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Volumn 70, Issue 5, 2004, Pages 741-750

Isolation and characterisation of a novel dehydration-induced Grp94 homologue from the resurrection plant Xerophyta viscosa

Author keywords

[No Author keywords available]

Indexed keywords

WATER STRESS;

EID: 4544328490     PISSN: 02546299     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0254-6299(15)30175-7     Document Type: Article
Times cited : (8)

References (54)
  • 2
    • 0026553672 scopus 로고
    • PROSITE: A dictionary of sites and patterns in proteins
    • Bairoch A (1992) PROSITE: a dictionary of sites and patterns in proteins. Nucleic Acids Research 20: 2013-2018
    • (1992) Nucleic Acids Research , vol.20 , pp. 2013-2018
    • Bairoch, A.1
  • 4
    • 0025782902 scopus 로고
    • An ABA and GA modulated gene expressed in the barley embryo encodes an aldose reductase related protein
    • Bartels D, Engelhardt K, Roncarati R, Schneider K, Rotter M, Salamini F (1991) An ABA and GA modulated gene expressed in the barley embryo encodes an aldose reductase related protein. The EMBO Journal 10: 1037-1043
    • (1991) The EMBO Journal , vol.10 , pp. 1037-1043
    • Bartels, D.1    Engelhardt, K.2    Roncarati, R.3    Schneider, K.4    Rotter, M.5    Salamini, F.6
  • 5
    • 0002380156 scopus 로고
    • Desiccation-tolerance in vegetative plant tissues and seeds: Protein synthesis in relation to desiccation and a potential role for protection and repair mechanisms
    • Somera GN, Osmond C, Bolis CL (eds) Springer, New York
    • Bewley JD, Oliver MJ (1992) Desiccation-tolerance in vegetative plant tissues and seeds: protein synthesis in relation to desiccation and a potential role for protection and repair mechanisms. In: Somera GN, Osmond C, Bolis CL (eds) Water and Life: A Comparative Analysis of Water Relationships at the Organismic, Cellular and Molecular Levels. Springer, New York, pp 41-160
    • (1992) Water and Life: A Comparative Analysis of Water Relationships at the Organismic, Cellular and Molecular Levels , pp. 41-160
    • Bewley, J.D.1    Oliver, M.J.2
  • 8
    • 0031081346 scopus 로고    scopus 로고
    • Plant responses to water deficit
    • Bray EA (1997) Plant responses to water deficit. Trends in Plant Science 2: 48-54
    • (1997) Trends in Plant Science , vol.2 , pp. 48-54
    • Bray, E.A.1
  • 9
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 & Co.- A holding for a folding
    • Buchner J (1999) Hsp90 & Co.- a holding for a folding. Trends in Biochemical Sciences 24: 136-141
    • (1999) Trends in Biochemical Sciences , vol.24 , pp. 136-141
    • Buchner, J.1
  • 10
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones and thermotolerance
    • Bush KT, Goldberg AL, Nigam SK (1997) Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones and thermotolerance. Journal of Biological Chemistry 272: 9086-9092
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 9086-9092
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 12
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review
    • Csermely P, Schnaider T, Soti C, Prohaszka Z, Nardai G (1998) The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review. Pharmacology and Therapeutics 79: 129-168
    • (1998) Pharmacology and Therapeutics , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohaszka, Z.4    Nardai, G.5
  • 13
    • 0026893762 scopus 로고
    • Bean homologues of the mammalian glucose-regulated proteins: Induction by tunicamycin and interaction with newly synthesised seed storage proteins in the endoplasmic reticulum
