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Volumn 119, Issue 2, 1999, Pages 511-520

Evidence for a slow-turnover form of the Ca2+-independent phosphoenolpyruvate carboxylase kinase in the aleurone-endosperm tissue of germinating barley seeds

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; AGAROSE; ALEURONE; CALCIUM; DEXTRAN; ENDOSPERM; ENZYME ACTIVITY; EXTRACTION; GERMINATION; PHOSPHOENOLPYRUVATE CARBOXYLASE; PHOSPHORYLATION; PLANT PRODUCT; POLYPEPTIDE; PROTEIN KINASE; PYRUVATE KINASE; RADIOLABELLING; WESTERN BLOTTING;

EID: 0032817253     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.119.2.511     Document Type: Article
Times cited : (28)

References (49)
  • 1
    • 0029310578 scopus 로고
    • A rice membrane calcium-dependent protein kinase is induced by gibberellin
    • Abo-El-Saad M, Wu R (1995) A rice membrane calcium-dependent protein kinase is induced by gibberellin. Plant Physiol 108: 787-793
    • (1995) Plant Physiol , vol.108 , pp. 787-793
    • Abo-El-Saad, M.1    Wu, R.2
  • 3
    • 0026537508 scopus 로고
    • Regulatory phosphorylation of sorghum leaf phosphoenlpyruvate carboxylase: Identification of the protein-serine kinase and some elements of the signaltransduction cascade
    • Bakrim N, Echevarría C, Cretín C, Arrio-Dupont M, Pierre JN, Vidal J, Chollet R, Gadal P (1992) Regulatory phosphorylation of Sorghum leaf phosphoenlpyruvate carboxylase: identification of the protein-serine kinase and some elements of the signaltransduction cascade. Eur J Biochem 204: 821-830
    • (1992) Eur J Biochem , vol.204 , pp. 821-830
    • Bakrim, N.1    Echevarría, C.2    Cretín, C.3    Arrio-Dupont, M.4    Pierre, J.N.5    Vidal, J.6    Chollet, R.7    Gadal, P.8
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantification 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
  • 5
    • 0025737971 scopus 로고
    • Circadian rhythms in the activity of a plant protein kinase
    • Carter PJ, Nimmo HG, Fewson CA, Wilkins MB (1991) Circadian rhythms in the activity of a plant protein kinase. EMBO J 10: 2063-2068
    • (1991) EMBO J , vol.10 , pp. 2063-2068
    • Carter, P.J.1    Nimmo, H.G.2    Fewson, C.A.3    Wilkins, M.B.4
  • 6
    • 0000756509 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase: A ubiquitous, highly regulated enzyme in plants
    • Chollet R, Vidai J, O'Leary MH (1996) Phosphoenolpyruvate carboxylase: a ubiquitous, highly regulated enzyme in plants. Annu Rev Plant Physiol Plant Mol Biol 47: 273-298
    • (1996) Annu Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 273-298
    • Chollet, R.1    Vidai, J.2    O'Leary, M.H.3
  • 7
    • 0028843449 scopus 로고
    • Hormonal regulation of organic and phosphoric acid release by barley aleurone layers and scutella
    • Drozdowicz YM, Jones RL (1995) Hormonal regulation of organic and phosphoric acid release by barley aleurone layers and scutella. Plant Physiol 108: 769-776
    • (1995) Plant Physiol , vol.108 , pp. 769-776
    • Drozdowicz, Y.M.1    Jones, R.L.2
  • 8
    • 0031568218 scopus 로고    scopus 로고
    • In vivo phosphorylation of phosphoenolpyruvate carboxylase in guard cells of Vicia faba L. Is enhanced by fusicoccin and suppressed by abscisic acid
    • Du Z, Karthik A, Outlaw WH Jr (1997) In vivo phosphorylation of phosphoenolpyruvate carboxylase in guard cells of Vicia faba L. is enhanced by fusicoccin and suppressed by abscisic acid. Arch Biochem Biophys 337: 345-350
