.
26. Benaroudj, N., Fouchaq, B. & Ladjimi, M.M. (1997) The COOH-terminal peptide binding domain is essential for self-association of the molecular chaperone HSC70. J. Biol. Chem 272, 8744-8751.
27. Farr, C.D. & Witt, S.N. (1997) Kinetic evidence for peptide-induced oligomerization of the molecular chaperone DnaK at heat shock temperatures. Biochemistry 36, 10793-10800.
28. Takeda, S. & McKay, D.B. (1996) Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone. Biochemistry 35, 4636-4644.
29. Benaroudj, N., Batetier, G., Triniolles, F. & Ladjimi, M.M. (1995) Self-association of the molecular chaperone HSC70. Biochemistry 34, 15282-15290.
30. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
31. Philo, J.S. (1994) Acquisition and interpretation of data for biological and synthetic polymer systems. In Modern Analytical Ultracentrifugation (Schuster, T.M. & Laue, T.M., eda), pp. 156-170. Birkhauser, Boston.
32. Wilbanks, S.M., Chen, L., Tsuruta, H., Hodgson, K.O. & McKay, D.B. (1995) Solution small-angle X-ray scattering study of the molecular chaperone Hsc70 and its subfragments. Biochemistry 34, 12095-12106.
33. Morshauser, R.C., Wang, H., Flynn, G.C. & Zuiderweg, E.R. (1995) The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology. Biochemistry 34, 6261-6266.