메뉴 건너뛰기




Volumn 208, Issue 4, 1999, Pages 599-605

Stress-induced expression of cyclophilins in proembryonic masses of Digitalis lanata does not protect against freezing/thawing stress

Author keywords

Abscisic acid; Cyclophilin; Digitalis; Jasmonic acid; Peptidyl prolyl cis trans isomerase; Proembryonic mass; Stress

Indexed keywords

ABSCISIC ACID; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; CRYOPRESERVATION; CYCLOPHILIN; CYCLOSPORIN A; CYTOSOL; ELECTROPHORESIS; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; FROST RESISTANCE; MOLECULAR WEIGHT; PROTEIN EXPRESSION; SENSOR; SORBITOL;

EID: 0040439865     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004250050598     Document Type: Article
Times cited : (33)

References (35)
  • 1
    • 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. EMBO J 10: 1037-1044
    • (1991) EMBO J , vol.10 , pp. 1037-1044
    • Bartels, D.1    Engelhardt, K.2    Roncarati, R.3    Schneider, K.4    Rotter, M.5    Salamini, F.6
  • 2
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • Boston RS, Viitanen PV, Vierling E (1996) Molecular chaperones and protein folding in plants. Plant Mol Biol 32: 191-222
    • (1996) Plant Mol Biol , vol.32 , pp. 191-222
    • Boston, R.S.1    Viitanen, P.V.2    Vierling, E.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0026799384 scopus 로고
    • Plant organelles contain distinct peptidylprolyl cis, trans-isomerases
    • Breiman A, Fawcett TW, Ghirardi ML, Mattoo AK (1992) Plant organelles contain distinct peptidylprolyl cis, trans-isomerases. J Biol Chem 267: 21293-21296
    • (1992) J Biol Chem , vol.267 , pp. 21293-21296
    • Breiman, A.1    Fawcett, T.W.2    Ghirardi, M.L.3    Mattoo, A.K.4
  • 5
    • 0027674915 scopus 로고
    • A leaf-specific gene stimulated by light during wheat acclimation to low temperature
    • Chauvin LP, Houde M, Sarhan F (1993) A leaf-specific gene stimulated by light during wheat acclimation to low temperature. Plant Mol Biol 23: 255-265
    • (1993) Plant Mol Biol , vol.23 , pp. 255-265
    • Chauvin, L.P.1    Houde, M.2    Sarhan, F.3
  • 6
    • 0028172340 scopus 로고
    • Isolation of an osmotic stress-and abscisic acid-induced gene encoding an acidic endochitinase from Lycopersicon chilense
    • Chen RD, Yu LX, Greer AF, Cheriti H. Tabaeizadeh Z (1994) Isolation of an osmotic stress-and abscisic acid-induced gene encoding an acidic endochitinase from Lycopersicon chilense. Mol Gen Genet 245: 195-202
    • (1994) Mol Gen Genet , vol.245 , pp. 195-202
    • Chen, R.D.1    Yu, L.X.2    Greer, A.F.3    Cheriti, H.4    Tabaeizadeh, Z.5
  • 7
    • 0040696944 scopus 로고
    • Cryopreservation of Digitalis lanata cells: Membrane area reduction of the protoplast during cryoprotector treatment and cooling
    • Diettrich B, Neumann D, Luckner M (1991) Cryopreservation of Digitalis lanata cells: membrane area reduction of the protoplast during cryoprotector treatment and cooling. J Plant Physiol 139: 212-217
    • (1991) J Plant Physiol , vol.139 , pp. 212-217
    • Diettrich, B.1    Neumann, D.2    Luckner, M.3
  • 8
    • 0030863169 scopus 로고    scopus 로고
    • Changes in the accumulation of cytosolic cyclophilin transcripts in cultured periwinkle cells following hormonal and stress treatments
    • Droual AM, Maaroufi H, Creche J, Chenieux JC, Rideau M, Hamdi S (1997) Changes in the accumulation of cytosolic cyclophilin transcripts in cultured periwinkle cells following hormonal and stress treatments. J Plant Physiol 151: 142-150
