메뉴 건너뛰기




Volumn 119, Issue 1, 1999, Pages 219-229

A conserved acidic motif in the N-terminal domain of nitrate reductase is necessary for the inactivation of the enzyme in the dark by phosphorylation and 14-3-3 binding

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL SEQUENCE; CASEIN KINASE II; DELETION MUTAGENESIS; ENZYME INACTIVATION; ENZYME STRUCTURE; NICOTIANA PLUMBAGINIFOLIA; NITRATE REDUCTASE; PHOSPHORYLATION; PROMOTER REGION;

EID: 0032840889     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.119.1.219     Document Type: Article
Times cited : (24)

References (48)
  • 1
    • 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 JL, Liao P-C, Gage DA, Huber SC (1996a) 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
  • 2
    • 0030096855 scopus 로고    scopus 로고
    • Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase
    • Bachmann M, Shiraishi N, Campbell WH, Yoo B-C, Harmon AC, Huber SC (1996b) Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase. Plant Cell 8: 505-517
    • (1996) Plant Cell , vol.8 , pp. 505-517
    • Bachmann, M.1    Shiraishi, N.2    Campbell, W.H.3    Yoo, B.-C.4    Harmon, A.C.5    Huber, S.C.6
  • 3
    • 0021771482 scopus 로고
    • Binary Agrobacterium vectors for plant transformation
    • Bevan M (1984) Binary Agrobacterium vectors for plant transformation. Nucleic Acids Res 12: 8711-8721
    • (1984) Nucleic Acids Res , vol.12 , pp. 8711-8721
    • Bevan, M.1
  • 4
    • 0000182975 scopus 로고
    • XL1-Blue: A high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection
    • Bullock WO, Fernandez JM, Short JM (1987) XL1-Blue: a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection. Biotechniques 5: 376-378
    • (1987) Biotechniques , vol.5 , pp. 376-378
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 5
    • 0000324745 scopus 로고    scopus 로고
    • Nitrate reductase biochemistry comes of age
    • Campbell WH (1996) Nitrate reductase biochemistry comes of age. Plant Physiol 111: 355-361
    • (1996) Plant Physiol , vol.111 , pp. 355-361
    • Campbell, W.H.1
  • 6
    • 0028089888 scopus 로고
    • An efficient site-directed mutagenesis method based on PCR
    • Chen B, Przybyla AE (1994) An efficient site-directed mutagenesis method based on PCR. Biotechniques 17: 657-659
    • (1994) Biotechniques , vol.17 , pp. 657-659
    • Chen, B.1    Przybyla, A.E.2
  • 7
    • 0002984178 scopus 로고
    • La nutrition minérale et en eau des plantes en horticulture avancée
    • Coïc Y, Lesaint C (1975) La nutrition minérale et en eau des plantes en horticulture avancée. Doc Tech Commerc Potasses Alsace 23: 1-22
    • (1975) Doc Tech Commerc Potasses Alsace , vol.23 , pp. 1-22
    • Coïc, Y.1    Lesaint, C.2
  • 8
    • 0029328453 scopus 로고
    • Nitrate: Nutrient and signal for plant growth
    • Crawford NM (1995) Nitrate: nutrient and signal for plant growth. Plant Cell 7: 859-868
    • (1995) Plant Cell , vol.7 , pp. 859-868
    • Crawford, N.M.1
  • 9
    • 0031127822 scopus 로고    scopus 로고
    • Nitrite reductase expression is regulated at the post-transcriptional level by the nitrogen source in Nicotiana plumbaginifolia and Arabidopsis thaliana
    • Crété P, Caboche M, Meyer C (1997) Nitrite reductase expression is regulated at the post-transcriptional level by the nitrogen source in Nicotiana plumbaginifolia and Arabidopsis thaliana. Plant J 11: 625-634
    • (1997) Plant J , vol.11 , pp. 625-634
    • Crété, P.1    Caboche, M.2    Meyer, C.3
  • 10
    • 0024839973 scopus 로고
    • Tissue distribution of the AMP-activated protein kinase and lack of activation by cyclic-AMP-dependent protein kinase, studied using a specific and sensitive peptide assay
    • Davies SP, Carling D, Hardie DG (1989) Tissue distribution of the AMP-activated protein kinase and lack of activation by cyclic-AMP-dependent protein kinase, studied using a specific and sensitive peptide assay. Eur J Biochem 186: 123-128