    • (1997) Arch Biochem Biophys , vol.337 , pp. 345-350
    • Du, Z.1    Karthik, A.2    Outlaw W.H., Jr.3
  • 9
    • 0029158988 scopus 로고
    • In vivo regulation of wheat-leaf phosphoenolpyruvate carboxylase by reversible phosphorylation
    • Duff SMG, Chollet R (1995) In vivo regulation of wheat-leaf phosphoenolpyruvate carboxylase by reversible phosphorylation. Plant Physiol 107: 775-782
    • (1995) Plant Physiol , vol.107 , pp. 775-782
    • Duff, S.M.G.1    Chollet, R.2
  • 11
    • 0025027207 scopus 로고
    • Reversible light activation of the phosphoenolpyruvate carboxylase proteinserine kinase in maize leaves
    • Echevarría C, Vidal J, Jiao J-A, Chollet R (1990) Reversible light activation of the phosphoenolpyruvate carboxylase proteinserine kinase in maize leaves. FEBS Lett 275: 25-28
    • (1990) FEBS Lett , vol.275 , pp. 25-28
    • Echevarría, C.1    Vidal, J.2    Jiao, J.-A.3    Chollet, R.4
  • 14
    • 0000069105 scopus 로고    scopus 로고
    • Signal transduction in barley aleurone protoplasts is calcium dependent and independent
    • Gilroy S (1996) Signal transduction in barley aleurone protoplasts is calcium dependent and independent. Plant Cell 8: 2193-2209
    • (1996) Plant Cell , vol.8 , pp. 2193-2209
    • Gilroy, S.1
  • 15
    • 0026534659 scopus 로고
    • Gibberellic acid and abscisic acid coordinately regulate cytoplasmic calcium and secretory activity in barley aleurone protoplast
    • Gilroy S, Jones RL (1992) Gibberellic acid and abscisic acid coordinately regulate cytoplasmic calcium and secretory activity in barley aleurone protoplast. Proc Natl Acad Sci USA 89: 3591-3595
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3591-3595
    • Gilroy, S.1    Jones, R.L.2
  • 16
    • 0032037523 scopus 로고    scopus 로고
    • Expression and localization of phosphoenolpyruvate carboxylase in developing and germinating wheat grains
    • González MC, Osuna L, Echevarría C, Vidal J, Cejudo J (1998) Expression and localization of phosphoenolpyruvate carboxylase in developing and germinating wheat grains. Plant Physiol 116: 1249-1258
    • (1998) Plant Physiol , vol.116 , pp. 1249-1258
    • González, M.C.1    Osuna, L.2    Echevarría, C.3    Vidal, J.4    Cejudo, J.5
  • 17
    • 0030482709 scopus 로고    scopus 로고
    • Higher plant phosphoenolpyruvate carboxylase kinase is regulated at the level of translatable mRNA in response to light or a circadian rhythm
    • Hartwell J, Smith LH, Wilkins MB, Jenkins GI, Nimmo HG (1996) Higher plant phosphoenolpyruvate carboxylase kinase is regulated at the level of translatable mRNA in response to light or a circadian rhythm. Plant J 10: 1071-1078
    • (1996) Plant J , vol.10 , pp. 1071-1078
    • Hartwell, J.1    Smith, L.H.2    Wilkins, M.B.3    Jenkins, G.I.4    Nimmo, H.G.5
  • 19
    • 0343374101 scopus 로고
    • N-(6-Aminohexyl)-5-chloro-1-naphthalenesulfonamide, a calmodulin antagonist, inhibits cell proliferation
    • Hidaka H, Sasaki Y, Tanaka T, Endo T, Ohno S, Fujii Y, Nagata T (1981) N-(6-Aminohexyl)-5-chloro-1-naphthalenesulfonamide, a calmodulin antagonist, inhibits cell proliferation. Proc Natl Acad Sci USA 78: 4354-4357
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 4354-4357
    • Hidaka, H.1    Sasaki, Y.2    Tanaka, T.3    Endo, T.4    Ohno, S.5    Fujii, Y.6    Nagata, T.7
  • 20
    • 0024637446 scopus 로고
