Expression and crystallization of the yeast Hsp82 chaperone, and preliminary X-ray diffraction studies of the amino-terminal domain

Proteins: Structure, Function and Genetics

Volumn 25, Issue 4, 1996, Pages 517-522

  Prodromou, Chrisostomos ^a   Piper, Peter W ^a   Pearl, Laurence H ^a  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

crystallization; Hsp (heat shock protein); overexpression; Saccharomyces cerevisiae

Indexed keywords

CHAPERONE;

AMINO TERMINAL SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; ENANTIOMER; PRIORITY JOURNAL; PROTEIN EXPRESSION; SACCHAROMYCES CEREVISIAE; STRAIN DIFFERENCE; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; CLONING, MOLECULAR; ESCHERICHIA COLI; HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; X-RAY DIFFRACTION;

SACCHAROMYCES CEREVISIAE;

EID: 0029797764     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199608)25:4<517::AID-PROT13>3.0.CO;2-K     Document Type: Article

References (33)

1. Kelley, P.M., Schlessinger, M.J. Antibodies to two major chicken heat shock proteins cross-react with similar proteins in widely divergent species. Mol. Cell Biol. 2:267-274, 1982.
2. Welch, W.J., Feramisco, J.R. Purification of the major mammalian heat shock proteins. J. Biol. Chem. 257:4949-4959, 1982.
3. Lindquist, S., Craig, E.A. The heat shock proteins. Annu. Rev. Genet. 22:631-677, 1988.
4. Gething, M.J., Sambrook, J. Protein folding in the cell. Nature 355:33-45, 1992.
5. Borkovich, K.A., Farrelly, F.W., Finkelstein, D.B., Taulien, J., Lindquist, S. Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol. Cell. Biol. 9:3919-3930, 1989.
6. Wiech, H., Buchner J., Zimmermann, R., Jakob, U. HSP90 chaperones protein folding in vitro. Nature 358:169-170, 1992.
7. src with the cellular proteins PP50 and PP90. Curr. Top. Microbiol. Immunol. 123:1-23, 1983.
8. Matts, R.L., Hurst, R. Evidence for the association of the heme-regulated eIF-2α kinase with the 90-kDa heat shock protein in rabbit reticulocyte lysate in situ. J. Biol. Chem. 264:15542-15547, 1989.
9. Miyata, Y., Yahara, Y. The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. J. Biol. Chem. 267:7042-7047, 1992.
10. Rose, D.W., Wettenhall, R.E.H., Kudicki, W., Kramer, G., Hardesty, B. The 90-kilodalton peptide of the heme-regulated eIF-2α kinase has sequence similarity with the 90-kilodalton heat shock protein. Biochemistry 26:6583-6587, 1987.
11. Ziemieck, A., Catelli, M-G., Joab, I., Moncharmont, B. Association of the heat shock protein HSP90 with steroid hormone receptors and tyrosine kinase oncogene products. Biochem. Biophys. Res. Commun. 138:1298-1307, 1986.
12. v-src. J. Biol. Chem. 260:14292-14296, 1985.
13. src, and two cellular proteins. Cell 25:363-372, 1981.
14. Brugge, J.S., Yuonemoto, W., and Darrow, D. Interaction between the Rous sarcoma virus transforming protein and two cellular phosphoproteins: analysis of the turnover and distribution of this complex. Mol. Cell. Biol. 4:2697-2704, 1983.
15. Aligue, R., Akhavannik, H., Russell, P. A role for HSP90 in cell-cycle control: wee1 tyrosine kinase activity requires interaction with HSP90. EMBO J. 13:6099-6106, 1994.
16. Dougherty, J.J., Rabideau, D.A., Iannotti, A.M., Sullivan, W.P., Toft, D.O. Identification of the 90 kDa substrate of rat liver type II casein kinase with the heat shock protein which binds steroid receptors. Biochem. Biophys. Acta 927: 74-80, 1987.
17. Walker, A.I., Hunt, T., Jackson, R.J., Anderson, C.W. Double-stranded DNA induces the phosphorylation of several proteins including the 90,000 mol. wt. heat-shock protein in animal cell extracts. EMBO J. 4:139-145, 1985.
18. Catelli, M.G., Binart, N., Jung-Testas, I., Renoir, J.-M., Baulieu, E.-E., Feramisco, J.R., Welch, W.J. The common 90-kD protein component of non-transformed '8S' steroid receptors is a heat shock protein. EMBO J. 4:3131-3135, 1985.
19. Sanchez, E.R., Toft, D.O., Schlesinger, M.J., Pratt, W.B. Evidence that the 90-kDa phosphoprotein associated with untransformed L-cell glucocorticoid receptor is a murine heat shock protein. J. Biol. Chem. 260:12398-12401, 1985.
20. Jakob, U., Buchner, J. Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones. TIBS 19: 205-211, 1994.
21. Nishida, E., Koyasu, S., Sakai, H., Yahara, I. Calmodulin-regulated binding of the 90-kDa heat shock protein to actin filaments. J. Biol. Chem. 261:16033-16036, 1986.
22. Miniami, Y., Kawasaki, H., Suzuki, K., Yahara, I. The calmodulin-binding domain of the mouse 90-kDa heat shock protein. J. Biol. Chem. 268:9604-9610, 1993.
23. Koyasu, S., Nishada, E., Kadowaki, T., Matsuzaki, F., Harada, F., Kasuga, M., Sakai, H., Yahara, I. Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins. Proc. Natl. Acad. Sci. U.S.A. 83: 8054-8058, 1986.
24. Sanchez, E.R., Redmond, T., Scherrer, L.C., Pratt, W.B. Evidence that the 90-kilodalton heat shock protein is associated with tubulin-containing complexes in L-cell cytosol and in intact PtK cells. Mol. Endocrinol. 2:756-760, 1980.
25. Pratt, W.B. The role of heat-shock proteins in regulating the function, folding and trafficking of the glucocorticoid receptor. J. Biol. Chem. 268:21455-21458, 1993.
26. Smith, D.F. Dynamics of heat-shock protein 90-progesterone receptor-binding and the disactivation loop model for steroid-receptor complexes. Mol. Endocrinol. 7:1418-1429, 1993.
27. Tai, P.-K.K., Chang, H., Albers, M.W., Schreiber, S.L., Toft, D.O., Faber, L.E. P59 (FK506 binding protein 59) interaction with heat shock proteins is highly conserved and may involve proteins other than steroid receptors. Biochemistry 32:8842-8847, 1993.
28. Cheng, L., Hirst, K., Piper, P.W. Authentic temperature-regulation of a heat shock gene inserted into yeast on a high copy number vector. Influences of overexpression of Hsp90 protein on high temperature growth and thermotolerance. Biochem. Biophys. Acta 1132:26-34, 1992.
29. Chayen, N.E., Shaw Stewart, P.D., Maeder, D.L., Blow, D.M. An automated system for microbatch protein crystallization and screening. J. Appl. Crystallogr. 23:297-302, 1990.
30. Jancarik, J., Kim, S.-H. Spares matrix sampling: A screening method for crystallization of proteins. J. Appl. Crystallogr. 24:409-411, 1991.
31. Leslie, A.G.W. "MOSFLM Users Guide." Cambridge, UK: MRC-LMB, 1995.
32. Collaborative Computational Project No. 4. Acta Crystallogr. D50:760-763, 1994.
33. Chayen, N.E., Radcliffe, J.W., Blow, D.M. Control of nucleation in the crystallization of lysozyme. Protein Sci. 2:113-118, 1993.