    • D'Amico L, Valsasina B, Daminati MG Fabbrini MS, Nitti G, Bollini R, Ceriotti A, Vitale A (1992) Bean homologues of the mammalian glucose-regulated proteins: induction by tunicamycin and interaction with newly synthesised seed storage proteins in the endoplasmic reticulum. Plant Journal 2: 443-455
    • (1992) Plant Journal , vol.2 , pp. 443-455
    • D'Amico, L.1    Valsasina, B.2    Daminati, M.G.3    Fabbrini, M.S.4    Nitti, G.5    Bollini, R.6    Ceriotti, A.7    Vitale, A.8
  • 16
    • 0000531516 scopus 로고
    • Analysis of sorting signals responsible for the accumulation of soluble reticuloplasmins in the plant endoplasmic reticulum
    • Denecke J, Ek B, Caspers M, Sinjorgo KMC, Palva ET (1993) Analysis of sorting signals responsible for the accumulation of soluble reticuloplasmins in the plant endoplasmic reticulum. Journal of Experimental Botany, Supplement 44: 213-221
    • (1993) Journal of Experimental Botany, Supplement , vol.44 , pp. 213-221
    • Denecke, J.1    Ek, B.2    Caspers, M.3    Sinjorgo, K.M.C.4    Palva, E.T.5
  • 17
    • 0034486488 scopus 로고    scopus 로고
    • A comparison of mechanisms of desiccation tolerance among three angiosperm resurrection plant species
    • Farrant JM (2000) A comparison of mechanisms of desiccation tolerance among three angiosperm resurrection plant species. Plant Ecology 151: 29-35
    • (2000) Plant Ecology , vol.151 , pp. 29-35
    • Farrant, J.M.1
  • 19
    • 0001078949 scopus 로고
    • Desiccation tolerant flowering plants in southern Africa
    • Gaff DF (1971) Desiccation tolerant flowering plants in southern Africa. Science 174: 1033-1034
    • (1971) Science , vol.174 , pp. 1033-1034
    • Gaff, D.F.1
  • 20
    • 0030889010 scopus 로고    scopus 로고
    • A predicted consensus structure for the N-terminal fragment of the heat shock protein Hps90 family
    • Gerloff DL, Cohen FE, Korostensky C, Turcotte M, Gonnet GH, Benner SA (1997) A predicted consensus structure for the N-terminal fragment of the heat shock protein Hps90 family. Proteins 27: 450-458
    • (1997) Proteins , vol.27 , pp. 450-458
    • Gerloff, D.L.1    Cohen, F.E.2    Korostensky, C.3    Turcotte, M.4    Gonnet, G.H.5    Benner, S.A.6
  • 21
    • 0033581021 scopus 로고    scopus 로고
    • The importance of ATP binding and hydrolysis by Hsp90 in formation and function of protein heterocomplexes
    • Grenert JP, Johnson BD, Toft DO (1999) The importance of ATP binding and hydrolysis by Hsp90 in formation and function of protein heterocomplexes. Journal of Biological Chemistry 274: 17525-17533
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 17525-17533
    • Grenert, J.P.1    Johnson, B.D.2    Toft, D.O.3
  • 27
    • 0030809270 scopus 로고    scopus 로고
    • Protein folding in vivo: Unravelling complex pathways
    • Johnson JL, Craig E (1997) Protein folding in vivo: Unravelling complex pathways. Cell 90: 210-204
    • (1997) Cell , vol.90 , pp. 210-1204
    • Johnson, J.L.1    Craig, E.2
  • 28
    • 0022833371 scopus 로고
    • Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin
    • Koch G, Smith M, Macer D, Webster P, Mortara R (1986) Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin. Journal of Cell Science 86: 217-232
    • (1986) Journal of Cell Science , vol.86 , pp. 217-232
    • Koch, G.1    Smith, M.2    Macer, D.3    Webster, P.4    Mortara, R.5
  • 29
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi Y, Segal M, Normington K, Gething M-J, Sambrook J (1988) The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332: 462-464
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.-J.4    Sambrook, J.5
