A disulfide bridge mediated by cysteine 574 is formed in the dimer of the 70-kDa heat shock protein

Journal of Biochemistry

Volumn 139, Issue 4, 2006, Pages 677-687

  Nemoto, Takayuki K ^a   Fukuma, Yutaka ^a   Itoh, Hideaki ^b   Takagi, Takashi ^c   Ono, Toshio ^a  

^a NAGASAKI UNIVERSITY GRADUATE SCHOOL OF BIOMEDICAL SCIENCES   (Japan)

^b AKITA UNIVERSITY   (Japan)

^c TOHOKU UNIVERSITY   (Japan)

Author keywords

Client binding; Dimer; Disulfide bridge; Hsp70; Lid

Indexed keywords

CYSTEINE; DIMER; DISULFIDE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70;

AMINO ACID ANALYSIS; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DIMERIZATION; ELECTROPHORETIC MOBILITY; HUMAN; HUMAN CELL; NONHUMAN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, GEL; CYSTEINE; DIMERIZATION; DISULFIDES; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HELA CELLS; HSP70 HEAT-SHOCK PROTEINS; HUMANS; IMMUNOBLOTTING; MOLECULAR WEIGHT; PLASMIDS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS;

EID: 33745667754     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvj071     Document Type: Article

References (29)

1. Xu, Z., Horwich, A.L., and Sigler, P.B. (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP) 7 chaperonin complex. Nature 388, 741-750
2. Minami, Y., Kimura, Y., Kawasaki, H., Suzuki, K., and Yahara, I. (1994) The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. Mol. Cell. Biol. 14, 1459-1464
3. Nemoto, T., Ohara-Nemoto, Y., Ota, M., Takagi, T., and Yokoyama, K. (1995) Mechanism of dimer formation of the 90-kDa heat-shock protein. Eur. J. Biochem 233, 1-8
4. Prodromou, C., Roe, S.M., O'Brien, R., Ladbury, J.E., Piper, P.W., and Pearl, L.H. (1997) Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90, 65-75
5. Prodromou, C., Roe, S.M., Piper, P.W., and Pearl, L.H. (1997) A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Nature Struct. Biol 4, 477-482
6. Stebbins, C.E., Russo, A.A., Schneider, C., Rosen, N., Hartl, F.U., and Pavletich, N.P. (1997) Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89, 239-250
7. Meyer, P., Prodromou, C., Hu, B., Vaughan, C., Roe, S.M., Panaretou, B., Piper, P.W., and Pearl, L.H. (2003) Structural and functional analysis of the middle segment of Hsp90: implications for ATP hydrolysis and client protein cochaperone interactions. Mol. Cell 11, 647-658
8. Welch, W.J. and Feramisco, J.R. (1982) Purification of the major mammalian heat shock proteins. J. Biol. Chem. 257, 14949-14959
9. Palleros, D.R., Reid, K.L., Shi, L., and Fink, A.L. (1993) DnaK ATPase activity revisited. FEBS Lett. 336, 124-128
10. Blond-Elguindi, S., Fourie, A.M., Sambrook, J.F., and Gething, M.-J., H. (1993) Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers. J. Biol. Chem. 268, 12730-12735
11. Azem, A., Oppliger, W., Lustig, A., Jeno, P., Feifel, B., Schatz, G., and Horst, M. (1997) The mitochondrial hsp70 chaperone system: effect of adenine nucleotides, peptide substrate, and mGrpE on the oligomeric state of mhsp70. J. Biol. Chem. 272, 20901-20906
12. Kim, D., Lee, Y.J., and Corry, P.M. (1992) Constitutive HSP70: oligomerization and its dependence on ATP binding. J. Cell Physiol. 153, 353-361
13. Chappell, T.G., Konforti, B.B., Schmid, S.L., and Rothman, J.E. (1987) The ATPase core of a clathrin uncoating protein. J. Biol. Chem. 262, 746-751
14. Stevens, S.Y., Cai S., Pellecchia, M., and Zuiderweg, E.R.P. (2003) The solution structure of the bacterial HSP70 chaperone protein domain DnaK (393-507) in complex with the peptide NRLLLTG. Prot. Sci. 12, 2588-2596
15. Burkholder, W.F., Zhao, X., Zhu, X., Hendrickson, W.A., Gragerov, A., and Gottesman, M.E. (1996) Mutations in the C-terminal fragment of DnaK affecting peptide binding. Proc. Natl. Acad. Sci. USA 93, 10632-10637
16. Takeda, S. and McKay, D.B. (1996) Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone. Biochemistry 35, 4636-4644
17. Wang, C. and Lee M.R. (1993) High-level expression of soluble rat hsc70 in Escherichia coli: purification and characterization of the cloned enzyme. Biochem. J. 294, 69-77
18. Flynn, G.C., Chappell, T.G., and Rothman, J.E. (1989) Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 245, 385-390
19. Benaroudj, N., Fouchaq, B., and 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
20. Fouchaq, B., Benaroudj, N., Ebel, C., and Ladjimi, M.M. (1999) Oligomerization of the 17-kDa peptide-binding domain of the molecular chaperone HSC70. Eur. J. Biochem. 259, 379-384
21. Wang, T.F., Chang, J.-H., and 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
22. Chou, C.-C., Forouhar, F., Yeh, Y.-H., Shr, H.-L., Wang, C., and Hsiao, C.-D. (2003) Crystal structure of the C-terminal 10-kDa subdomain of Hsc70. J. Biol. Chem. 278, 30311-30316
23. Hunt, C. and Morimoto, R.I. (1985) Conserved features of eukaryotic hsp90 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc. Natl. Acad. Sci. USA 82, 6455-6459
24. Milner, C.M. and Campbell, R.D. (1990) Structure and expression of the three MHC-linked HSP70 genes. Immunogenetics 32, 242-251
25. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
26. Nishihara, J., Ishibashi, T., Sakai, M., Nishi, S., Kumazaki, T., Hatanaka Y., Tsuda, S., and Hikichi, K. (1992) Characterization of cysteine residues of glutathione S-transferase P: evidence for steric hindrance of substrate binding by a bulky adduct to cysteine 47. Biochem. Biophys. Res. Commun. 188, 424-432
27. Nemoto, T., Ota, M., Ohara-Nemoto, Y., and Kaneko, M. (1995) Identification of dimeric structure of proteins by use of the glutathione S-transferase-fusion expression system. Anal. Biochem. 227, 396-399
28. Nemoto, T. and Sato, N. (1998) Oligomeric forms of the 90-kDa heat shock protein. Biochem. J. 330, 989-995
29. Ohno, M., Kitabatake, N., and Tani, F. (2004) Role of the C-terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activity. FEBS Lett. 576, 281-286