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Volumn 17, Issue 4, 1999, Pages 407-413

Site-directed mutagenesis of serine 158 demonstrates its role in spinach leaf sucrose-phosphate synthase modulation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME MODIFICATION; ENZYME PURIFICATION; MONOCLONAL ANTIBODY; PROTEIN PHOSPHORYLATION; SPINACH; SUCROSE PHOSPHATE SYNTHASE KINASE; SUCROSE PHOSPHATE SYNTHASE; TARGETED MUTAGENESIS; TOBACCO; TRANSGENE; TRANSGENIC PLANT;

EID: 0033082670     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1999.00389.x     Document Type: Article
Times cited : (42)

References (27)
  • 1
    • 0030602179 scopus 로고    scopus 로고
    • 14-3-3 proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform-specific manner and reduce dephosphorylation of Ser-543 by endogenous protein phosphatases
    • Bachmann, M., Huber, J.L., Athwal, G.S., Wu, K., Ferl, R.J. and Huber, S.C. (1996a) 14-3-3 proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform-specific manner and reduce dephosphorylation of Ser-543 by endogenous protein phosphatases. FEBS Lett. 398, 26-30.
    • (1996) FEBS Lett. , vol.398 , pp. 26-30
    • Bachmann, M.1    Huber, J.L.2    Athwal, G.S.3    Wu, K.4    Ferl, R.J.5    Huber, S.C.6
  • 2
    • 0029924885 scopus 로고    scopus 로고
    • The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 protein
    • Bachmann, M., Huber, J.L., Liao, P.-C., Gage, D.A. and Huber, S.C. (1996b) The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 protein. FEBS Lett. 387, 127-131.
    • (1996) FEBS Lett. , vol.387 , pp. 127-131
    • Bachmann, M.1    Huber, J.L.2    Liao, P.-C.3    Gage, D.A.4    Huber, S.C.5
  • 3
    • 0039437707 scopus 로고
    • The equilibrium of the reaction catalyzed by sucrose phosphate synthase
    • Barber, G.A. (1985) The equilibrium of the reaction catalyzed by sucrose phosphate synthase. Plant Physiol. 79, 1127-1128.
    • (1985) Plant Physiol. , vol.79 , pp. 1127-1128
    • Barber, G.A.1
  • 4
    • 0001084898 scopus 로고
    • Regulation of spinach leaf sucrose-phosphate synthase by glucose-6-phosphate, inorganic phosphate, and pH
    • Doehlert, D.C. and Huber, S.C. (1983) Regulation of spinach leaf sucrose-phosphate synthase by glucose-6-phosphate, inorganic phosphate, and pH. Plant Physiol. 73, 989-994.
    • (1983) Plant Physiol. , vol.73 , pp. 989-994
    • Doehlert, D.C.1    Huber, S.C.2
  • 5
    • 0001012359 scopus 로고
    • Biochemical and genetic analysis of different patatin isoforms expressed in various organs of potato (Solanum tuberosum L)
    • Hoefgen, R. and Willmitzer, L. (1990) Biochemical and genetic analysis of different patatin isoforms expressed in various organs of potato (Solanum tuberosum L). Plant Sci. 66, 221-230.
    • (1990) Plant Sci. , vol.66 , pp. 221-230
    • Hoefgen, R.1    Willmitzer, L.2
  • 6
    • 0026507983 scopus 로고
    • Site-specific serine phosphorylation of spinach leaf sucrose-phosphate synthase
    • Huber, J.L.A. and Huber, S.C. (1992a) Site-specific serine phosphorylation of spinach leaf sucrose-phosphate synthase. Biochem. J. 283, 877-882.
    • (1992) Biochem. J. , vol.283 , pp. 877-882
    • Huber, J.L.A.1    Huber, S.C.2
  • 7
    • 0040419081 scopus 로고    scopus 로고
    • Role and regulation of sucrose-phosphate synthase in higher plants
    • Huber, J.L.A. and Huber, S.C. (1996) Role and regulation of sucrose-phosphate synthase in higher plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47, 431-444.
    • (1996) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.47 , pp. 431-444
    • Huber, J.L.A.1    Huber, S.C.2
  • 8
    • 0024671488 scopus 로고
    • Protein phosphorylation as a mechanism for regulation of spinach leaf sucrose-phosphate synthase activity
    • Huber, J.L.A., Huber, S.C. and Nielsen, T.H. (1989a) Protein phosphorylation as a mechanism for regulation of spinach leaf sucrose-phosphate synthase activity. Arch. Biochem. Biophys. 270, 681-690.