    • (1989) Eur J Biochem , vol.186 , pp. 123-128
    • Davies, S.P.1    Carling, D.2    Hardie, D.G.3
  • 11
    • 0000684333 scopus 로고
    • 2 fixation in the control of nitrate-reductase activity in barley leaves
    • 2 fixation in the control of nitrate-reductase activity in barley leaves. Planta 190: 277-283
    • (1993) Planta , vol.190 , pp. 277-283
    • Decires, A.1    Delatorre, A.2    Delgado, B.3    Lara, C.4
  • 12
    • 0029583746 scopus 로고
    • Identification of a regulatory phosphorylation site in the hinge 1 region of nitrate reductase from spinach (Spinacea oleracea) leaves
    • Douglas P, Morrice N, MacKintosh C (1995) Identification of a regulatory phosphorylation site in the hinge 1 region of nitrate reductase from spinach (Spinacea oleracea) leaves. FEBS Lett 377: 113-117
    • (1995) FEBS Lett , vol.377 , pp. 113-117
    • Douglas, P.1    Morrice, N.2    MacKintosh, C.3
  • 14
    • 0001290697 scopus 로고
    • Isolation and characterization of Nicotiana plumbaginifolia nitrate reductase-deficient mutants: Genetic and biochemical analysis of the NIA complementation group
    • Gabard J, Marion-Poll A, Chérel I, Meyer C, Müller AJ, Caboche M (1987) Isolation and characterization of Nicotiana plumbaginifolia nitrate reductase-deficient mutants: genetic and biochemical analysis of the NIA complementation group. Mol Gen Genet 209: 596-606
    • (1987) Mol Gen Genet , vol.209 , pp. 596-606
    • Gabard, J.1    Marion-Poll, A.2    Chérel, I.3    Meyer, C.4    Müller, A.J.5    Caboche, M.6
  • 15
    • 0000924662 scopus 로고
    • Rapid modulation of nitrate reductase in pea roots
    • Glaab J, Kaiser WM (1993) Rapid modulation of nitrate reductase in pea roots. Planta 191: 173-179
    • (1993) Planta , vol.191 , pp. 173-179
    • Glaab, J.1    Kaiser, W.M.2
  • 16
    • 0029105061 scopus 로고
    • Inactivation of nitrate reductase involves NR-protein phosphorylation and subsequent 'binding' of an inhibitor protein
    • Glaab J, Kaiser WM (1995) Inactivation of nitrate reductase involves NR-protein phosphorylation and subsequent 'binding' of an inhibitor protein. Planta 195: 514-518
    • (1995) Planta , vol.195 , pp. 514-518
    • Glaab, J.1    Kaiser, W.M.2
  • 17
    • 85032070731 scopus 로고
    • The use of mutants and transgenic plants to study nitrate assimilation
    • Hoff T, Truong H-N, Caboche M (1994) The use of mutants and transgenic plants to study nitrate assimilation. Plant Cell Environ 17: 489-506
    • (1994) Plant Cell Environ , vol.17 , pp. 489-506
    • Hoff, T.1    Truong, H.-N.2    Caboche, M.3
  • 18
    • 0026633177 scopus 로고
    • Reversible light/dark modulation of spinach leaf nitrate reductase activity involves protein phosphorylation
    • Huber JL, Huber SC, Campbell WH, Redinbaugh MG (1992) Reversible light/dark modulation of spinach leaf nitrate reductase activity involves protein phosphorylation. Arch Biochem Biophys 296: 58-65
    • (1992) Arch Biochem Biophys , vol.296 , pp. 58-65
    • Huber, J.L.1    Huber, S.C.2    Campbell, W.H.3    Redinbaugh, M.G.4
  • 19
    • 0028323675 scopus 로고
    • Regulation of maize leaf nitrate reductase activity involves both gene expression and protein phosphorylation
    • Huber JL, Redinbaugh MG, Huber SC, Campbell WH (1994) Regulation of maize leaf nitrate reductase activity involves both gene expression and protein phosphorylation. Plant Physiol 106: 1667-1674
    • (1994) Plant Physiol , vol.106 , pp. 1667-1674
    • Huber, J.L.1    Redinbaugh, M.G.2    Huber, S.C.3    Campbell, W.H.4
  • 20
    • 0000137376 scopus 로고
    • Rapid modulation of spinach leaf nitrate reductase activity by photosynthesis. II. In vitro modulation by ATP and AMP