    • (1997) J Plant Physiol , vol.151 , pp. 142-150
    • Droual, A.M.1    Maaroufi, H.2    Creche, J.3    Chenieux, J.C.4    Rideau, M.5    Hamdi, S.6
  • 9
    • 0028050923 scopus 로고
    • Peptidyl-prolyl cis/trans isomerases and their effectors
    • Engl.
    • Fischer G (1994) Peptidyl-prolyl cis/trans isomerases and their effectors. Angew Chem Int Ed (Engl.) 33: 1415-1436
    • (1994) Angew Chem Int Ed , vol.33 , pp. 1415-1436
    • Fischer, G.1
  • 10
    • 0025599920 scopus 로고
    • Structure and expression of cytosolic cyclophilin/peptidyl-prolyl cis-trans isomerase of higher plants and production of active tomato cyclophilin in Escherichia coli
    • Gasser CS, Gunning DA, Budelier KA, Brown SM (1990) Structure and expression of cytosolic cyclophilin/peptidyl-prolyl cis-trans isomerase of higher plants and production of active tomato cyclophilin in Escherichia coli. Proc Natl Acad Sci USA 87: 9519-9523
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9519-9523
    • Gasser, C.S.1    Gunning, D.A.2    Budelier, K.A.3    Brown, S.M.4
  • 11
    • 0025700714 scopus 로고
    • Characterization of the human cyclophilin gene and of related processed pseudogenes
    • Haendler B, Hofer E (1990) Characterization of the human cyclophilin gene and of related processed pseudogenes. Eur J Biochem 190: 477-482
    • (1990) Eur J Biochem , vol.190 , pp. 477-482
    • Haendler, B.1    Hofer, E.2
  • 12
    • 85032132015 scopus 로고
    • Gene expression under temperature stress
    • Howarth CJ, Ougham HJ (1993) Gene expression under temperature stress. New Phytol 125: 1-26
    • (1993) New Phytol , vol.125 , pp. 1-26
    • Howarth, C.J.1    Ougham, H.J.2
  • 13
    • 0028940309 scopus 로고
    • Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo
    • Jakob U, Lilie H, Meyer I, Buchner J (1995) Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo. J Biol Chem 270: 7288-7294
    • (1995) J Biol Chem , vol.270 , pp. 7288-7294
    • Jakob, U.1    Lilie, H.2    Meyer, I.3    Buchner, J.4
  • 14
    • 0025858482 scopus 로고
    • Structure of human cyclophilin and its binding site for cyclosporin a determined by X-ray crystallography and NMR spectroscopy
    • Kallen J, Spitzfaden C, Zurini MGM, Wider G, Widmer H, Wuthrich K, Walkinshaw MD (1991) Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy. Nature 353: 276-279
    • (1991) Nature , vol.353 , pp. 276-279
    • Kallen, J.1    Spitzfaden, C.2    Zurini, M.G.M.3    Wider, G.4    Widmer, H.5    Wuthrich, K.6    Walkinshaw, M.D.7
  • 15
    • 0028483257 scopus 로고
    • Cloning of cDNAs for genes that are early-responsive to dehydration stress (ERDs) in Arabidopsis thalania L.: Identification of three ERDs as HSP cognate genes
    • Kiyosue T, Yamaguchi-Shinozaki K, Shinozaki K (1994) Cloning of cDNAs for genes that are early-responsive to dehydration stress (ERDs) in Arabidopsis thalania L.: Identification of three ERDs as HSP cognate genes. Plant Mol Biol 25: 791-798
    • (1994) Plant Mol Biol , vol.25 , pp. 791-798
    • Kiyosue, T.1    Yamaguchi-Shinozaki, K.2    Shinozaki, K.3
  • 16
    • 0027945623 scopus 로고
    • Influence of additives on resolution and focusing efficiency in free-flow isoelectric focusing
    • Kullertz G, Fischer G (1994) Influence of additives on resolution and focusing efficiency in free-flow isoelectric focusing. J Chromatogr 684: 329-341
