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Volumn 237, Issue 5, 2013, Pages 1401-1413

Factors involved in the rise of phosphoenolpyruvate carboxylase-kinase activity caused by salinity in sorghum leaves

Author keywords

Calcium dependent protein kinase; Phosphoenolpyruvate carboxylase; Phosphoenolpyruvate carboxylase kinase; Protein turnover; Regulatory phosphorylation; Salt stress; Sorghum; Ubiquitin proteasome

Indexed keywords

PHOSPHOENOLPYRUVATE CARBOXYLASE KINASE; PROTEIN SERINE THREONINE KINASE; SODIUM CHLORIDE; VEGETABLE PROTEIN;

EID: 84876718233     PISSN: 00320935     EISSN: 14322048     Source Type: Journal    
DOI: 10.1007/s00425-013-1855-7     Document Type: Article
Times cited : (35)

References (69)
  • 2
    • 0038119834 scopus 로고    scopus 로고
    • A conserved 19-amino acid synthetic peptide from the carboxy terminus of phosphoenolpyruvate carboxylase inhibits the in vitro phosphorylation of the enzyme by the calcium-independent phosphoenolpyruvate carboxylase kinase
    • Alvarez R, García-Mauriño S, Feria AB, Vidal J, Echevarría C (2003) A conserved 19-amino acid synthetic peptide from the carboxy terminus of phosphoenolpyruvate carboxylase inhibits the in vitro phosphorylation of the enzyme by the calcium-independent phosphoenolpyruvate carboxylase kinase. Plant Physiol 132: 1097-1106.
    • (2003) Plant Physiol , vol.132 , pp. 1097-1106
    • Alvarez, R.1    García-Mauriño, S.2    Feria, A.B.3    Vidal, J.4    Echevarría, C.5
  • 3
    • 0001647194 scopus 로고
    • Exogenous ABA as a modulator of the response of sorghum to high salinity
    • Amzallag GN, Lerner HR, Poljakoff-Mayber A (1990) Exogenous ABA as a modulator of the response of sorghum to high salinity. J Exp Bot 41: 1529-1534.
    • (1990) J Exp Bot , vol.41 , pp. 1529-1534
    • Amzallag, G.N.1    Lerner, H.R.2    Poljakoff-Mayber, A.3
  • 4
    • 15744398974 scopus 로고    scopus 로고
    • Genome-wide identification of the rice calcium-dependent protein kinase and its closely related kinase gene families: comprehensive analysis of the CDPKs gene family in rice
    • Asano T, Tanaka N, Yang GX, Hayashi N, Komatsu S (2005) Genome-wide identification of the rice calcium-dependent protein kinase and its closely related kinase gene families: comprehensive analysis of the CDPKs gene family in rice. Plant Cell Physiol 46: 356-366.
    • (2005) Plant Cell Physiol , vol.46 , pp. 356-366
    • Asano, T.1    Tanaka, N.2    Yang, G.X.3    Hayashi, N.4    Komatsu, S.5
  • 7
    • 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
  • 8
    • 20444374151 scopus 로고    scopus 로고
    • Eto Brute? Role of ACS turnover in regulating ethylene biosynthesis
    • Chae HS, Kieber JJ (2005) Eto Brute? Role of ACS turnover in regulating ethylene biosynthesis. Trends Plant Sci 10: 291-296.
    • (2005) Trends Plant Sci , vol.10 , pp. 291-296
    • Chae, H.S.1    Kieber, J.J.2
  • 9
    • 84862972606 scopus 로고    scopus 로고
    • Cloning of a calcium-dependent protein kinase gene NtCDPK12, and its induced expression by high-salt and drought in Nicotiana tabacum
    • Chen S, Liu GS, Wang YY, Sun YH, Chen J (2011) Cloning of a calcium-dependent protein kinase gene NtCDPK12, and its induced expression by high-salt and drought in Nicotiana tabacum. J Integr Agric 12: 1851-1860.
    • (2011) J Integr Agric , vol.12 , pp. 1851-1860
    • Chen, S.1    Liu, G.S.2    Wang, Y.Y.3    Sun, Y.H.4    Chen, J.5
  • 10
    • 0035983609 scopus 로고    scopus 로고
    • Calcium signaling through protein kinases. The Arabidopsis calcium-dependent protein kinase gene family
    • Cheng SH, Willmann MR, Chen HC, Sheen J (2002) Calcium signaling through protein kinases. The Arabidopsis calcium-dependent protein kinase gene family. Plant Physiol 129: 469-485.
