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Volumn 47, Issue 10, 2009, Pages 859-866

Functional characterization of orchardgrass endoplasmic reticulum-resident Hsp90 (DgHsp90) as a chaperone and an ATPase

Author keywords

ATPase; Chaperone; Endoplasmic reticulum; Heat shock protein 90; Orchardgrass (Dactylis glomerata L.); Thermotolerance

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BENZOQUINONE DERIVATIVE; CHAPERONE; COMPLEMENTARY DNA; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HYDROGEN PEROXIDE; MACROCYCLIC LACTAM; OXIDIZING AGENT; VEGETABLE PROTEIN;

EID: 68149158278     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2009.06.008     Document Type: Article
Times cited : (14)

References (39)
  • 1
    • 85163503890 scopus 로고    scopus 로고
    • The effects of heat stress on cereal yield and quality
    • Basra A.S. (Ed), Food Products Press, Binghamton, NY
    • Stone P. The effects of heat stress on cereal yield and quality. In: Basra A.S. (Ed). Crop Responses and Adaptation to Temperature (2001), Food Products Press, Binghamton, NY 243-291
    • (2001) Crop Responses and Adaptation to Temperature , pp. 243-291
    • Stone, P.1
  • 3
    • 2442445139 scopus 로고    scopus 로고
    • Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response
    • Wang W., Vinocur B., Shoseyov O., and Altmant A. Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response. Trends Plant Sci. 9 (2004) 244-252
    • (2004) Trends Plant Sci. , vol.9 , pp. 244-252
    • Wang, W.1    Vinocur, B.2    Shoseyov, O.3    Altmant, A.4
  • 5
    • 0033230242 scopus 로고    scopus 로고
    • Protein folding in the plant cell
    • Miernyk J.A. Protein folding in the plant cell. Plant Physiol. 121 (1999) 695-703
    • (1999) Plant Physiol. , vol.121 , pp. 695-703
    • Miernyk, J.A.1
  • 6
    • 0031873752 scopus 로고    scopus 로고
    • The 90 kDa molecular chaperone family: structure, function, and clinical applications
    • Csermely P., Schnaider T., Sôti C., Prohászka Z., and Nardai G. The 90 kDa molecular chaperone family: structure, function, and clinical applications. Pharmacol. Ther. 79 (1998) 129-168
    • (1998) Pharmacol. Ther. , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Sôti, C.3    Prohászka, Z.4    Nardai, G.5
  • 7
    • 0034817255 scopus 로고    scopus 로고
    • The Hsp90 family of proteins in Arabidopsis thaliana
    • Krishna P., and Gloor G. The Hsp90 family of proteins in Arabidopsis thaliana. Cell Stress Chaperones 6 (2001) 238-246
    • (2001) Cell Stress Chaperones , vol.6 , pp. 238-246
    • Krishna, P.1    Gloor, G.2
  • 8
    • 0037099046 scopus 로고    scopus 로고
    • Chaperoning signaling pathways: molecular chaperones as stress-sensing 'heat shock' proteins
    • Nollen E.A.A., and Morimoto R. Chaperoning signaling pathways: molecular chaperones as stress-sensing 'heat shock' proteins. J. Cell Sci. 115 (2002) 2809-2816
    • (2002) J. Cell Sci. , vol.115 , pp. 2809-2816
    • Nollen, E.A.A.1    Morimoto, R.2
  • 10
    • 0032539709 scopus 로고    scopus 로고
    • Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence
    • Scheibel T., Weikl T., and Buchner J. Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence. Proc. Natl. Acad. Sci. USA 95 (1998) 1495-1499
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1495-1499
    • Scheibel, T.1    Weikl, T.2    Buchner, J.3
  • 11
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia R., and Braakman I. Quality control in the endoplasmic reticulum protein factory. Nature 426 (2003) 891-894
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 12
    • 0032007324 scopus 로고    scopus 로고
    • Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96
    • Nicchitta C.V. Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96. Curr. Opin. Immunol. 10 (1998) 103-109
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 103-109
    • Nicchitta, C.V.1
  • 13
    • 0242289417 scopus 로고    scopus 로고
    • Glucose-regulated stress proteins and antibacterial immunity
    • Rapp U.K., and Kaufmann S.H.E. Glucose-regulated stress proteins and antibacterial immunity. Trends Microbiol. 11 (2003) 519-526