    • 4 phosphoenolpyruvate carboxylase by a soluble protein kinase from maize leaves
    • 4 phosphoenolpyruvate carboxylase by a soluble protein kinase from maize leaves. Arch Biochem Biophys 269: 526-535
    • (1989) Arch Biochem Biophys , vol.269 , pp. 526-535
    • Jiao, J.-A.1    Chollet, R.2
  • 22
    • 0030087964 scopus 로고    scopus 로고
    • Okadaic acid, a protein phosphatase inhibitor, blocks calcium changes, gene expression, and cell death induced by gibberellin in wheat aleurone cells
    • Kuo A, Cappelluti S, Cervantes-Cervantes M, Rodriguez M, Bush DS (1996) Okadaic acid, a protein phosphatase inhibitor, blocks calcium changes, gene expression, and cell death induced by gibberellin in wheat aleurone cells. Plant Cell 8: 259-269
    • (1996) Plant Cell , vol.8 , pp. 259-269
    • Kuo, A.1    Cappelluti, S.2    Cervantes-Cervantes, M.3    Rodriguez, M.4    Bush, D.S.5
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0030752239 scopus 로고    scopus 로고
    • Regulatory phosphorylation of banana fruit phosphoenolpyruvate carboxylase by a copurifying phosphoenolpyruvate carboxylase-kinase
    • Law RD, Plaxton WC (1997) Regulatory phosphorylation of banana fruit phosphoenolpyruvate carboxylase by a copurifying phosphoenolpyruvate carboxylase-kinase. Eur J Biochem 247: 642-651
    • (1997) Eur J Biochem , vol.247 , pp. 642-651
    • Law, R.D.1    Plaxton, W.C.2
  • 25
    • 0027331397 scopus 로고
    • 4 phosphoenolpyruvate-carboxylase protein-kinase polypeptides and their reversible light activation in maize leaves
    • 4 phosphoenolpyruvate-carboxylase protein-kinase polypeptides and their reversible light activation in maize leaves. Arch Biochem Biophys 307: 416-419
    • (1993) Arch Biochem Biophys , vol.307 , pp. 416-419
    • Li, B.1    Chollet, R.2
  • 26
    • 0000612160 scopus 로고
    • Endosperm acidification and related metabolic changes in the developing barley grain
    • Macnicol PK, Jacobsen JV (1992) Endosperm acidification and related metabolic changes in the developing barley grain. Plant Physiol 98: 1098-1104
    • (1992) Plant Physiol , vol.98 , pp. 1098-1104
    • Macnicol, P.K.1    Jacobsen, J.V.2
  • 27
    • 0031818948 scopus 로고    scopus 로고
    • Role of phosphoenolpyruvate carboxylase in malate production by the developing barley aleurone layer
    • Macnicol PK, Raymond P (1998) Role of phosphoenolpyruvate carboxylase in malate production by the developing barley aleurone layer. Physiol Plant 103: 132-138
    • (1998) Physiol Plant , vol.103 , pp. 132-138
    • Macnicol, P.K.1    Raymond, P.2
  • 28
    • 0009321376 scopus 로고
    • Secretion of L-malic acid by barley aleurone layers
    • Mikola J, Virtanen M (1980) Secretion of L-malic acid by barley aleurone layers (abstract no. 783). Plant Physiol 65: S-142
    • (1980) Plant Physiol , vol.65
    • Mikola, J.1    Virtanen, M.2
  • 29
    • 0022802017 scopus 로고
    • Purification of the phosphorylated night form and dephosphorylated day form of phosphoenolpyruvate carboxylase from bryophyllum fedtschenkoi
    • Nimmo GA, Nimmo HG, Hamilton ID, Fewson CA, Wilkins MB (1986) Purification of the phosphorylated night form and dephosphorylated day form of phosphoenolpyruvate carboxylase from Bryophyllum fedtschenkoi. Biochem J 239: 213-220
    • (1986) Biochem J , vol.239 , pp. 213-220
    • Nimmo, G.A.1    Nimmo, H.G.2    Hamilton, I.D.3    Fewson, C.A.4    Wilkins, M.B.5
  • 30
    • 0026535168 scopus 로고