    • (2002) Plant Physiol , vol.129 , pp. 469-485
    • Cheng, S.H.1    Willmann, M.R.2    Chen, H.C.3    Sheen, J.4
  • 13
    • 77950638285 scopus 로고    scopus 로고
    • Expressional analysis and role of calcium regulated kinases in abiotic stress signalling
    • Das R, Pandey GK (2010) Expressional analysis and role of calcium regulated kinases in abiotic stress signalling. Curr Genomics 11: 2-13.
    • (2010) Curr Genomics , vol.11 , pp. 2-13
    • Das, R.1    Pandey, G.K.2
  • 15
    • 0242416930 scopus 로고    scopus 로고
    • The unique phosphoenolpyruvate carboxylase kinase
    • Echevarría C, Vidal J (2003) The unique phosphoenolpyruvate carboxylase kinase. Plant Physiol Biochem 41: 541-547.
    • (2003) Plant Physiol Biochem , vol.41 , pp. 541-547
    • Echevarría, C.1    Vidal, J.2
  • 16
    • 0025027207 scopus 로고
    • Reversible light activation of phosphoenolpyruvate carboxylase protein-serine kinase in maize leaves
    • Echevarría C, Vidal J, Jiao JA, Chollet R (1990) Reversible light activation of phosphoenolpyruvate carboxylase protein-serine 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
  • 20
    • 57749107450 scopus 로고    scopus 로고
    • Regulation of phosphoenolpyruvate carboxylase phosphorylation by metabolites and abscisic acid during the development and germination of barley seeds
    • Feria AB, Alvarez R, Cochereau L, Vidal J, García-Mauriño S, Echevarría C (2008) Regulation of phosphoenolpyruvate carboxylase phosphorylation by metabolites and abscisic acid during the development and germination of barley seeds. Plant Physiol 148: 761-774.
    • (2008) Plant Physiol , vol.148 , pp. 761-774
    • Feria, A.B.1    Alvarez, R.2    Cochereau, L.3    Vidal, J.4    García-Mauriño, S.5    Echevarría, C.6
  • 21
    • 0036159274 scopus 로고    scopus 로고
    • Arabidopsis thaliana contains two phosphoenolpyruvate carboxylase kinase genes with different expression patterns
    • Fontaine V, Hartwell J, Jenkins GI, Nimmo GA, Nimmo HG (2002) Arabidopsis thaliana contains two phosphoenolpyruvate carboxylase kinase genes with different expression patterns. Plant Cell Environ 25: 115-122.
    • (2002) Plant Cell Environ , vol.25 , pp. 115-122
    • Fontaine, V.1    Hartwell, J.2    Jenkins, G.I.3    Nimmo, G.A.4    Nimmo, H.G.5
  • 22
    • 33745678052 scopus 로고    scopus 로고
    • Characterization and functional analysis of phosphoenolpyruvate carboxylase kinase genes in rice
    • Fukayama H, Tamai T, Taniguchi Y, Sullivan S, Miyao M, Nimmo HG (2006) Characterization and functional analysis of phosphoenolpyruvate carboxylase kinase genes in rice. Plant J 47: 258-268.
    • (2006) Plant J , vol.47 , pp. 258-268
    • Fukayama, H.1    Tamai, T.2    Taniguchi, Y.3    Sullivan, S.4    Miyao, M.5    Nimmo, H.G.6
  • 24
    • 85099527220 scopus 로고    scopus 로고
    • 4 PEPC from sorghum leaves is specifically activated by a synthetic peptide from its C-terminal
    • 4 PEPC from sorghum leaves is specifically activated by a synthetic peptide from its C-terminal. Physiol Plant 133: P11-P124.
    • (2008) Physiol Plant , vol.133
    • Gandullo, J.1    Alvarez, R.2    Echevarría, C.3
  • 25
    • 84858861967 scopus 로고    scopus 로고
    • Characterization of StABF1, a stress-responsive bZIP transcription factor from Solanum tuberosum L. that is phosphorylated by StCDPK2 in vitro
    • García MN, Giammaria V, Grandellis C, Téllez-Iñón MT, Ulloa RM, Capiati DA (2012) Characterization of StABF1, a stress-responsive bZIP transcription factor from Solanum tuberosum L. that is phosphorylated by StCDPK2 in vitro. Planta 235: 761-778.