    • (2003) Trends Microbiol. , vol.11 , pp. 519-526
    • Rapp, U.K.1    Kaufmann, S.H.E.2
  • 14
    • 0023660180 scopus 로고
    • Isolation and identification of partial cDNA clones for endoplasmin, the major glycoprotein of mammalian endoplasmic reticulum
    • Smith M.J., and Koch G.L.E. Isolation and identification of partial cDNA clones for endoplasmin, the major glycoprotein of mammalian endoplasmic reticulum. J. Mol. Biol. 194 (1987) 345-347
    • (1987) J. Mol. Biol. , vol.194 , pp. 345-347
    • Smith, M.J.1    Koch, G.L.E.2
  • 15
    • 0027571389 scopus 로고
    • A pathogen-induced gene of barley encodes a Hsp90 homologue showing striking similarity to vertebrate forms resident in the endoplasmic reticulum
    • Walther-Larsen H., Brandt J., Collinge D.B., and Thordal-Christensen H. A pathogen-induced gene of barley encodes a Hsp90 homologue showing striking similarity to vertebrate forms resident in the endoplasmic reticulum. Plant Mol. Biol. 21 (1993) 1097-1108
    • (1993) Plant Mol. Biol. , vol.21 , pp. 1097-1108
    • Walther-Larsen, H.1    Brandt, J.2    Collinge, D.B.3    Thordal-Christensen, H.4
  • 16
    • 0027689307 scopus 로고
    • HSP90 homologue from Madagascar periwinkle (Catharanthus roseus): cDNA sequence, regulation of protein expression and location in the endoplamic reticulum
    • Schröder G., Beck M., Eichel J., Vetter H.-P., and Schröder G. HSP90 homologue from Madagascar periwinkle (Catharanthus roseus): cDNA sequence, regulation of protein expression and location in the endoplamic reticulum. Plant Mol. Biol. 23 (1993) 583-594
    • (1993) Plant Mol. Biol. , vol.23 , pp. 583-594
    • Schröder, G.1    Beck, M.2    Eichel, J.3    Vetter, H.-P.4    Schröder, G.5
  • 18
    • 0026893762 scopus 로고
    • Bean homologs of the mammalian glucose-regulated proteins: induction by tunicamycin and interaction with newly synthesized seed storage proteins in the endoplasmic reticulum
    • D'Amico L., Valsasina B., Daminati M.G., Fabbrini S., Nitti G., Bollini R., Ceriotti A., and Vitale A. Bean homologs of the mammalian glucose-regulated proteins: induction by tunicamycin and interaction with newly synthesized seed storage proteins in the endoplasmic reticulum. Plant J. 2 (1992) 443-455
    • (1992) Plant J. , vol.2 , pp. 443-455
    • D'Amico, L.1    Valsasina, B.2    Daminati, M.G.3    Fabbrini, S.4    Nitti, G.5    Bollini, R.6    Ceriotti, A.7    Vitale, A.8
  • 20
    • 0035830914 scopus 로고    scopus 로고
    • The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli
    • Huang H.C., Sherman M.Y., Kandror O., and Goldberg A.L. The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli. J. Biol. Chem. 276 (2001) 3920-3928
    • (2001) J. Biol. Chem. , vol.276 , pp. 3920-3928
    • Huang, H.C.1    Sherman, M.Y.2    Kandror, O.3    Goldberg, A.L.4
  • 21
    • 4544318828 scopus 로고    scopus 로고
    • Chaperone activity of recombinant maize chloroplast protein synthesis elongation factor, EF-Tu
    • Rao D., Moncilovic I., Kobayashi S., Callegari E., and Ristic Z. Chaperone activity of recombinant maize chloroplast protein synthesis elongation factor, EF-Tu. Eur. J. Biochem. 271 (2004) 3684-3692
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3684-3692
    • Rao, D.1    Moncilovic, I.2    Kobayashi, S.3    Callegari, E.4    Ristic, Z.5
  • 22
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou B., Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Pipers P.W., and Pearl L.H. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17 (1998) 4829-4836
    • (1998) EMBO J. , vol.17 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3    O'Brien, R.4    Ladbury, J.E.5    Pipers, P.W.6    Pearl, L.H.7
  • 23
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumer agent
    • Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U., and Pavletich N.P. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumer agent. Cell 89 (1997) 239-250
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 24
    • 58149185931 scopus 로고    scopus 로고
    • Cloning and expression of glucose regulated 78 (GRP78) in Fenneropenaeus chinensis
    • 10.1007/s11033-007-9178-z
