The second metal-binding site of 70 kDa heat-shock protein is essential for ADP binding, ATP hydrolysis and ATP synthesis

Biochemical Journal

Volumn 378, Issue 3, 2004, Pages 793-799

  Wu, Xueji ^a   Yano, Mihiro ^a   Washida, Hiroyo ^a   Kido, Hiroshi ^a  

^a UNIVERSITY OF TOKUSHIMA   (Japan)

Author keywords

ATP hydrolysis; ATP synthesis; Calcium magnesium binding site; Chaperone; Nucleoside diphosphate kinase; Nucleotide binding

Indexed keywords

ADENOSINETRIPHOSPHATE; BIOSYNTHESIS; ENZYMES; HYDROLYSIS; PROTEINS;

CATALYTIC CENTRES;

BIOCHEMISTRY;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ASPARTIC ACID; GLUTAMIC ACID; HEAT SHOCK PROTEIN 70; HISTIDINE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; HUMAN; HYDROLYSIS; KINETICS; METAL BINDING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SYNTHESIS; SITE DIRECTED MUTAGENESIS;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; BINDING SITES; ESCHERICHIA COLI; HSP70 HEAT-SHOCK PROTEINS; HUMANS; HYDROLYSIS; METALS; MUTAGENESIS, SITE-DIRECTED; NUCLEOSIDE-DIPHOSPHATE KINASE; RECOMBINANT PROTEINS; TEMPERATURE;

EID: 1642464581     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031680     Document Type: Article

References (33)

1. Beckmann, R. P., Mizzen, L. E. and Welch, W. J. (1990) Interaction of Hsp70 with newly synthesized proteins: implications for protein folding and assembly. Science 248, 850-854
2. Kang, J., Ostermann, J., Shilling, J., Neupert, W., Craig, E. A. and Pfanner, N. (1990) Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature (London) 348, 137-143
3. Wagner, I., Arlt, H., van Dyck, L., Langer, T. and Neupert, W. (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J. 13, 5135-5145
4. Hartl, F.-U. (1996) Molecular chaperones in cellular protein folding. Nature (London) 381, 571-579
5. Bukau, B. and Norwich, A. L (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366
6. Blond-Elguindi, S., Fourie, A. M., Sambrook, J. F. and Gething, M. J. (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
7. Freeman, B. C., Myers, M. P., Schumacher, R. and 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
8. Harrison, C. J., Hayer-Hartl, M., Di Liberto, M., Hartl, F. and Kuriyan, J. (1997) Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276, 431-435
9. Hiromura, M., Yano, M., Mori, H., Inoue, M. and Kido, H. (1998) Intrinsic ADP-ATP exchange activity is a novel function of the molecular chaperone, Hsp70. J. Biol. Chem. 273, 5435-5438
10. Müller-Dieckmann, H. J. and Schulz, G. E. (1995) Substrate specificity and assembly of the catalytic center derived from two structures of ligated uridylate kinase. J. Mol. Biol. 246, 522-530
11. Mathews, I. I., Erion, M. D. and Ealick, S. E. (1998) Structure of human adenosine kinase at 1.5 Å resolution. Biochemistry 37, 15607-15620
12. Berry, M. B., Meador, B., Bilderback, T., Liang, P., Glaser, M. and Phillips, Jr, G. N. (1994) The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP. Proteins 19, 183-198
13. Marcu, M. G., Chadli, A., Bouhouche, I., Catelli, M. and Neckers, L. M. (2000) The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone. J. Biol. Chem. 275, 37181-37186
14. Sriram, M., Osipiuk, J., Freeman, B., Morimoto, R. I. and Joachimiak, A. (1997) Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain. Structure 5, 403-414
15. Barthel, T. K. and Walker, G. C. (1999) Inferences concerning the ATPase properties of DnaK and other HSP70s are affected by the ADP kinase activity of copurifying nucleoside-diphosphate kinase. J. Biol. Chem. 274, 36670-36678
16. Leung, S. M. and Hightower, L. E. (1997) A 16-kDa protein functions as a new regulatory protein for Hsc70 molecular chaperone and is identified as a member of the Nm23/nucleoside diphosphate kinase family. J. Biol. Chem. 272, 2607-2614
17. Hunt, C. and Morimoto, R. I. (1985) Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc. Natl. Acad. Sci. U.S.A. 82, 6455-6459
18. Yano, M., Mori, S., Niwa, Y., Inoue, M. and Kido, H. (1997) Intrinsic nucleoside diphosphate kinase-like activity as a novel function of 14-3-3 proteins. FEBS Lett 419, 244-248
19. Schmid, D., Baici, A., Gehring, H. and Christen, P. (1994) Kinetics of molecular chaperone action. Science 263, 971-973
20. Ohtsuki, K., Yokoyama, M., Koike, T. and Ishida, N. (1984) Nucleosidediphosphate kinase in Escherichia coli: its polypeptide structure and reaction intermediate. Biochem. Int. 8, 715-723
21. Ohtsuki, K. and Yokoyama, M. (1987) Direct activation of guanine nucleotide binding proteins through a high-energy phosphate-transfer by nucleoside diphosphate-kinase. Biochem. Biophys. Res. Commun. 148, 300-307.
22. Erent, M., Gonin, P., Cherfils, J., Tissier, P., Raschella, G., Giartosio, A., Agou, F., Sarger, C., Lacombe, M. L., Konrad, M. and Lascu, I. (2001) Structural and catalytic properties and homology modelling of the human nucleoside diphosphate kinase C, product of the DRnm23 gene. Eur. J. Biochem. 268, 1972-1981
23. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
24. Kido, H., Vita, A. and Horecker, B. L. (1985) Ligand binding to proteins by equilibrium gel penetration. Methods Enzymol. 117, 342-346
25. Muñoz-Dorado, J., Inouye, S. and Inouye, M. (1990) Nucleoside diphosphate kinase from Myxococcus xanthus. II. Biochemical characterization. J. Biol. Chem. 265, 2707-2712
26. McCarty, J. S. and Walker, G. C. (1991) DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity. Proc. Natl. Acad. Sci. U.S.A. 88, 9513-9517
27. O'Brien, M. C., Flaherty, K. M. and McKay, D. B. (1996) Lysine 71 of the chaperone protein Hsc70 is essential for ATP hydrolysis. J. Biol. Chem. 271, 15874-15878
28. Rajapandi, T., Wu, C., Eisenberg, E. and Greene, L. (1998) Characterization of D10S and K71E mutants of human cytosolic Hsp70. Biochemistry 37, 7244-7250
29. Schlossman, D. M., Schmid, S. L., Braell, W. A. and Rothman, J. E. (1984) An enzyme that removes Clathrin coats: purification of an uncoating ATPase. J. Cell Biol. 99, 723-733
30. Osipiuk, J., Walsh, M. A., Freeman, B. C., Morimoto, R. I. and Joachimiak, A. (1999) Structure of a new crystal form of human Hsp70 ATPase domain. Acta. Crystallogr. D Biol. Crystallogr. 55, 1105-1107
31. Rose, T., Sebo, P., Bellalou, J. and Ladant, D. (1995) Interaction of calcium with Bordetella pertussis adenylate cyclase toxin. Characterization of multiple calcium-binding sites and calcium-induced conformational changes. J. Biol. Chem. 270, 26370-26376
32. Palleros, D. R., Shi, L., Reid, K. L. and Fink, A. L. (1994) Hsp70-protein complexes. Complex stability and conformation of bound substrate protein. J. Biol. Chem. 269, 13107-13114
33. Sadis, S. and Hightower, L. E. (1992) Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange. Biochemistry 31, 9406-9412