    • (2012) Planta , vol.235 , pp. 761-778
    • García, M.N.1    Giammaria, V.2    Grandellis, C.3    Téllez-Iñón, M.T.4    Ulloa, R.M.5    Capiati, D.A.6
  • 26
    • 0038581911 scopus 로고    scopus 로고
    • Characterization of salt stress-enhanced phosphoenolpyruvate carboxylase kinase activity in leaves of Sorghum vulgare: independence from osmotic stress, involvement of ion toxicity and significance of dark phosphorylation
    • García-Mauriño S, Monreal JA, Alvarez R, Vidal J, Echevarría C (2003) Characterization of salt stress-enhanced phosphoenolpyruvate carboxylase kinase activity in leaves of Sorghum vulgare: independence from osmotic stress, involvement of ion toxicity and significance of dark phosphorylation. Planta 216: 648-655.
    • (2003) Planta , vol.216 , pp. 648-655
    • García-Mauriño, S.1    Monreal, J.A.2    Alvarez, R.3    Vidal, J.4    Echevarría, C.5
  • 28
    • 0037934476 scopus 로고    scopus 로고
    • Abiotic stresses affecting water balance induce phosphoenolpyruvate carboxylase expression in roots of wheat seedlings
    • Gonzalez MC, Sanchez R, Cejudo FJ (2003) Abiotic stresses affecting water balance induce phosphoenolpyruvate carboxylase expression in roots of wheat seedlings. Planta 216: 985-992.
    • (2003) Planta , vol.216 , pp. 985-992
    • Gonzalez, M.C.1    Sanchez, R.2    Cejudo, F.J.3
  • 29
    • 26444479151 scopus 로고    scopus 로고
    • Metabolite and post-translational control of phosphoenolpyruvate carboxylase from leaves and mesophyll cell protoplasts of Arabidopsis thaliana
    • Gousset-Dupont A, Lebouteiller B, Monreal J, Echevarría C, Pierre JN, Hodges M, Vidal J (2005) Metabolite and post-translational control of phosphoenolpyruvate carboxylase from leaves and mesophyll cell protoplasts of Arabidopsis thaliana. Plant Sci 169: 96-1101.
    • (2005) Plant Sci , vol.169 , pp. 96-1101
    • Gousset-Dupont, A.1    Lebouteiller, B.2    Monreal, J.3    Echevarría, C.4    Pierre, J.N.5    Hodges, M.6    Vidal, J.7
  • 30
    • 65649103703 scopus 로고    scopus 로고
    • In vivo regulatory phosphorylation of the phosphoenolpyruvate carboxylase AtPPC1 in phosphate-starved Arabidopsis thaliana
    • Gregory AL, Hurley BA, Tran HT, Valentine AJ, She YM, Knowles VL, Plaxton WC (2009) In vivo regulatory phosphorylation of the phosphoenolpyruvate carboxylase AtPPC1 in phosphate-starved Arabidopsis thaliana. Biochem J 420: 57-65.
    • (2009) Biochem J , vol.420 , pp. 57-65
    • Gregory, A.L.1    Hurley, B.A.2    Tran, H.T.3    Valentine, A.J.4    She, Y.M.5    Knowles, V.L.6    Plaxton, W.C.7
  • 31
    • 0033231543 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase kinase is a novel protein kinase regulated at the level of expression
    • Hartwell J, Gill A, Nimmo GA, Wilkins MB, Jenkins GI, Nimmo HG (1999) Phosphoenolpyruvate carboxylase kinase is a novel protein kinase regulated at the level of expression. Plant J 20: 333-342.
    • (1999) Plant J , vol.20 , pp. 333-342
    • Hartwell, J.1    Gill, A.2    Nimmo, G.A.3    Wilkins, M.B.4    Jenkins, G.I.5    Nimmo, H.G.6
  • 34
    • 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 Nat Acad Sci USA 78: 4354-4357.
