Interdomain communication in the molecular chaperone DnaK

Biochemical Journal

Volumn 369, Issue 3, 2003, Pages 627-634

  Han, Wanjiang ^a   Christen, Philipp ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

ATPase; GrpE; Heat shock protein 70 (Hsp70); Intrinsic fluorescence; Nucleotide

Indexed keywords

ESCHERICHIA COLI; FLUORESCENCE; SUBSTRATES;

PEPTIDE BINDING;

PROTEINS;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; LIGAND; PEPTIDE; PROTEIN DNAK; TRYPTOPHAN;

ARTICLE; ESCHERICHIA COLI; FLUORESCENCE; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; ESCHERICHIA COLI PROTEINS; FLUORESCENCE; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; KINETICS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0037330236     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020943     Document Type: Article

References (32)

1. Frydman, J. (2001) Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70, 603-647
2. Zhu, X., Zhao, X., Burkholder, W. F., Gragerov, A., Ogata, C. M., Gottesman, M. E. and Hendrickson, W. A. (1996) Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272, 1606-1614
3. 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
4. + but not ATP hydrolysis. Nature (London) 365, 664-666
5. Schmid, D., Baici, A., Gehring, H. and Christen, P. (1994) Kinetics of molecular chaperone action. Science 263, 971-973
6. McCarty, J. S., Buchberger, A., Reinstein, J. and Bukau, B. (1995) The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249, 126-137
7. Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C. and Zylicz, M. (1991) Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. U.S.A. 88, 2874-2878
8. Buchberger, A., Schröder, H., Büttner, M., Valencia, A. and Bukau, B. (1994) A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Nat. Struct. Biol. 1, 95-101
9. Schönfeld, H.-J., Schmidt, D., Schröder, H. and 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
10. Harrison, C. J., Hayer-Hartl, M., Liberto, M. D., Hartl, F.-U. and Kuriyan, J. (1997) Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Nature (London) 276, 431-435
11. Ziegelhoffer, T., Lopez-Buesa, P. and Craig, E. (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J. Biol. Chem. 270, 10412-10419
12. Karzai, A. W. and McMacken, R. (1996) A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein. J. Biol. Chem. 271, 11236-11246
13. Pierpaoli, E. V., Sandmeier, E., Baici, A., Schönfeld, H.-J., Gisler, S. and Christen, P. (1997) The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system. J. Mol. Biol. 269, 757-768
14. Pierpaoli, E. V., Sandmeier, E., Schönfeld, H.-J. and Christen, P. (1998) Control of the DnaK chaperone cycle by substoichiometric concentrations of the co-chaperones DnaJ and GrpE. J. Biol Chem. 273, 6643-6649
15. Grimshaw, J. P., JeLesarov, I., Schönfeld, H.-J. and Christen, P. (2001) Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system. J. Biol. Chem. 276, 2098-2104
16. Palleros, D. R., Reid, K. L., McCarty, J. S., Walker, G. C. and Fink, A. L. (1992) DnaK, hsp73, and their molten globules. Two different ways heat shock proteins respond to heat. J. Biol. Chem. 267, 5279-5285
17. Banecki, B., Zylicz, M., Bertoli, E. and Tanlani, F. (1992) Structural and functional relationships in DnaK and DnaK756 heat-shock proteins from Escherichia coli. J. Biol. Chem. 267, 25051-25058
18. Slepenkov, S. V. and Witt, S. N. (1998) Kinetics of the reactions of the Escherichia coli molecular chaperone DnaK with ATP: evidence that a three-step reaction precedes ATP hydrolysis. Biochemistry 37, 16749-16756
19. Feifel, B., Sandmeier, E., Schönfeld, H.-J. and Christen, P. (1996) Potassium ions and the molecular-chaperone activity of DnaK. Eur. J. Biochem. 237, 318-321
20. Hellebust, H., Uhlen, M. and Enfors, S. O. (1990) Interaction between heat shock protein DnaK and recombinant staphylococcal protein A. J. Bacteriol. 172, 5030-5034
21. Schönfeld, H.-J., Schmidt, D. and Zulauf, M. (1995) Investigation of the molecular chaperone DnaJ by analytical ultracentrifugation. Progr. Colloid Polym. Sci. 99, 7-10
22. Packschies, L., Theyssen, H., Buchberger, A., Bukau, B., Goody, R. S. and Reinstein, J. (1997) GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Biochemistry 36, 3417-3422
23. Mally, A. and Witt, S. N. (2001) GrpE accelerates peptide binding and release from the high affinity state of DnaK. Nat. Struct. Biol. 8, 254-257
24. Buchberger, A., Theyssen, H., Schröder, H., McCarty, J. S., Virgallita, G., Milkereit, P., Reinstein, J. and Bukau, B. (1995) Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. J. Biol. Chem. 270, 16903-16910
25. Jordan, R. and McMacken, R. (1995) Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins. J. Biol. Chem. 270, 4563-4569
26. Pierpaoli, E. V., Gisler, S. M. and Christen, P. (1998) Sequence-specific rates of interaction of target peptides with the molecular chaperones DnaK and DnaJ. Biochemistry 37, 16741-16748
27. Feifel, B., Schönfeld, H.-J. and Christen, P. (1998) D-peptide ligands for the co-chaperone DnaJ. J. Biol. Chem. 273, 11999-12002
28. Neidhardt, F. C., VanBogeler, R. A. and Vaughn, V. (1984) The genetics and regulation of heat-schock proteins. Annu. Rev. Genet. 18, 295-329
29. Theyssen, H., Schuster, H. P., Packschies, L., Bukau, B. and Reinstein, J. (1996) The second step of ATP binding to DnaK induces peptide release. J. Mol. Biol. 263, 657-670
30. Buczynski, G., Slepenkov, S. V., Sehorn, M. G. and Witt, S. N. (2001) Characterization of a lidless form of the molecular chaperone DnaK: deletion of the lid increases peptide on- and off-rate constants. J. Biol. Chem. 276, 27231-27236
31. Mayer, M. P., Schröder, H., Rudiger, S., Paal, K., Laufen. T. and Bukau, B. (2000) Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat. Struct. Biol. 7, 586-593
32. Pellecchia, M., Montgomery, D. L., Stevens, S. Y., Vander Kooi, C. W., Feng, H. P., Gierasch, L. M. and Zuiderweg, E. R. (2000) Structural insights into substrate binding by the molecular chaperone DnaK. Nat. Struct. Biol. 7, 298-303