    • Luan W., Li F., Zhang J., Wang B., and Xiang J. Cloning and expression of glucose regulated 78 (GRP78) in Fenneropenaeus chinensis. Mol. Biol. Rep. (2008) 10.1007/s11033-007-9178-z
    • (2008) Mol. Biol. Rep.
    • Luan, W.1    Li, F.2    Zhang, J.3    Wang, B.4    Xiang, J.5
  • 25
  • 26
    • 49749118645 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress activates the expression of a sub-group of protein disulfide isomerase genes and AtbZip60 modulates the response in Arabidopsis thaliana
    • Lu D.-P., and Christopher D.A. Endoplasmic reticulum stress activates the expression of a sub-group of protein disulfide isomerase genes and AtbZip60 modulates the response in Arabidopsis thaliana. Mol. Genet. Genomics 280 (2008) 199-210
    • (2008) Mol. Genet. Genomics , vol.280 , pp. 199-210
    • Lu, D.-P.1    Christopher, D.A.2
  • 27
    • 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., and Liu S. rHsp90 gene expression in response to several environmental stresses in rice (Oryza sativa L.). Plant Physiol. Biochem. 44 (2006) 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
  • 28
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier L., Usherwood Y.-K., Chung K.T., and Hendershot L.M. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol. Biol. Cell 13 (2002) 4456-4469
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.-K.2    Chung, K.T.3    Hendershot, L.M.4
  • 29
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of Hsp90-associated proteins
    • Bose S., Weikl W., Bügl H., and Buchner J. Chaperone function of Hsp90-associated proteins. Science 274 (1996) 1715-1717
    • (1996) Science , vol.274 , pp. 1715-1717
    • Bose, S.1    Weikl, W.2    Bügl, H.3    Buchner, J.4
  • 34
    • 0034693228 scopus 로고    scopus 로고
    • Hsp90 chaperone activity requires the full-length protein and interaction among its multiple domains
    • Johnson B.D., Chadli A., Felts S.J., Bouhouche I., Catelli M.G., and Toft D.O. Hsp90 chaperone activity requires the full-length protein and interaction among its multiple domains. J. Biol. Chem. 275 (2000) 32499-32507
    • (2000) J. Biol. Chem. , vol.275 , pp. 32499-32507
    • Johnson, B.D.1    Chadli, A.2    Felts, S.J.3    Bouhouche, I.4    Catelli, M.G.5    Toft, D.O.6
  • 35
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance
    • Bush K.T., Goldberg A.L., and Nigam S.K. Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance. J. Biol. Chem. 272 (1997) 9086-9092
    • (1997) J. Biol. Chem. , vol.272 , pp. 9086-9092
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 36
    • 58249109502 scopus 로고    scopus 로고
    • Enhanced thermotolerance of E. coli by expressed OsHsp90 from rice (Oryza sativa L.)
    • Liu D., Lu Z., Mao Z., and Liu S. Enhanced thermotolerance of E. coli by expressed OsHsp90 from rice (Oryza sativa L.). Curr. Microbiol. 58 (2009) 129-133
    • (2009) Curr. Microbiol. , vol.58 , pp. 129-133
    • Liu, D.1    Lu, Z.2    Mao, Z.3    Liu, S.4
  • 37
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucl. Acids Symp. Ser. 41 (1999) 95-98
    • (1999) Nucl. Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 38
    • 0024970220 scopus 로고
    • A dual-labeling method for identifying differentially expressed genes: use in the identification of cDNA clones that hybridize to RNAs whose abundance in tomato flowers is potentially regulated by gibberellins
    • Olszewski N.E., Gast R.T., and Ausubel F.M. A dual-labeling method for identifying differentially expressed genes: use in the identification of cDNA clones that hybridize to RNAs whose abundance in tomato flowers is potentially regulated by gibberellins. Gene 77 (1989) 155-162
    • (1989) Gene , vol.77 , pp. 155-162
    • Olszewski, N.E.1    Gast, R.T.2    Ausubel, F.M.3
  • 39
    • 0037013252 scopus 로고    scopus 로고
    • Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress
    • Shen Y., Meunier L., and Hendershot L.M. Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress. J. Biol. Chem. 277 (2002) 15947-15956
    • (2002) J. Biol. Chem. , vol.277 , pp. 15947-15956
    • Shen, Y.1    Meunier, L.2    Hendershot, L.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.