    • (1981) Proc Nat 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
  • 36
    • 3242719687 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase: a new era of structural biology
    • Izui K, Matsumura H, Furumoto T, Kai Y (2004) Phosphoenolpyruvate carboxylase: a new era of structural biology. Annu Rev Plant Biol 55: 69-84.
    • (2004) Annu Rev Plant Biol , vol.55 , pp. 69-84
    • Izui, K.1    Matsumura, H.2    Furumoto, T.3    Kai, Y.4
  • 37
    • 77957226474 scopus 로고    scopus 로고
    • Turnover of LeACS2, a wound-inducible 1-aminocyclopropane-1-carboxylic acid synthase in tomato, is regulated by phosphorylation/dephosphorylation
    • Kamiyoshihara Y, Iwata M, Fukaya T, Tatsuki M, Mori H (2010) Turnover of LeACS2, a wound-inducible 1-aminocyclopropane-1-carboxylic acid synthase in tomato, is regulated by phosphorylation/dephosphorylation. Plant J 64: 140-150.
    • (2010) Plant J , vol.64 , pp. 140-150
    • Kamiyoshihara, Y.1    Iwata, M.2    Fukaya, T.3    Tatsuki, M.4    Mori, H.5
  • 38
    • 0025158107 scopus 로고
    • Protein kinase recognition sequence motifs
    • Kemp BE, Pearson RB (1990) Protein kinase recognition sequence motifs. Trends Biochem Sci 15: 342-346.
    • (1990) Trends Biochem Sci , vol.15 , pp. 342-346
    • Kemp, B.E.1    Pearson, R.B.2
  • 40
    • 0032510705 scopus 로고    scopus 로고
    • Kinetic and calcium-binding properties of three calcium-dependent protein kinase isoenzymes from soybean
    • Lee YJ, Yoo BC, Harmon AC (1998) Kinetic and calcium-binding properties of three calcium-dependent protein kinase isoenzymes from soybean. Biochemistry 37: 6801-6809.
    • (1998) Biochemistry , vol.37 , pp. 6801-6809
    • Lee, Y.J.1    Yoo, B.C.2    Harmon, A.C.3
  • 41
    • 0000148601 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase kinase in tobacco leaves is activated by light in a similar but not identical way as in maize
    • Li B, Zhang XQ, Chollet R (1996) Phosphoenolpyruvate carboxylase kinase in tobacco leaves is activated by light in a similar but not identical way as in maize. Plant Physiol 111: 497-505.
    • (1996) Plant Physiol , vol.111 , pp. 497-505
    • Li, B.1    Zhang, X.Q.2    Chollet, R.3
  • 42
    • 50949092777 scopus 로고    scopus 로고
    • Biotic and abiotic stress responses through calcium-dependent protein kinase (CDPK) signaling in wheat (Triticum aestivum L.)
    • Li A, Wang X, Leseberg CH, Jia J, Mao L (2008) Biotic and abiotic stress responses through calcium-dependent protein kinase (CDPK) signaling in wheat (Triticum aestivum L.). Plant Signal Behav 3: 654-656.
    • (2008) Plant Signal Behav , vol.3 , pp. 654-656
    • Li, A.1    Wang, X.2    Leseberg, C.H.3    Jia, J.4    Mao, L.5
  • 43
    • 0345791401 scopus 로고    scopus 로고
    • Structure and expression of phosphoenolpyruvate carboxylase kinase genes in solanaceae. A novel gene exhibits alternative splicing
    • Marsh JT, Sullivan S, Hartwell J, Nimmo HG (2003) Structure and expression of phosphoenolpyruvate carboxylase kinase genes in solanaceae. A novel gene exhibits alternative splicing. Plant Physiol 133: 2021-2028.
    • (2003) Plant Physiol , vol.133 , pp. 2021-2028
    • Marsh, J.T.1    Sullivan, S.2    Hartwell, J.3    Nimmo, H.G.4
  • 46
    • 33847291932 scopus 로고    scopus 로고
    • Effect of LiCl on phosphoenolpyruvate carboxylase kinase and the phosphorylation of phosphoenolpyruvate carboxylase in leaf disks and leaves of Sorghum vulgare
    • Monreal JA, López-Baena FJ, Vidal J, Echevarría C, García-Mauriño S (2007b) Effect of LiCl on phosphoenolpyruvate carboxylase kinase and the phosphorylation of phosphoenolpyruvate carboxylase in leaf disks and leaves of Sorghum vulgare. Planta 225: 801-812.