    • (1989) Arch. Biochem. Biophys. , vol.270 , pp. 681-690
    • Huber, J.L.A.1    Huber, S.C.2    Nielsen, T.H.3
  • 9
    • 0001471155 scopus 로고
    • Role of sucrose-phosphate synthase in sucrose metabolism in leaves
    • Huber, S.C. and Huber, J.L. (1992b) Role of sucrose-phosphate synthase in sucrose metabolism in leaves. Plant Physiol. 99, 1275-1278.
    • (1992) Plant Physiol. , vol.99 , pp. 1275-1278
    • Huber, S.C.1    Huber, J.L.2
  • 10
    • 0002621297 scopus 로고
    • The regulation of sucrose synthesis in leaves
    • (Pollock, C.J., Farrar, J.F. and Gordon, A.J., eds). Oxford: Oxford University Press
    • Huber, S.C., Huber, J.L.A. and McMichael, R.W. Jr (1993) The regulation of sucrose synthesis in leaves. In Carbon Partitioning Within and Between Organisms (Pollock, C.J., Farrar, J.F. and Gordon, A.J., eds). Oxford: Oxford University Press, pp. 1-26.
    • (1993) Carbon Partitioning Within and Between Organisms , pp. 1-26
    • Huber, S.C.1    Huber, J.L.A.2    McMichael R.W., Jr.3
  • 12
    • 0002379220 scopus 로고
    • Variation among species in light activation of sucrose-phosphate synthase
    • Huber, S.C., Nielsen, T.H., Huber, J.L.A. and Pharr, D.M. (1989b) Variation among species in light activation of sucrose-phosphate synthase. Plant Cell Physiol. 30, 277-286.
    • (1989) Plant Cell Physiol. , vol.30 , pp. 277-286
    • Huber, S.C.1    Nielsen, T.H.2    Huber, J.L.A.3    Pharr, D.M.4
  • 13
    • 0026701313 scopus 로고
    • Rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Properties of phospho- and dephospho-forms and of two mutants in which Ser32 has been changed by site-directed mutagenesis
    • Kurland, I.J., el-Maghrabi, M.R., Correia, J.J. and Pilkis, S.J. (1992) Rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Properties of phospho- and dephospho-forms and of two mutants in which Ser32 has been changed by site-directed mutagenesis. J. Biol. Chem. 267, 4416-4423.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4416-4423
    • Kurland, I.J.1    El-Maghrabi, M.R.2    Correia, J.J.3    Pilkis, S.J.4
  • 14
    • 0001041359 scopus 로고
    • Purification and properties of sucrose-phosphate synthase from seeds of Pisum sativum
    • Lunn, J.E. and ap Rees, T. (1990) Purification and properties of sucrose-phosphate synthase from seeds of Pisum sativum. Phytochem. 29, 1057-1064.
    • (1990) Phytochem. , vol.29 , pp. 1057-1064
    • Lunn, J.E.1    Ap Rees, T.2
  • 15
    • 0028795834 scopus 로고
    • Spinach leaf sucrose-phosphate synthase and nitrate reductase are phosphorylated/inactivated by multiple protein kinases in vitro
    • McMichael, R.W. Jr, Bachmann, M. and Huber, S.C. (1995) Spinach leaf sucrose-phosphate synthase and nitrate reductase are phosphorylated/inactivated by multiple protein kinases in vitro. Plant Physiol. 108, 1077-1082.
    • (1995) Plant Physiol. , vol.108 , pp. 1077-1082
    • McMichael R.W., Jr.1    Bachmann, M.2    Huber, S.C.3
  • 16
    • 0027133515 scopus 로고
    • Identification of the major regulatory phosphorylation site in sucrose-phosphate synthase
    • McMichael, R.W. Jr, Klein, R.R., Salvucci, M.E. and Huber, S.C. (1993) Identification of the major regulatory phosphorylation site in sucrose-phosphate synthase. Arch. Biochem. Biophys. 307, 248-252.
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 248-252
    • McMichael R.W., Jr.1    Klein, R.R.2    Salvucci, M.E.3    Huber, S.C.4
  • 17
    • 0024278583 scopus 로고
    • Yeast (Saccharomyces cerevisiae) fructose-1,6-bisphosphatase. Properties of phospho and dephospho forms and of two mutants in which serine 11 has been changed by site-directed mutagenesis
    • Marcus, F., Rittenhouse, J., Moberly, L., Edelstein, I., Hiller, E. and Rogers, D.T. (1988) Yeast (Saccharomyces cerevisiae) fructose-1,6-bisphosphatase. Properties of phospho and dephospho forms and of two mutants in which serine 11 has been changed by site-directed mutagenesis. J. Biol. Chem. 263, 6058-6062.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6058-6062
    • Marcus, F.1    Rittenhouse, J.2    Moberly, L.3    Edelstein, I.4    Hiller, E.5    Rogers, D.T.6
  • 18
    • 0028150472 scopus 로고
    • Sucrose phosphate synthase is regulated, via metabolites and protein phosphorylation in potato tubers, in a manner analogous to the enzyme in leaves
    • Reimholz, R., Geigenberger, P. and Stitt, M. (1994) Sucrose phosphate synthase is regulated, via metabolites and protein phosphorylation in potato tubers, in a manner analogous to the enzyme in leaves. Planta, 192, 480-488.
