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Volumn 474, Issue 1-2, 2011, Pages 29-38

Molecular characterization and expression of a gene encoding cytosolic Hsp90 from Pennisetum glaucum and its role in abiotic stress adaptation

Author keywords

Chaperone activity; Heat stress cDNA library; Heterologous expression; Homology modeling; Phylogenetic analysis; Real time PCR

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID; AMINO ACID DERIVATIVE; CHAPERONE; COMPLEMENTARY DNA; HEAT SHOCK PROTEIN 90; METHIONYLGLUTAMYLGLUTAMYLVALYLASPARTIC ACID; POLYPEPTIDE; PROTEIN; RECOMBINANT HEAT SHOCK PROTEIN 90; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 79952004351     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2010.12.004     Document Type: Article
Times cited : (37)

References (39)
  • 1
    • 33646176246 scopus 로고    scopus 로고
    • Crystal structure of an HSP90-nucleotide-p23/Sba1 closed chaperone complex
    • Ali M.M., Roe S.M., Vaughan C.K., Meyer P., Panaretou B., Piper P.W., et al. Crystal structure of an HSP90-nucleotide-p23/Sba1 closed chaperone complex. Nature 2006, 440:1013-1017.
    • (2006) Nature , vol.440 , pp. 1013-1017
    • Ali, M.M.1    Roe, S.M.2    Vaughan, C.K.3    Meyer, P.4    Panaretou, B.5    Piper, P.W.6
  • 2
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 3
    • 0024519049 scopus 로고
    • The cDNA-derived amino acid sequence of chick heat shock protein Mr 90 000 (HSP90) reveals a "DNA like" structure: potential site of interaction with steroid receptors
    • Binart N., Chambraud B., Dumas B., Rowland D.A., Bigogne C., Levin J.M., et al. The cDNA-derived amino acid sequence of chick heat shock protein Mr 90 000 (HSP90) reveals a "DNA like" structure: potential site of interaction with steroid receptors. Biochem. Biophys. Res. Commun. 1989, 159:140-147.
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 140-147
    • Binart, N.1    Chambraud, B.2    Dumas, B.3    Rowland, D.A.4    Bigogne, C.5    Levin, J.M.6
  • 4
    • 0024421221 scopus 로고
    • Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
    • 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.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farrelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 5
    • 0031943566 scopus 로고    scopus 로고
    • Analysis of chaperone function using citrate synthase as nonnative substrate protein
    • Buchner J., Grallert H., Jakob U. Analysis of chaperone function using citrate synthase as nonnative substrate protein. Methods Enzymol. 1998, 290:323-338.
    • (1998) Methods Enzymol. , vol.290 , pp. 323-338
    • Buchner, J.1    Grallert, H.2    Jakob, U.3
  • 6
    • 33746660802 scopus 로고    scopus 로고
    • Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms
    • Chen B., Zhong D., Monteiro A. Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms. BMC Genomics 2006, 7:156. 10.1186/1471-2164-7-156.
    • (2006) BMC Genomics , vol.7 , pp. 156
    • Chen, B.1    Zhong, D.2    Monteiro, A.3
  • 7
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 1987, 162:156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 8
    • 34948893963 scopus 로고    scopus 로고
    • Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones
    • Dollins D.E., Warren J.J., Immormino R.M., Gewirth D.T. Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones. Mol. Cell 2007, 28:41-56.
    • (2007) Mol. Cell , vol.28 , pp. 41-56
    • Dollins, D.E.1    Warren, J.J.2    Immormino, R.M.3    Gewirth, D.T.4
  • 9
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: the role of molecular chaperones
    • Frydman J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 2001, 70:603-647.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 10
    • 0242556837 scopus 로고    scopus 로고
    • Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein
    • Hubert D.A., Tornero P., Belkhadir Y., Krishna P., Takahashi A., Shirasu K., et al. Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein. EMBO J. 2003, 22:5679-5689.
    • (2003) EMBO J. , vol.22 , pp. 5679-5689
    • Hubert, D.A.1    Tornero, P.2    Belkhadir, Y.3    Krishna, P.4    Takahashi, A.5    Shirasu, K.6
  • 11
    • 58149271606 scopus 로고    scopus 로고
    • Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms
    • Johnson J.L., Brown C. Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms. Cell Stress Chaperones 2009, 14:83-94.
    • (2009) Cell Stress Chaperones , vol.14 , pp. 83-94
    • Johnson, J.L.1    Brown, C.2
  • 12
    • 0023664776 scopus 로고
    • An inspection of the domain between putative TATA box and translation start site in 79 plant genes
    • Joshi J.P. An inspection of the domain between putative TATA box and translation start site in 79 plant genes. Nucleic Acids Res. 1987, 15:6643-6653.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 6643-6653