    • (2007) Planta , vol.225 , pp. 801-812
    • Monreal, J.A.1    López-Baena, F.J.2    Vidal, J.3    Echevarría, C.4    García-Mauriño, S.5
  • 47
    • 77954692389 scopus 로고    scopus 로고
    • Involvement of phospholipase D and phosphatidic acid in the light-dependent up-regulation of sorghum leaf phosphoenolpyruvate carboxylase-kinase
    • Monreal JA, López-Baena FJ, Vidal J, Echevarría C, García-Mauriño S (2010) Involvement of phospholipase D and phosphatidic acid in the light-dependent up-regulation of sorghum leaf phosphoenolpyruvate carboxylase-kinase. J Exp Bot 61: 2819-2827.
    • (2010) J Exp Bot , vol.61 , pp. 2819-2827
    • Monreal, J.A.1    López-Baena, F.J.2    Vidal, J.3    Echevarría, C.4    García-Mauriño, S.5
  • 48
    • 0035209387 scopus 로고    scopus 로고
    • Phosphatidic acid: an emerging plant lipid second messenger
    • Munnik T (2001) Phosphatidic acid: an emerging plant lipid second messenger. Trends Plant Sci 6: 227-233.
    • (2001) Trends Plant Sci , vol.6 , pp. 227-233
    • Munnik, T.1
  • 49
    • 0029173702 scopus 로고
    • G protein activation stimulates phospholipase D signaling in plants
    • Munnik T, Arisz SA, de Vrije T, Musgrave A (1995) G protein activation stimulates phospholipase D signaling in plants. Plant Cell 7: 2197-2210.
    • (1995) Plant Cell , vol.7 , pp. 2197-2210
    • Munnik, T.1    Arisz, S.A.2    de Vrije, T.3    Musgrave, A.4
  • 50
    • 0002026818 scopus 로고
    • Changes in the kinetic properties and phosphorylation state of phosphoenolpyruvate carboxylase in Zea mays leaves in response to light and dark
    • Nimmo GA, McNaughton GAL, Fewson CA, Wilkins MB, Nimmo HG (1987) Changes in the kinetic properties and phosphorylation state of phosphoenolpyruvate carboxylase in Zea mays leaves in response to light and dark. FEBS Lett 213: 18-22.
    • (1987) FEBS Lett , vol.213 , pp. 18-22
    • Nimmo, G.A.1    McNaughton, G.A.L.2    Fewson, C.A.3    Wilkins, M.B.4    Nimmo, H.G.5
  • 51
    • 0034931337 scopus 로고    scopus 로고
    • Partial purification and characterization of a protein inhibitor of phosphoenolpyruvate carboxylase kinase
    • Nimmo GA, Wilkins MB, Nimmo HG (2001) Partial purification and characterization of a protein inhibitor of phosphoenolpyruvate carboxylase kinase. Planta 213: 250-257.
    • (2001) Planta , vol.213 , pp. 250-257
    • Nimmo, G.A.1    Wilkins, M.B.2    Nimmo, H.G.3
  • 54
    • 0012301153 scopus 로고
    • Involvement of abscisic acid in photosynthetic process in Hordeum vulgare L. during salinity stress
    • Popova LP, Stoinova ZG, Maslenkova LT (1995) Involvement of abscisic acid in photosynthetic process in Hordeum vulgare L. during salinity stress. J Plant Growth Regul 14: 211-218.
    • (1995) J Plant Growth Regul , vol.14 , pp. 211-218
    • Popova, L.P.1    Stoinova, Z.G.2    Maslenkova, L.T.3
  • 55
    • 77953598327 scopus 로고    scopus 로고
    • Water for agriculture: maintaining food security under growing scarcity
    • Rosegrant MW, Ringler C, Zhu T (2009) Water for agriculture: maintaining food security under growing scarcity. Annu Rev Enviro Resour 34: 205-222.
    • (2009) Annu Rev Enviro Resour , vol.34 , pp. 205-222
    • Rosegrant, M.W.1    Ringler, C.2    Zhu, T.3
  • 56
    • 0033624156 scopus 로고    scopus 로고
    • 2+-dependent protein kinase confers both cold and salt/drought tolerance on rice plants
    • 2+-dependent protein kinase confers both cold and salt/drought tolerance on rice plants. Plant J 23: 319-327.
