Molecular characterization, expression pattern and function analysis of the OsHSP90 family in rice

References

• Frydman J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu Rev Biochem. 2001;70:603–647.
   PubMed Web of Science ®Google Scholar
• Young JC, Moarefi I, Hartl FU. Hsp90: a specialized but essential protein-folding tool. J Cell Biol. 2001;154:267–273.
   PubMed Web of Science ®Google Scholar
• Picard D. Heat-shock protein 90, a chaperone for folding and regulation. Cell Mol Life Sci. 2002;59:1640–1648.
   PubMed Web of Science ®Google Scholar
• Wegele H, Muller L, Buchner J. Hsp70 and Hsp90–a relay team for protein folding. Rev Physiol Biochem Pharmacol. 2004;151:1–44.
   PubMed Web of Science ®Google Scholar
• Balch WE, Morimoto RI, Dillin A, et al. Adapting proteostasis for disease intervention. Science. 2008;319:916–919.
   PubMed Web of Science ®Google Scholar
• Hartl FU, Hayer-Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol. 2009;16:574–581.
   PubMed Web of Science ®Google Scholar
• Doyle SM, Shorter J, Zolkiewski M, et al. Asymmol/letric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity. Nat Struct Mol Biol. 2007;14:114–122.
   PubMed Web of Science ®Google Scholar
• Pearl LH, Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem. 2006;75:271–294.
   PubMed Web of Science ®Google Scholar
• Taipale M, Jarosz DF, Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol. 2010;11:515–528.
   PubMed Web of Science ®Google Scholar
• Pratt WB, Morishima Y, Osawa Y. The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts. J Biol Chem. 2008;283:22885–22889.
   PubMed Web of Science ®Google Scholar
• Riggs DL, Cox MB, Cheung-Flynn J, et al. Functional specificity of co-chaperone interactions with Hsp90 client proteins. Crit Rev Biochem Mol Biol. 2004;39:279–295.
   PubMed Web of Science ®Google Scholar
• Wandinger SK, Richter K, Buchner J. The Hsp90 chaperone machinery. J Biol Chem. 2008;283:18473–18477.
   PubMed Web of Science ®Google Scholar
• Richter K, Buchner J. Hsp90: chaperoning signal transduction. J Cell Physiol. 2001;188:281–290.
   PubMed Web of Science ®Google Scholar
• Pratt WB, Krishna P, Olsen LJ. Hsp90-binding immunophilins in plants: the protein movers. Trends Plant Sci. 2001;6:54–58.
   PubMed Web of Science ®Google Scholar
• Krishna P, Gloor G. The Hsp90 family of proteins in Arabidopsis thaliana. Cell Stress Chaperones. 2001;6:238–246.
   PubMed Web of Science ®Google Scholar
• Milioni D, Hatzopoulos P. Genomic organization of hsp90 gene family in Arabidopsis. Plant Mol Biol. 1997;35:955–961.
   PubMed Web of Science ®Google Scholar
• Mishra SK, Tripp J, Winkelhaus S, et al. In the complex family of heat stress transcription factors, HsfA1 has a unique role as master regulator of thermotolerance in tomato. Genes Dev. 2002;16:1555–1567.
   PubMed Web of Science ®Google Scholar
• Kotak S, Port M, Ganguli A, et al. Characterization of C-terminal domains of Arabidopsis heat stress transcription factors (Hsfs) and identification of a new signature combination of plant class A Hsfs with AHA and NES motifs essential for activator function and intracellular localization. Plant J. 2004;39:98–112.
   PubMed Web of Science ®Google Scholar
• Nover L, Bharti K, Doring P, et al. Arabidopsis and the heat stress transcription factor world: how many heat stress transcription factors do we need? Cell Stress Chaperones. 2001;6:177–189.
   PubMed Web of Science ®Google Scholar
• Baniwal SK, Bharti K, Chan KY, et al. Heat stress response in plants: a complex game with chaperones and more than twenty heat stress transcription factors. J Biosci. 2004;29:471–487.
   PubMed Web of Science ®Google Scholar
• Hahn A, Bublak D, Schleiff E, et al. Crosstalk between Hsp90 and Hsp70 chaperones and heat stress transcription factors in tomato. Plant Cell. 2011;23:741–755.