    • 2+-dependent protein kinase phosphorylates phosphorao/pyruvate carboxylase in maize
    • 2+-dependent protein kinase phosphorylates phosphorao/pyruvate carboxylase in maize. FEBS Lett 302: 86-88
    • (1992) FEBS Lett , vol.302 , pp. 86-88
    • Ogawa, N.1    Okumura, S.2    Izui, K.3
  • 31
    • 0000247316 scopus 로고    scopus 로고
    • In vivo and in vitro phosphorylation of the phosphoenolpyruvate carboxylase from wheat seeds during germination
    • Osuna L, González MC, Cejudo FJ, Vidal J, Echevarría C (1996) In vivo and in vitro phosphorylation of the phosphoenolpyruvate carboxylase from wheat seeds during germination. Plant Physiol 111: 551-558
    • (1996) Plant Physiol , vol.111 , pp. 551-558
    • Osuna, L.1    González, M.C.2    Cejudo, F.J.3    Vidal, J.4    Echevarría, C.5
  • 33
    • 0027751629 scopus 로고
    • Production and properties of recombinant C3-type phosphoenolpyruvate carboxylase from sorghum vulgare: In vitro phosphorylation by leaf and root pyrpc protein serine kinase
    • Pacquit V, Santi S, Cretin C, Bui VL, Vidal J, Gadal P (1993) Production and properties of recombinant C3-type phosphoenolpyruvate carboxylase from Sorghum vulgare: in vitro phosphorylation by leaf and root PyrPC protein serine kinase. Biochem Biophys Res Commun 197: 1415-1423
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 1415-1423
    • Pacquit, V.1    Santi, S.2    Cretin, C.3    Bui, V.L.4    Vidal, J.5    Gadal, P.6
  • 35
  • 36
    • 11944252555 scopus 로고
    • Calcium-modulated proteins: Target of intracellular calcium signals in higher plants
    • Roberts DM, Harmon AC (1992) Calcium-modulated proteins: target of intracellular calcium signals in higher plants. Annu Rev Plant Physiol Plant Mol Biol 43: 375-414
    • (1992) Annu Rev Plant Physiol Plant Mol Biol , vol.43 , pp. 375-414
    • Roberts, D.M.1    Harmon, A.C.2
  • 37
    • 0001221102 scopus 로고
    • Phosphoenolpyruvate carboxylase activity and concentration in the endosperm of developing and germinating castor oil seeds
    • Sangwan RS, Singh N, Plaxton WC (1992) Phosphoenolpyruvate carboxylase activity and concentration in the endosperm of developing and germinating castor oil seeds. Plant Physiol 99: 445-449
    • (1992) Plant Physiol , vol.99 , pp. 445-449
    • Sangwan, R.S.1    Singh, N.2    Plaxton, W.C.3
  • 38
    • 0001692673 scopus 로고
    • Phosphorylation of soybean (Glycine max L.) nodule phosphoenolpyruvate carboxylase in vitro decreases its sensitivity to inhibition by L-malate
    • Schuller KA, Werner D (1993) Phosphorylation of soybean (Glycine max L.) nodule phosphoenolpyruvate carboxylase in vitro decreases its sensitivity to inhibition by L-malate. Plant Physiol 101: 1267-1273
    • (1993) Plant Physiol , vol.101 , pp. 1267-1273
    • Schuller, K.A.1    Werner, D.2
  • 39
    • 0000665321 scopus 로고    scopus 로고
    • Modulation of calmodulin mRNA and protein levels in barley aleurone
    • Schuurink RC, Chan PV, Jones RL (1996) Modulation of calmodulin mRNA and protein levels in barley aleurone. Plant Physiol 111: 371-380
    • (1996) Plant Physiol , vol.111 , pp. 371-380
    • Schuurink, R.C.1    Chan, P.V.2    Jones, R.L.3
  • 40
    • 0029952805 scopus 로고    scopus 로고
    • Light regulation of phosphoenol-pyruvate carboxylase in barley mesophyll protoplasts is modulated by protein synthesis and calcium, and not necessarily correlated with phosphoenolpyruvate carboxylase kinase activity