    • (1994) J Chromatogr , vol.684 , pp. 329-341
    • Kullertz, G.1    Fischer, G.2
  • 17
    • 0028170154 scopus 로고
    • Differentation by preparative continuous free flow-isoelectric focusing of cyclosporin A inhibitable peptidyl-prolyl cisjtrans isomerase of human erythrocytes
    • Kullertz G, Meyer S, Fischer G (1994) Differentation by preparative continuous free flow-isoelectric focusing of cyclosporin A inhibitable peptidyl-prolyl cisjtrans isomerase of human erythrocytes. Electrophoresis 7: 960-967
    • (1994) Electrophoresis , vol.7 , pp. 960-967
    • Kullertz, G.1    Meyer, S.2    Fischer, G.3
  • 18
    • 0028948241 scopus 로고
    • Induction of heat, freezing and salt tolerance by heat and salt shock in Saccharomyces cerevisiae
    • Lewis JG, Learmonth RP, Watson K (1995) Induction of heat, freezing and salt tolerance by heat and salt shock in Saccharomyces cerevisiae. Microbiology 141: 687-694
    • (1995) Microbiology , vol.141 , pp. 687-694
    • Lewis, J.G.1    Learmonth, R.P.2    Watson, K.3
  • 20
    • 0028158402 scopus 로고
    • Light-regulated, tissue-specific immunophilins in a higher plant
    • Luan S, Albers MW, Schreiber SL (1994a) Light-regulated, tissue-specific immunophilins in a higher plant. Proc Natl Acad Sci USA 91: 984-988
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 984-988
    • Luan, S.1    Albers, M.W.2    Schreiber, S.L.3
  • 21
    • 0028445305 scopus 로고
    • pCyP B: A chloroplast-localized, heat shock-responsive cyclophilin from fava bean
    • Luan, S, Lane WS, Schreiber SL (1994b) pCyP B: a chloroplast-localized, heat shock-responsive cyclophilin from fava bean. Plant Cell 6: 885-892
    • (1994) Plant Cell , vol.6 , pp. 885-892
    • Luan, S.1    Lane, W.S.2    Schreiber, S.L.3
  • 22
    • 0000362850 scopus 로고
    • Effects of abiotic stresses on cyclophilin gene expression in maize and bean and sequence analysis of bean cyclophilin cDNA
    • Marivet J, Frendo P, Burkard G (1992) Effects of abiotic stresses on cyclophilin gene expression in maize and bean and sequence analysis of bean cyclophilin cDNA. Plant Sci 84: 171-178
    • (1992) Plant Sci , vol.84 , pp. 171-178
    • Marivet, J.1    Frendo, P.2    Burkard, G.3
  • 23
    • 0028951175 scopus 로고
    • DNA sequence analysis of a cyclophilin gene from maize: Developmental expression and regulation by salicylic acid
    • Marivet J, Frendo P, Burkard G (1995) DNA sequence analysis of a cyclophilin gene from maize: developmental expression and regulation by salicylic acid Mol Gen Genet 247: 222-228
    • (1995) Mol Gen Genet , vol.247 , pp. 222-228
    • Marivet, J.1    Frendo, P.2    Burkard, G.3
  • 24
    • 0001017259 scopus 로고
    • Abscisic acid-regulated gene expression in relation to freezing tolerance in alfalfa
    • Mohapatra SS, Poole RJ, Dhindsa RS (1988) Abscisic acid-regulated gene expression in relation to freezing tolerance in alfalfa. Plant Physiol 87: 468-473
    • (1988) Plant Physiol , vol.87 , pp. 468-473
    • Mohapatra, S.S.1    Poole, R.J.2    Dhindsa, R.S.3
  • 25
    • 0014454095 scopus 로고
    • Kinetics of the reversible inhibition of enzyme catalyzed reactions by tight-binding inhibitors
    • Morrison JF (1969) Kinetics of the reversible inhibition of enzyme catalyzed reactions by tight-binding inhibitors. Biochim Biophys Acta 185: 269-286
    • (1969) Biochim Biophys Acta , vol.185 , pp. 269-286