    • Joshi, J.P.1
  • 13
    • 0023650367 scopus 로고
    • Putative polyadenylation signals in nuclear genes of higher plants: a compilation and analysis
    • Joshi J.P. Putative polyadenylation signals in nuclear genes of higher plants: a compilation and analysis. Nucleic Acids Res. 1987, 15:9627-9640.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 9627-9640
    • Joshi, J.P.1
  • 15
    • 0028330069 scopus 로고
    • Temperature-sensitive mutants of hsp82 of the budding yeast Saccharomyces cerevisiae
    • Kimura Y., Matsumoto S., Yahara I. Temperature-sensitive mutants of hsp82 of the budding yeast Saccharomyces cerevisiae. Mol. Gen. Genet. 1994, 242:517-527.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 517-527
    • Kimura, Y.1    Matsumoto, S.2    Yahara, I.3
  • 16
    • 0034817255 scopus 로고    scopus 로고
    • The Hsp90 family of proteins in Arabidopsis thaliana
    • Krishna P., Gloor G. The Hsp90 family of proteins in Arabidopsis thaliana. Cell Stress Chaperone 2001, 6:238-246.
    • (2001) Cell Stress Chaperone , vol.6 , pp. 238-246
    • Krishna, P.1    Gloor, G.2
  • 17
    • 0347087451 scopus 로고    scopus 로고
    • Molecular chaperone HSP90 associates with resistance protein N and its signaling proteins SGT1 and Rar1 to modulate an innate immune response in plants
    • Liu Y., Burch-Smith T., Schiff M., Feng S., Dinesh-Kumar S.P. 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.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2101-2108
    • Liu, Y.1    Burch-Smith, T.2    Schiff, M.3    Feng, S.4    Dinesh-Kumar, S.P.5
  • 18
    • 33747759740 scopus 로고    scopus 로고
    • RHsp90 gene expression in response to several environmental stresses in rice (Oryza sativa L.)
    • Liu D., Zhang X., Cheng Y., Takano T., Liu S. rHsp90 gene expression in response to several environmental stresses in rice (Oryza sativa L.). Plant Physiol. Biochem. 2006, 44:380-386.
    • (2006) Plant Physiol. Biochem. , vol.44 , pp. 380-386
    • Liu, D.1    Zhang, X.2    Cheng, Y.3    Takano, T.4    Liu, S.5
  • 19
    • 58249109502 scopus 로고    scopus 로고
    • Enhanced thermotolerance of E. coli by expressed OsHsp90 from rice (Oryza sativa L.)
    • Liu D., Lu Z., Zijun Mao Z., Liu S. Enhanced thermotolerance of E. coli by expressed OsHsp90 from rice (Oryza sativa L.). Curr. Microbiol. 2009, 58:129-133.
    • (2009) Curr. Microbiol. , vol.58 , pp. 129-133
    • Liu, D.1    Lu, Z.2    Zijun Mao, Z.3    Liu, S.4
  • 20
    • 21344498791 scopus 로고
    • A simple and efficient method for DNA extraction from grapevine cultivars and Vitis species and Ampelopsis
    • Lodhi M.A., Ye G.N., Weeden N.F., Reisch B.I. A simple and efficient method for DNA extraction from grapevine cultivars and Vitis species and Ampelopsis. Plant Mol. Biol. Rep. 1994, 12:6-13.
    • (1994) Plant Mol. Biol. Rep. , vol.12 , pp. 6-13
    • Lodhi, M.A.1    Ye, G.N.2    Weeden, N.F.3    Reisch, B.I.4
  • 21
    • 0242641582 scopus 로고    scopus 로고
    • High throughput virus-induced gene silencing implicates heat shock protein 90 in plant disease resistance
    • Lu R., Malcuit I., Moffett P., Ruiz M.T., Peart J., Wu A.J., et al. High throughput virus-induced gene silencing implicates heat shock protein 90 in plant disease resistance. EMBO J. 2003, 22:5690-5699.
    • (2003) EMBO J. , vol.22 , pp. 5690-5699
    • Lu, R.1    Malcuit, I.2    Moffett, P.3    Ruiz, M.T.4    Peart, J.5    Wu, A.J.6
  • 22
    • 0031470696 scopus 로고    scopus 로고
    • Genomic organization of hsp90 gene family in Arabidopsis
    • Milioni D., Hatzopoulos P. Genomic organization of hsp90 gene family in Arabidopsis. Plant Mol. Biol. 1997, 35:955-961.
    • (1997) Plant Mol. Biol. , vol.35 , pp. 955-961
    • Milioni, D.1    Hatzopoulos, P.2
  • 23
    • 0028012587 scopus 로고
    • The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo
    • 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. 1994, 14:1459-1464.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1459-1464
    • Minami, Y.1    Kimura, Y.2    Kawasaki, H.3    Suzuki, K.4    Yahara, I.5
  • 24
    • 34447135020 scopus 로고    scopus 로고
    • Isolation and characterization of expressed sequence tags (ESTs) from subtracted cDNA libraries of Pennisetum glaucum seedlings
    • Mishra R.N., Reddy P.S., Nair S., Markandeya G., Reddy A.R., Sopory S.K., et al. Isolation and characterization of expressed sequence tags (ESTs) from subtracted cDNA libraries of Pennisetum glaucum seedlings. Plant Mol. Biol. 2007, 64:713-732.
    • (2007) Plant Mol. Biol. , vol.64 , pp. 713-732
    • Mishra, R.N.1    Reddy, P.S.2    Nair, S.3    Markandeya, G.4    Reddy, A.R.5    Sopory, S.K.6
  • 25