    • (2000) Plant J , vol.23 , pp. 319-327
    • Saijo, Y.1    Hata, S.2    Kyozuka, J.3    Shimamoto, K.4    Izui, K.5
  • 57
    • 0023375195 scopus 로고
    • The neighbour-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N, Nei M (1987) The neighbour-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4: 406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 58
    • 33645243627 scopus 로고    scopus 로고
    • Arabidopsis phosphoenolpyruvate carboxylase genes encode immunologically unrelated polypeptides and are differentially expressed in response to drought and salt stress
    • Sanchez R, Flores A, Cejudo FJ (2006) Arabidopsis phosphoenolpyruvate carboxylase genes encode immunologically unrelated polypeptides and are differentially expressed in response to drought and salt stress. Planta 223: 901-909.
    • (2006) Planta , vol.223 , pp. 901-909
    • Sanchez, R.1    Flores, A.2    Cejudo, F.J.3
  • 62
    • 0001393755 scopus 로고
    • Generation and maintenance of concentration gradients between the mesophyll and bundle sheath in maize leaves
    • Stitt M, Heldt HW (1985) Generation and maintenance of concentration gradients between the mesophyll and bundle sheath in maize leaves. Biochim Biophys Acta 808: 400-414.
    • (1985) Biochim Biophys Acta , vol.808 , pp. 400-414
    • Stitt, M.1    Heldt, H.W.2
  • 63
    • 4444234182 scopus 로고    scopus 로고
    • Roots, cycles and leaves. Expression of the phosphoenolpyruvate carboxylase kinase gene family in soybean
    • Sullivan S, Jenkins GI, Nimmo HG (2004) Roots, cycles and leaves. Expression of the phosphoenolpyruvate carboxylase kinase gene family in soybean. Plant Physiol 135: 2078-2087.
    • (2004) Plant Physiol , vol.135 , pp. 2078-2087
    • Sullivan, S.1    Jenkins, G.I.2    Nimmo, H.G.3
  • 64
    • 15744386874 scopus 로고    scopus 로고
    • Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused desensitization and abolished responsiveness to regulatory phosphorylation
    • Takahashi-Terada A, Kotera M, Ohshima K, Furumoto T, Matsumura H, Kai Y, Izui K (2005) Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused desensitization and abolished responsiveness to regulatory phosphorylation. J Biol Chem 280: 11798-11806.
    • (2005) J Biol Chem , vol.280 , pp. 11798-11806
    • Takahashi-Terada, A.1    Kotera, M.2    Ohshima, K.3    Furumoto, T.4    Matsumura, H.5    Kai, Y.6    Izui, K.7
  • 65
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28: 2731-2739.
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 66
    • 0037699019 scopus 로고    scopus 로고
    • A novel C-terminal proteolytic processing of cytosolic pyruvate kinase, its phosphorylation and degradation by the proteasome in developing soybean seeds
    • Tang GQ, Hardin SC, Dewey R, Huber SC (2003) A novel C-terminal proteolytic processing of cytosolic pyruvate kinase, its phosphorylation and degradation by the proteasome in developing soybean seeds. Plant J 34: 77-99.
    • (2003) Plant J , vol.34 , pp. 77-99
    • Tang, G.Q.1    Hardin, S.C.2    Dewey, R.3    Huber, S.C.4
  • 67
    • 0035798058 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase kinase involved in C4 photosynthesis in Flaveria trinervia: cDNA cloning and characterization
    • Tsuchida Y, Furumoto T, Izumida A, Hata S, Izui K (2001) Phosphoenolpyruvate carboxylase kinase involved in C4 photosynthesis in Flaveria trinervia: cDNA cloning and characterization. FEBS Lett 507: 318-322.
    • (2001) FEBS Lett , vol.507 , pp. 318-322
    • Tsuchida, Y.1    Furumoto, T.2    Izumida, A.3    Hata, S.4    Izui, K.5
  • 69
    • 0035213385 scopus 로고    scopus 로고
    • Plant salt tolerance
    • Zhu JK (2001) Plant salt tolerance. Trends Plant Sci 6: 66-71.
    • (2001) Trends Plant Sci , vol.6 , pp. 66-71
    • Zhu, J.K.1


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