    • (1994) Planta , vol.192 , pp. 480-488
    • Reimholz, R.1    Geigenberger, P.2    Stitt, M.3
  • 19
    • 0001646879 scopus 로고
    • Expression of a tuber-specific storage protein in transgenic tobacco plants: Demonstration of an esterase activity
    • Rosahl, S., Schell, J. and Willmitzer, L. (1987) Expression of a tuber-specific storage protein in transgenic tobacco plants: demonstration of an esterase activity. EMBO J. 6, 1155-1159.
    • (1987) EMBO J. , vol.6 , pp. 1155-1159
    • Rosahl, S.1    Schell, J.2    Willmitzer, L.3
  • 20
    • 0024991575 scopus 로고
    • Sucrose-phosphate synthase is dephosphorylated by protein phosphatase 2A in spinach leaves. Evidence from the effects of okadaic acid and microcystin
    • Siegl, G., MacKintosh, C. and Stitt, M. (1990) Sucrose-phosphate synthase is dephosphorylated by protein phosphatase 2A in spinach leaves. Evidence from the effects of okadaic acid and microcystin. FEBS Lett. 270, 198-202.
    • (1990) FEBS Lett. , vol.270 , pp. 198-202
    • Siegl, G.1    MacKintosh, C.2    Stitt, M.3
  • 21
    • 0027549493 scopus 로고
    • Purification, cloning and expression of spinach leaf sucrose-phosphate synthase in Escherichia coli
    • Sonnewald, U., Quick, W.P., MacRae, E., Krause, K.P. and Stitt, M. (1993) Purification, cloning and expression of spinach leaf sucrose-phosphate synthase in Escherichia coli. Planta, 189, 174-181.
    • (1993) Planta , vol.189 , pp. 174-181
    • Sonnewald, U.1    Quick, W.P.2    MacRae, E.3    Krause, K.P.4    Stitt, M.5
  • 22
    • 0000846432 scopus 로고
    • Control of photosynthetic sucrose formation
    • (Hatch, M.D. and Boardman, N.K., eds). New York: Academic Press
    • Stitt, M., Huber, S.C. and Kerr, P.S. (1987) Control of photosynthetic sucrose formation. In Biochemistry of Plants, Volume 10 (Hatch, M.D. and Boardman, N.K., eds). New York: Academic Press, pp. 328-409.
    • (1987) Biochemistry of Plants , vol.10 , pp. 328-409
    • Stitt, M.1    Huber, S.C.2    Kerr, P.S.3
  • 23
    • 0000007754 scopus 로고
    • Coarse control of sucrose-phosphate synthase in leaves: Alterations of the kinetic properties in response to the rate of photosynthesis and the accumulation of sucrose
    • Stitt, M., Wilke, I., Feil, R. and Heldt, H.W. (1988) Coarse control of sucrose-phosphate synthase in leaves: alterations of the kinetic properties in response to the rate of photosynthesis and the accumulation of sucrose. Planta, 174, 217-230.
    • (1988) Planta , vol.174 , pp. 217-230
    • Stitt, M.1    Wilke, I.2    Feil, R.3    Heldt, H.W.4
  • 24
    • 0023645302 scopus 로고
    • Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate
    • Thorsness, P.E. and Koshland, D.E. Jr (1987) Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate. J. Biol. Chem. 262, 10422-10425.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10422-10425
    • Thorsness, P.E.1    Koshland D.E., Jr.2
  • 25
    • 0031177703 scopus 로고    scopus 로고
    • Protein phosphorylation as a mechanism for regulation of sucrose-phosphate synthase under osmotic stress conditions
    • Toroser, D. and Huber, S.C. (1997) Protein phosphorylation as a mechanism for regulation of sucrose-phosphate synthase under osmotic stress conditions. Plant Physiol. 114, 947-955.
    • (1997) Plant Physiol. , vol.114 , pp. 947-955
    • Toroser, D.1    Huber, S.C.2
  • 26
    • 0001647909 scopus 로고
    • Purification and preliminary characterization of sucrose-phosphate synthase using monoclonal antibodies
    • Walker, J.L. and Huber, S.C. (1989) Purification and preliminary characterization of sucrose-phosphate synthase using monoclonal antibodies. Plant Physiol. 89, 518-524.
    • (1989) Plant Physiol. , vol.89 , pp. 518-524
    • Walker, J.L.1    Huber, S.C.2


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