    • Smith LH, Lillo C, Nimmo HG, Wilkins MB (1996) Light regulation of phosphoenol-pyruvate carboxylase in barley mesophyll protoplasts is modulated by protein synthesis and calcium, and not necessarily correlated with phosphoenolpyruvate carboxylase kinase activity. Planta 200: 174-180
    • (1996) Planta , vol.200 , pp. 174-180
    • Smith, L.H.1    Lillo, C.2    Nimmo, H.G.3    Wilkins, M.B.4
  • 41
    • 0000593284 scopus 로고    scopus 로고
    • Gibberellic acid induces vacuolar acidification in barley aleurone
    • Swanson SJ, Jones RJ (1996) Gibberellic acid induces vacuolar acidification in barley aleurone. Plant Cell 8: 2211-2221
    • (1996) Plant Cell , vol.8 , pp. 2211-2221
    • Swanson, S.J.1    Jones, R.J.2
  • 42
    • 0025164851 scopus 로고
    • 15 with a mammalian cyclic AMP-dependent protein kinase diminishes sensitivity to inhibition by malate
    • 15 with a mammalian cyclic AMP-dependent protein kinase diminishes sensitivity to inhibition by malate. FEBS Lett 259: 241-244
    • (1990) FEBS Lett , vol.259 , pp. 241-244
    • Terada, K.1    Kai, T.2    Okuno, S.3    Fujisawa, H.4    Izui, K.5
  • 44
    • 0002741914 scopus 로고
    • Recovery of active highly purified phosphoenolpyruvate carboxylase from specific immunoadsorbent column
    • Vidai J, Godbillon P, Gadal P (1981) Recovery of active highly purified phosphoenolpyruvate carboxylase from specific immunoadsorbent column. FEBS Lett 118: 31-34
    • (1981) FEBS Lett , vol.118 , pp. 31-34
    • Vidai, J.1    Godbillon, P.2    Gadal, P.3
  • 46
    • 0027328106 scopus 로고
    • Partial purification and characterization of phosphoenolpyruvate carboxylase protein-serine kinase from illuminated maize leaves
    • Wang YH, Chollet R (1993) Partial purification and characterization of phosphoenolpyruvate carboxylase protein-serine kinase from illuminated maize leaves. Arch Biochem Biophys 304: 496-502
    • (1993) Arch Biochem Biophys , vol.304 , pp. 496-502
    • Wang, Y.H.1    Chollet, R.2
  • 47
    • 0031571143 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase protein kinase from soybean root nodules: Partial purification, characterization, and up/down-regulation by photosynthate supply from the shoots
    • Zhang XQ, Chollet R (1997) Phosphoenolpyruvate carboxylase protein kinase from soybean root nodules: partial purification, characterization, and up/down-regulation by photosynthate supply from the shoots. Arch Biochem Biophys 343: 260-268
    • (1997) Arch Biochem Biophys , vol.343 , pp. 260-268
    • Zhang, X.Q.1    Chollet, R.2
  • 48
    • 0028873231 scopus 로고
    • In vitro regulatory phosphorylation of soybean nodule phosphoenolpyruvate carboxylase
    • Zhang XQ, Li B, Chollet R (1995) In vitro regulatory phosphorylation of soybean nodule phosphoenolpyruvate carboxylase. Plant Physiol 108: 1561-1568
    • (1995) Plant Physiol , vol.108 , pp. 1561-1568
    • Zhang, X.Q.1    Li, B.2    Chollet, R.3
  • 49
    • 0028021303 scopus 로고
    • Lessened malate inhibition of guard-cell phosphoenolpyruvate carboxylase velocity during stomatal opening
    • Zhang XQ, Outlaw WH Jr, Chollet R (1994) Lessened malate inhibition of guard-cell phosphoenolpyruvate carboxylase velocity during stomatal opening. FEBS Lett 352: 45-48
    • (1994) FEBS Lett , vol.352 , pp. 45-48
    • Zhang, X.Q.1    Outlaw W.H., Jr.2    Chollet, R.3


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