Expression of five AtHsp90 genes in Saccharomyces cerevisiae reveals functional differences of AtHsp90s under abiotic stresses

Journal of Plant Physiology

Volumn 167, Issue 14, 2010, Pages 1172-1178

  Song, Hongmiao ^a,b   Fan, Pengxiang ^a   Shi, Wuliang ^a   Zhao, Rongmin ^c   Li, Yinxin ^a  

^a INSTITUTE OF BOTANY   (China)

^b INSTITUTE OF PLANT PROTECTION AND MICROBIOLOGY   (China)

^c UNIVERSITY OF TORONTO   (Canada)

Author keywords

Abiotic stress; Arabidopsis thaliana; Cofactors; Functional expression; Heat shock protein 90; Saccharomyces cerevisiae

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; SACCHAROMYCES CEREVISIAE;

ARABIDOPSIS PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PROTEIN BINDING;

GENETICS; GROWTH, DEVELOPMENT AND AGING; METABOLISM; SACCHAROMYCES CEREVISIAE; TWO HYBRID SYSTEM;

ARABIDOPSIS PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 77955055168     PISSN: 01761617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jplph.2010.03.016     Document Type: Article

References (24)

1. 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 1989, 9:3919-3930.
2. Cao D.S., Forehlich J.E., Zhang H., Cheng C.L. The chlorate-resistant and photomorphogenesis- defective mutant cr88 encodes a chloroplast-targeted Hsp90. Plant J 2003, 33:107-118.
3. Cha J.Y., Ermawati N., Jung M.H., Su'udi M., Kim K.Y., Kim J.Y., Han C.D., Lee K.H., Son D. Characterization of orchardgrass p23, a flowering plant Hsp90 cohort protein. Cell Stress Chaperones 2009, 14:233-243.
4. Ishiguro S., Watanabe Y., Ito N., Nonaka H., Takeda N., Sakai T., Kanaya H., Okada K. SHEPHERD is the Arabidopsis GRP94 responsible for the formation of functional CLAVATA proteins. EMBO J 2002, 21:898-908.
5. Kimura Y., Matsumoto S., Yahara I. Temperature-sensitive mutants of Hsp82 of the budding yeast Saccharomyces cerevisiae. Mol Gen Genet 1994, 242:517-527.
6. Krishna P., Gloor G. The Hsp90 family of proteins in Arabidopsis thaliana. Cell Stress Chaperones 2001, 6:238-246.
7. Krishna P., Zhang Z.M. Plant hsp90 chaperone system: the p23 surprise!. Am Soc Plant Biologists 2003.
8. McLaughlin S.H., Sobott F., Yao Z.P., Zhang W., Nielsen P.R., Grossmann J.G., Laue E.D., Robinson C.V., Jackson S.E. The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins. J Mol Biol 2006, 356:746-758.
9. Meyer P., Prodromou C., Hu B., Vaughan C., Roe S.M., Panaretou B., Piper P.W., Pearl L.H. Structural and functional analysis of the middle segment of Hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol Cell 2003, 11:647-658.
10. Milioni D., Hatzopoulos P. Genomic organization of Hsp90 gene family in Arabidopsis. Plant Mol Biol 1997, 35:955-961.
11. Nathan D.F., Lindquist S. Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol Cell Biol 1995, 15:3917-3925.
12. Nathan D.F., Vos M.H., Lindquist S. In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc Natl Acad Sci U S A 1997, 94:12949-12956.
13. Piper P.W., Panaretou B., Millson S.H., Truman A., Mollapour M., Pearl L.H., Prodromou C. Yeast is selectively hypersensitised to heat shock protein 90 (Hsp90)-targetting drugs with heterologous expression of the human Hsp90β, a property that can be exploited in screens for new Hsp90 chaperone inhibitors. Gene 2003, 302:165-170.
14. Prassinos C., Haralampidis K., Milioni D., Samakovli D., Krambis K., Hatzopoulos P. Complexity of Hsp90 in organelle targeting. Plant Mol Biol 2008, 67:323-334.
15. Pratt W.B., Toft D.O. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med 2003, 228:111-133.
16. Queitsch C., Sangster T.A., Lindquist S. Hsp90 as a capacitor of phenotypic variation. Nature 2002, 417:618-625.
17. Samakovli D., Thanou A., Valmas C., Hatzopoulos P. Hsp90 canalizes developmental perturbation. J Exp Bot 2007, 58:3513-3524.
18. Sangster T.A., Bahrami A., Wilczek A., Watanabe E., Schellenberg K., McLellan C., Kelley A., Kong S.W., Queitsch C., Lindquist S. Phenotypic diversity and altered environmental plasticity in Arabidopsis thaliana with reduced Hsp90 levels. PLoS ONE 2007, 7:1-14.
19. Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., Hartl F.U., Moarefi I. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 2000, 101:199-210.
20. Shiau A.K., Harris S.F., Southworth D.R., Agard D.A. Structural analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell 2006, 127:329-340.
21. Taylor P., Dornan J., Carrello A., Minchin R.F., Thomas R., Walkinshaw M.D. Two structures of Cyclophilin 40: folding and fidelity in the TPR domains. Structure 2001, 9:431-438.
22. Uetz P., Giot L., Cagney G., Mansfield T.A., Judson R.S., Knight J.R., Lockshon D., Narayan V., Srinivasan M., Pochart P., Qureshi-Emil A., Li Y., Godwin B., Conover D., Kalbfleisch T., Vijayadamodar G., Yang M., Johnston M., Fields S., Rothberg J.M. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 2000, 403:623-627.
23. Wang W.X., Vinocur B., Shoseryov O., Altman A. Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response. Trends Plant Sci 2004, 9:244-252.
24. Zhao R.M., Davey M., Hsu Y.C., Kaplanek P., Tong A., Parsons A.B., Krogan N., Cagney G., Mai D., Greenblatt J., Boone C., Emili A., Houry W.A. Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the Hsp90 chaperone. Cell 2005, 120:715-727.