  • 30
    • 0034817255 scopus 로고    scopus 로고
    • The Hsp90 family of proteins in Arabidopsis thaliana
    • Krishna P, Gloor G (2001) The Hsp90 family of proteins in Arabidopsis thaliana. Cell Stress and Chaperones 6: 238-246
    • (2001) Cell Stress and Chaperones , vol.6 , pp. 238-246
    • Krishna, P.1    Gloor, G.2
  • 31
    • 0027208741 scopus 로고
    • Tumour rejection antigen Gp96/Grp94 is an ATPase: Implications for protein folding and antigen presentation
    • Li Z, Srivastava P (1993) Tumour rejection antigen Gp96/Grp94 is an ATPase: implications for protein folding and antigen presentation. The EMBO Journal 12: 3143-3151
    • (1993) The EMBO Journal , vol.12 , pp. 3143-3151
    • Li, Z.1    Srivastava, P.2
  • 32
    • 0033230242 scopus 로고    scopus 로고
    • Protein folding in the plant cell
    • Miernyk JA (1999) Protein folding in the plant cell. Plant Physiology 121: 695-703
    • (1999) Plant Physiology , vol.121 , pp. 695-703
    • Miernyk, J.A.1
  • 34
    • 0033792170 scopus 로고    scopus 로고
    • An aldose reductase homolog from the resurrection plant Xerophyta viscosa Baker
    • Mundree SG, Whittaker A, Thomson JA, Farrant JM (2000) An aldose reductase homolog from the resurrection plant Xerophyta viscosa Baker. Planta 211: 693-700
    • (2000) Planta , vol.211 , pp. 693-700
    • Mundree, S.G.1    Whittaker, A.2    Thomson, J.A.3    Farrant, J.M.4
  • 35
    • 0035677637 scopus 로고    scopus 로고
    • Molecular characterisation of XVT8, a stress-responsive gene from the resurrection plant, Xerophyta viscosa Baker
    • Ndima T, Farrant JM, Thomson JA, Mundree SG (2001) Molecular characterisation of XVT8, a stress-responsive gene from the resurrection plant, Xerophyta viscosa Baker. Plant Growth Regulation 35: 137-145
    • (2001) Plant Growth Regulation , vol.35 , pp. 137-145
    • Ndima, T.1    Farrant, J.M.2    Thomson, J.A.3    Mundree, S.G.4
  • 37
    • 0000818625 scopus 로고    scopus 로고
    • Desiccation-tolerance of plant tissues: A mechanistic overview
    • Oliver MJ, Bewley JD (1997) Desiccation-tolerance of plant tissues: A mechanistic overview. Horticultural Review 18: 171-213
    • (1997) Horticultural Review , vol.18 , pp. 171-213
    • Oliver, M.J.1    Bewley, J.D.2
  • 38
    • 0000675009 scopus 로고
    • Heat shock proteins and stress tolerance
    • Morimoto RI, Tissieres A, Georgopoulos C (eds) Cold Spring Harbor Laboratory Press, New York
    • Parsell DA, Lindquist S (1994) Heat shock proteins and stress tolerance. In: Morimoto RI, Tissieres A, Georgopoulos C (eds) The Biology of Heat Shock Proteins and Molecular Chaperones. Cold Spring Harbor Laboratory Press, New York, pp 457-494
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 457-494
    • Parsell, D.A.1    Lindquist, S.2
  • 40
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterisation of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH (1997) Identification and structural characterisation of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90: 65-75
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 41
    • 0034725640 scopus 로고    scopus 로고
    • Ligand interaction in the adenosine nucleotide-binding domain of the Hsp90 chaperone, Grp94
    • Rosser MFN, Nicchitta CV (2000) Ligand interaction in the adenosine nucleotide-binding domain of the Hsp90 chaperone, Grp94. Journal of Biological Chemistry 275: 22798-22805
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 22798-22805
    • Rosser, M.F.N.1    Nicchitta, C.V.2
  • 43
    • 0027689307 scopus 로고