    • Morrison, J.F.1
  • 26
    • 0005318594 scopus 로고
    • Heavy metal-hormone interactions in rice plants - Effects on growth, net photosynthesis, and carbohydrate distribution
    • Moya JL, Ros R, Picazo I (1995) Heavy metal-hormone interactions in rice plants - effects on growth, net photosynthesis, and carbohydrate distribution. J Plant Growth Regul 14: 61-67
    • (1995) J Plant Growth Regul , vol.14 , pp. 61-67
    • Moya, J.L.1    Ros, R.2    Picazo, I.3
  • 27
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP-and GTP-binding proteins
    • Saraste M, Sibbald PR, Wittinghofer A (1990) The P-loop - a common motif in ATP-and GTP-binding proteins. Trends Biochem Sci 15: 430-434
    • (1990) Trends Biochem Sci , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 28
    • 0029364576 scopus 로고
    • Prolyl isomerases join the fold
    • Schmid FX (1995) Prolyl isomerases join the fold. Curr Biol 5, 993-994
    • (1995) Curr Biol , vol.5 , pp. 993-994
    • Schmid, F.X.1
  • 29
    • 0344364294 scopus 로고    scopus 로고
    • Database Accession number Y08320
    • Scholze C (1996) EMBL Entry, Database Accession number Y08320
    • (1996) EMBL Entry
    • Scholze, C.1
  • 30
    • 0028864461 scopus 로고
    • A ribosome associated peptidyl-prolyl cis/ trans isomerase identified as the trigger factor
    • Stoller G, Rücknagel KP, Nierhaus KH, Schmid FX, Fischer G, Rahfeld JU (1995) A ribosome associated peptidyl-prolyl cis/ trans isomerase identified as the trigger factor. EMBO J 14: 4939-4948
    • (1995) EMBO J , vol.14 , pp. 4939-4948
    • Stoller, G.1    Rücknagel, K.P.2    Nierhaus, K.H.3    Schmid, F.X.4    Fischer, G.5    Rahfeld, J.U.6
  • 32
    • 0006909936 scopus 로고
    • Morphogenesis and embryogenesis in long term cultures of Digitalis
    • Tewes A, Wappler A, Peschke EM, Garve R, Nover L (1982) Morphogenesis and embryogenesis in long term cultures of Digitalis. J Plant Physiol 106: 311-324
    • (1982) J Plant Physiol , vol.106 , pp. 311-324
    • Tewes, A.1    Wappler, A.2    Peschke, E.M.3    Garve, R.4    Nover, L.5
  • 33
    • 0028799459 scopus 로고
    • Early events in preprotein recognition in E. Coli -interaction of SRP and trigger factor with nascent polypeptides
    • Valent QA, Kendall DA, High S, Kusters R, Oudega B, Luirink J (1995) Early events in preprotein recognition in E. coli -interaction of SRP and trigger factor with nascent polypeptides. EMBO J 14: 5494-5505
    • (1995) EMBO J , vol.14 , pp. 5494-5505
    • Valent, Q.A.1    Kendall, D.A.2    High, S.3    Kusters, R.4    Oudega, B.5    Luirink, J.6
  • 34
    • 0039511731 scopus 로고
    • The influence of ABA and JAA on in-vivo phosphorylation of proteins in Funaria hygrometrica Hedw
    • Werner O, Bopp M (1993) The influence of ABA and JAA on in-vivo phosphorylation of proteins in Funaria hygrometrica Hedw. J Plant Physiol 141: 93-97
    • (1993) J Plant Physiol , vol.141 , pp. 93-97
    • Werner, O.1    Bopp, M.2
  • 35
    • 0027549719 scopus 로고
    • Expression of an ABA-responsive osmotin-like gene during the induction of freezing tolerance in Solanum commersonii
    • Zhu B, Chen THH, Li PH (1993) Expression of an ABA-responsive osmotin-like gene during the induction of freezing tolerance in Solanum commersonii. Plant Mol Biol 21: 729-735
    • (1993) Plant Mol Biol , vol.21 , pp. 729-735
    • Zhu, B.1    Chen, T.H.H.2    Li, P.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.