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl L.H., Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 2006, 75:271-294.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 26
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • Pfaffl M.W., Horgan G.W., Dempfle L. Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res. 2002, 30:e36.
    • (2002) Nucleic Acids Res. , vol.30
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 27
    • 14544308022 scopus 로고    scopus 로고
    • Tight regulation of expression of two Arabidopsis cytosolic Hsp90 genes during embryo development
    • Prasinos C., Krampis K., Samakovli D., Hatzopoulos P. Tight regulation of expression of two Arabidopsis cytosolic Hsp90 genes during embryo development. J. Exp. Bot. 2005, 56:633-644.
    • (2005) J. Exp. Bot. , vol.56 , pp. 633-644
    • Prasinos, C.1    Krampis, K.2    Samakovli, D.3    Hatzopoulos, P.4
  • 28
    • 0037030713 scopus 로고    scopus 로고
    • HSP90 as a capacitor of phenotypic variation
    • Queitsch C., Sangster T.A., Lindquist S. HSP90 as a capacitor of phenotypic variation. Nature 2002, 417:618-624.
    • (2002) Nature , vol.417 , pp. 618-624
    • Queitsch, C.1    Sangster, T.A.2    Lindquist, S.3
  • 29
    • 41849111591 scopus 로고    scopus 로고
    • A high-throughput, low-cost method for the preparation of "sequencing-ready" phage DNA template
    • Reddy P.S., Nair S., Mallikarjuna G., Kaul T., Markandeya G., Sopory S.K., et al. A high-throughput, low-cost method for the preparation of "sequencing-ready" phage DNA template. Anal. Biochem. 2008, 376:258-261.
    • (2008) Anal. Biochem. , vol.376 , pp. 258-261
    • Reddy, P.S.1    Nair, S.2    Mallikarjuna, G.3    Kaul, T.4    Markandeya, G.5    Sopory, S.K.6
  • 30
    • 77949263576 scopus 로고    scopus 로고
    • Molecular cloning and characterization of gene encoding for cytoplasmic Hsc70 from Pennisetum glaucum may play a protective role against abiotic stresses
    • Reddy P.S., Mallikarjuna G., Kaul T., Chakradhar T., Mishra R.N., Sopory S.K., et al. Molecular cloning and characterization of gene encoding for cytoplasmic Hsc70 from Pennisetum glaucum may play a protective role against abiotic stresses. Mol. Genet. Genomics 2010, 283:243-254.
    • (2010) Mol. Genet. Genomics , vol.283 , pp. 243-254
    • Reddy, P.S.1    Mallikarjuna, G.2    Kaul, T.3    Chakradhar, T.4    Mishra, R.N.5    Sopory, S.K.6
  • 31
    • 1542301827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • Research 0034.1-0034.11
    • Roy N.V., Paepe A.D., Speleman F. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol. 2003, 3. Research 0034.1-0034.11.
    • (2003) Genome Biol. , vol.3
    • Roy, N.V.1    Paepe, A.D.2    Speleman, F.3
  • 32
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels
    • Russell R.B., Barton G.J. Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels. Proteins 1992, 14:309-323.
    • (1992) Proteins , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2
  • 33
    • 11844277123 scopus 로고    scopus 로고
    • The HSP90 chaperone complex, an emerging force in plant development and phenotypic plasticity
    • Sangster T.A., Queitsch C. The HSP90 chaperone complex, an emerging force in plant development and phenotypic plasticity. Curr. Opin. Plant Biol. 2005, 8:86-92.
    • (2005) Curr. Opin. Plant Biol. , vol.8 , pp. 86-92
    • Sangster, T.A.1    Queitsch, C.2
  • 34
    • 1842782331 scopus 로고    scopus 로고
    • Under cover: causes, effects and implications of HSP90-mediated genetic capacitance
    • Sangster T.A., Lindquist S., Queitsch C. Under cover: causes, effects and implications of HSP90-mediated genetic capacitance. BioEssays 2004, 26:348-362.
    • (2004) BioEssays , vol.26 , pp. 348-362
    • Sangster, T.A.1    Lindquist, S.2    Queitsch, C.3
  • 35
    • 33750008686 scopus 로고    scopus 로고
    • Structural analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements
    • 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.
    • (2006) Cell , vol.127 , pp. 329-340
    • Shiau, A.K.1    Harris, S.F.2    Southworth, D.R.3    Agard, D.A.4
  • 37
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: emerging mechanistic insights
    • Taipale M., Jarosz D.F., Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat. Rev. Mol. Cell Biol. 2010, 11:515-528.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 38
    • 0031705810 scopus 로고    scopus 로고
    • Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with CIpA, CIpB, and HtpG in vivo
    • Thomas J.G., Baneyx F. Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with CIpA, CIpB, and HtpG in vivo. J. Bacteriol. 1998, 180:5165-5172.
    • (1998) J. Bacteriol. , vol.180 , pp. 5165-5172
    • Thomas, J.G.1    Baneyx, F.2


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