Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies

Journal of Molecular Biology

Volumn 285, Issue 3, 1999, Pages 903-907

  Maruya, Mikako ^a   Sameshima, Masazumi ^a   Nemoto, Takayuki ^b   Yahara, Ichiro ^a  

^a TOKYO METROPOLITAN INSTITUTE OF MEDICAL SCIENCE   (Japan)

^b IWATE MEDICAL UNIVERSITY   (Japan)

Author keywords

Dimer structure; Electron microscopy; HSP90; Molecular image; Monoclonal antibodies

Indexed keywords

DIMER; HEAT SHOCK PROTEIN 90; MONOCLONAL ANTIBODY;

AMINO TERMINAL SEQUENCE; ANTIGEN BINDING; ARTICLE; CARBOXY TERMINAL SEQUENCE; ELECTRON MICROSCOPY; HUMAN; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE;

EID: 0033593528     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2349     Document Type: Article

References (23)

1. Borkovich K. A., Farrelly F. W., Finkelstein D. B., Taulien J., Lindquist S. Hsp82 is an essential protein that is required in higher concentration for growth of cells at higher temperatures. Mol. Cell. Biol. 9:1989;3919-3930.
2. Csermely P., Kajtar J., Hollosi M., Jalsovszky G., Holly S., Kahn C. R., Gergely P. Jr., Soti C., Mihaly K., Somogy J. ATP induces a conformational change of the 90-kDa heat shock protein (hsp90). J. Biol. Chem. 268:1993;1901-1907.
3. Csermely P., Schnaider T., Soti C., Prohaszka Z., Nardai G. The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol. Ther. 79:1998;129-168.
4. Cutforth T., Rubin G. M. Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. Cell. 77:1994;1027-1036.
5. Freeman B. C., Morimoto R. I. 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. 15:1996;2969-2979.
6. Grenert J. P., Sullivan W. P., Fadden P., Haystead T. A. J., Clark J., Mimnaught E., Krutzsch H., Ochel H.-J., Schulte T. W., Sausville E., Neckers L. M., Toft D. O. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation. J. Biol. Chem. 272:1997;23843-23850.
7. Johnson J. L., Toft D. O. A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23. J. Biol. Chem. 269:1994;24989-24993.
8. Koyasu S., Nishida E., Kadowaki T., Matsuzaki F., Iida K., Harada F., Kasuga M., Sakai H., Yahara I. Two mammalian heat shock proteins, HSP90 and HSP100, are actin binding proteins. Proc. Natl Acad. Sci. USA. 83:1986;8054-8058.
9. Meng X., Devin J., Sullivan W. P., Toft D., Baulieu E.-E., Catelli M.-G. Mutational analysis of Hsp90α dimerization and subcellular localization: dimer disruption does not impede 'in vivo' interaction with estrogen receptor. J. Cell Sci. 109:1996;1677-1687.
10. Minami Y., Kawasaki H., Miyata Y., Suzuki K., Yahara I. Analysis of native forms and their isoform compositions of mouse 90-kDa heat shock protein, HSP90. J. Biol. Chem. 266:1991;10099-10103.
11. Minami Y., Kimura Y., Kawasaki H., Suzuki K., Yahara I. The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. Mol. Cell. Biol. 14:1994;1459-1464.
12. Miyata Y., Yahara I. The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. J. Biol. Chem. 267:1992;7042-7047.
13. Nemoto T., Ohara-Nemoto Y., Ota M., Takagi T., Yokoyama K. Mechanism of dimer formation of the 90-kDa heat-shock protein. Eur. J. Biochem. 233:1995;1-8.
14. Nemoto T., Sato N., Iwanari H., Yamashita H., Takagi T. Domain structures and immunogenic regions of the 90-kDa heat-shock protein (HSP90). J. Biol. Chem. 272:1997;26179-26187.
15. Pratt W. B. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J. Biol. Chem. 268:1993;21455-21458.
16. Prodromou C., Roe S. M., Piper P. W., Pearl L. H. A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Nature Struct. Biol. 4:1997a;477-482.
17. Prodromou C., Roe S. M., O'Brien R., Ladbury J. E., Piper P. W., Pearl L. H. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell. 90:1997b;65-75.
18. Scheibel T., Neuhofen S., Weikl T., Mayr C., Reinsterin J., Vogel P. D., Buchner J. ATP-binding properties of human Hsp90. J. Biol. Chem. 272:1997;18608-18613.
19. Scheibel T., Weiki T., Buchner J. Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence. Proc. Natl Acad. Sci. USA. 95:1998;1495-1499.
20. Stebbins C. E., Russo A. A., Schneider C., Rosen N., Hartl F. U., Pavietich N. P. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell. 89:1997;239-250.
21. Wiech H., Buchner J., Zimmermann R., Jakob U. Hsp90 chaperones protein folding in vitro. Nature. 358:1992;169-170.
22. Yonehara M., Minami Y., Kawata Y., Nagai J., Yahara I. Heat-induced chaperone activity of HSP90. J. Biol. Chem. 271:1996;2641-2645.
23. Yonezawa N., Nishida E., Sakai H., Koyasu S., Matsuzaki F., Iida K., Yahara I. Purification and characterization of the 90-kDa heat shock protein from mammalian tissues. Eur. J. Biochem. 177:1988;1-7.