   PubMed Web of Science ®Google Scholar
• Takahashi A, Casais C, Ichimura K, et al. HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis. Proc Natl Acad Sci USA. 2003;100:11777–11782.
   PubMed Web of Science ®Google Scholar
• Hubert DA, Tornero P, Belkhadir Y, et al. Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein. EMBO J. 2003;22:5679–5689.
   PubMed Web of Science ®Google Scholar
• Liu Y, Burch-Smith T, Schiff M, et al. Molecular chaperone Hsp90 associates with resistance protein N and its signaling proteins SGT1 and Rar1 to modulate an innate immune response in plants. J Biol Chem. 2004;279:2101–2108.
   PubMed Web of Science ®Google Scholar
• Sangster TA, Queitsch C. The HSP90 chaperone complex, an emerging force in plant development and phenotypic plasticity. Curr Opin Plant Biol. 2005;8:86–92.
   PubMed Web of Science ®Google Scholar
• Kitagawa K, Skowyra D, Elledge SJ, et al. SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex. Mol Cell. 1999;4:21–33.
   PubMed Web of Science ®Google Scholar
• Rutherford SL, Lindquist S. Hsp90 as a capacitor for morphological evolution. Nature. 1998;396:336–342.
   PubMed Web of Science ®Google Scholar
• Queitsch C, Sangster TA, Lindquist S. Hsp90 as a capacitor of phenotypic variation. Nature. 2002;417:618–624.
   PubMed Web of Science ®Google Scholar
• Wang W, Vinocur B, Shoseyov O, et al. Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response. Trends Plant Sci. 2004;9:244–252.
   PubMed Web of Science ®Google Scholar
• Skantar AM, Carta LK. Molecular characterization and phylogenetic evaluation of the hsp90 gene from selected nematodes. J Nematol. 2004;36:466–480.
   PubMed Web of Science ®Google Scholar
• Chen B, Piel WH, Gui L, et al. The HSP90 family of genes in the human genome: insights into their divergence and evolution. Genomics. 2005;86:627–637.
   PubMed Web of Science ®Google Scholar
• Wang GF, Wei X, Fan R, et al. Molecular analysis of common wheat genes encoding three types of cytosolic heat shock protein 90 (Hsp90): functional involvement of cytosolic Hsp90s in the control of wheat seedling growth and disease resistance. New Phytol. 2011;191:418–431.
   PubMed Web of Science ®Google Scholar
• Thompson JD, Gibson TJ, Plewniak F, et al. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 1997;25:4876–4882.
   PubMed Web of Science ®Google Scholar
• Tamura K, Dudley J, Nei M, et al. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol Biol Evol. 2007;24:1596–1599.
   PubMed Web of Science ®Google Scholar
• Yoshida S, Forno DA, Cook JH, et al. Laboratory manual for physiological studies of rice. Manila: International Rice Research Institute; 1976. pp. 61–67.
   Google Scholar
• Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) ethod. Methods. 2001;25:402–408.
   PubMed Web of Science ®Google Scholar
• LaVallie ER, DiBlasio EA, Kovacic S, et al. A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm. Biotechnology (N Y). 1993;11:187–193.
   PubMedGoogle Scholar
• Wang X, Shi X, Hao B, et al. Duplication and DNA segmental loss in the rice genome: implications for diploidization. New Phytol. 2005;165:937–946.
   PubMed Web of Science ®Google Scholar
• Kong H, Landherr LL, Frohlich MW, et al. Patterns of gene duplication in the plant SKP1 gene family in angiosperms: evidence for multiple mechanisms of rapid gene birth. Plant J. 2007;50:873–885.
   PubMed Web of Science ®Google Scholar
• Feder ME, Hofmann GE. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu Rev Physiol. 1999;61:243–282.
   PubMed Web of Science ®Google Scholar
• Cabiscol E, Piulats E, Echave P, et al. Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. J Biol Chem. 2000;275:27393–27398.
   PubMed Web of Science ®Google Scholar
• Kohanski MA, Dwyer DJ, Hayete B, et al. A common mechanism of cellular death induced by bactericidal antibiotics. Cell. 2007;130:797–810.
   PubMed Web of Science ®Google Scholar