    • Hsp90 homologue from Madagascar periwinkle (Catharanthus roseus): cDNA sequence, regulation of protein expression and location in the endoplasmic reticulum
    • Schroder G, Beck M, Eichel J, Vetter H-P, Schroder J (1993) Hsp90 homologue from Madagascar periwinkle (Catharanthus roseus): cDNA sequence, regulation of protein expression and location in the endoplasmic reticulum. Plant Molecular Biology 23: 583-594
    • (1993) Plant Molecular Biology , vol.23 , pp. 583-594
    • Schroder, G.1    Beck, M.2    Eichel, J.3    Vetter, H.-P.4    Schroder, J.5
  • 45
    • 0030301005 scopus 로고    scopus 로고
    • Differences in rehydration of three desiccation-tolerant angiosperm species
    • Sherwin HW, Farrant JM (1996) Differences in rehydration of three desiccation-tolerant angiosperm species. Annals of Botany 78: 703-710
    • (1996) Annals of Botany , vol.78 , pp. 703-710
    • Sherwin, H.W.1    Farrant, J.M.2
  • 46
    • 0023660117 scopus 로고
    • The glucose-regulated protein grp94 is related to heat shock protein Hsp90
    • Sorger PK, Pelham HRB (1987) The glucose-regulated protein grp94 is related to heat shock protein Hsp90. Journal of Molecular Biology 194: 341-344
    • (1987) Journal of Molecular Biology , vol.194 , pp. 341-344
    • Sorger, P.K.1    Pelham, H.R.B.2
  • 47
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumour agent
    • Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP (1997) Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumour agent. Cell 89: 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
  • 48
    • 85051580403 scopus 로고
    • Acquisition and loss of desiccation tolerance
    • Kigel J, Galilli G (eds) Marcel Dekker, New York
    • Vertucci CW, Farrant JM (1995) Acquisition and loss of desiccation tolerance. In: Kigel J, Galilli G (eds) Seed Development and Germination. Marcel Dekker, New York, pp 237-271
    • (1995) Seed Development and Germination , pp. 237-271
    • Vertucci, C.W.1    Farrant, J.M.2
  • 49
    • 0032725633 scopus 로고    scopus 로고
    • The endoplasmic reticulum-gateway of the secretory pathway
    • Vitale A, Denecke J (1999) The endoplasmic reticulum-gateway of the secretory pathway. Plant Cell 11: 615-628
    • (1999) Plant Cell , vol.11 , pp. 615-628
    • Vitale, A.1    Denecke, J.2
  • 50
    • 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 DB, Thordal-Christensen H (1993) A pathogen-induced gene of barley encodes a Hsp90 homologue showing striking similarity to vertebrate forms resident in the endoplasmic reticulum. Plant Molecular Biology 21: 1097-1108
    • (1993) Plant Molecular Biology , vol.21 , pp. 1097-1108
    • Walther-Larsen, H.1    Brandt, J.2    Collinge, D.B.3    Thordal-Christensen, H.4
  • 51
    • 0032554622 scopus 로고    scopus 로고
    • Structural transitions accompanying the activation of peptide binding to the endoplasmic reticulum Hsp90 chaperone Grp94
    • Wearsch PA, Voglino L, Nicchitta CV (1998) Structural transitions accompanying the activation of peptide binding to the endoplasmic reticulum Hsp90 chaperone Grp94. Biochemistry 37: 5709-5719
    • (1998) Biochemistry , vol.37 , pp. 5709-5719
    • Wearsch, P.A.1    Voglino, L.2    Nicchitta, C.V.3
  • 52
  • 53
    • 0026428621 scopus 로고
    • Crystal structure of an N-terminal fragment of the DNA gyrase B protein
    • Wigley DB, Davies GJ, Dodson EJ, Maxwell A, Dodson G (1991) Crystal structure of an N-terminal fragment of the DNA gyrase B protein. Nature 351: 624-629
    • (1991) Nature , vol.351 , pp. 624-629
    • Wigley, D.B.1    Davies, G.J.2    Dodson, E.J.3    Maxwell, A.4    Dodson, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.