    • Kaiser WM, Brendle-Behnisch E (1991) Rapid modulation of spinach leaf nitrate reductase activity by photosynthesis. II. In vitro modulation by ATP and AMP. Plant Physiol 96: 368-375
    • (1991) Plant Physiol , vol.96 , pp. 368-375
    • Kaiser, W.M.1    Brendle-Behnisch, E.2
  • 22
    • 0028317624 scopus 로고
    • Posttranslational regulation of nitrate reductase in higher plants
    • Kaiser WM, Huber SC (1994a) Posttranslational regulation of nitrate reductase in higher plants. Plant Physiol 106: 817-821
    • (1994) Plant Physiol , vol.106 , pp. 817-821
    • Kaiser, W.M.1    Huber, S.C.2
  • 24
    • 0030879978 scopus 로고    scopus 로고
    • Correlation between apparent activation state of nitrate reductase (NR), NR hysteresis and degradation of NR protein
    • Kaiser WM, Huber SC (1997) Correlation between apparent activation state of nitrate reductase (NR), NR hysteresis and degradation of NR protein. J Exp Bot 48: 1367-1374
    • (1997) J Exp Bot , vol.48 , pp. 1367-1374
    • Kaiser, W.M.1    Huber, S.C.2
  • 25
    • 34249833664 scopus 로고
    • Adenine nucleotides are apparently involved in the light-dark modulation of spinach-leaf nitrate reductase
    • Kaiser WM, Spill D, Brendle-Behnisch E (1992) Adenine nucleotides are apparently involved in the light-dark modulation of spinach-leaf nitrate reductase. Planta 186: 236-240
    • (1992) Planta , vol.186 , pp. 236-240
    • Kaiser, W.M.1    Spill, D.2    Brendle-Behnisch, E.3
  • 26
    • 84989675194 scopus 로고
    • Rapid modulation of nitrate reductase in leaves and roots: Indirect evidence for the involvement of protein phosphorylation/dephosphorylation
    • Kaiser WM, Spill D, Glaab J (1993) Rapid modulation of nitrate reductase in leaves and roots: indirect evidence for the involvement of protein phosphorylation/dephosphorylation. Physiol Plant 89: 557-562
    • (1993) Physiol Plant , vol.89 , pp. 557-562
    • Kaiser, W.M.1    Spill, D.2    Glaab, J.3
  • 27
    • 0029141487 scopus 로고
    • Phosphorylation/dephosphorylation of Komatsuna (Brassica campestris) leaf nitrate reductase in vivo and in vitro in response to environmental light conditions: Effects of protein kinase and protein phosphatase inhibitors
    • Kojima M, Wu S-J, Fukui H, Sugimoto T, Nanmori T, Oji Y (1995) Phosphorylation/dephosphorylation of Komatsuna (Brassica campestris) leaf nitrate reductase in vivo and in vitro in response to environmental light conditions: effects of protein kinase and protein phosphatase inhibitors. Physiol Plant 93: 139-145
    • (1995) Physiol Plant , vol.93 , pp. 139-145
    • Kojima, M.1    Wu, S.-J.2    Fukui, H.3    Sugimoto, T.4    Nanmori, T.5    Oji, Y.6
  • 28
    • 0028225390 scopus 로고
    • A glycine to aspartic acid change in the MoCo domain of nitrate reductase reduces both activity and phosphorylation levels in Arabidopsis
    • LaBrie S, Crawford NM (1994) A glycine to aspartic acid change in the MoCo domain of nitrate reductase reduces both activity and phosphorylation levels in Arabidopsis. J Biol Chem 269: 14497-14501
    • (1994) J Biol Chem , vol.269 , pp. 14497-14501
    • LaBrie, S.1    Crawford, N.M.2
  • 29
    • 0028321312 scopus 로고
    • Induction and turnover of nitrate reductase in Zea mays. Influence of light
    • Li XZ, Oaks A (1994) Induction and turnover of nitrate reductase in Zea mays. Influence of light. Plant Physiol 106: 1145-1149
    • (1994) Plant Physiol , vol.106 , pp. 1145-1149
    • Li, X.Z.1    Oaks, A.2
  • 30
    • 0027143553 scopus 로고
    • Magnesium and calcium inhibition of squash leaf NADH nitrate reductase
    • Lillo C (1993) Magnesium and calcium inhibition of squash leaf NADH nitrate reductase. Plant Cell Physiol 34: 1181-1185
    • (1993) Plant Cell Physiol , vol.34 , pp. 1181-1185
    • Lillo, C.1
  • 31
    • 0031397707 scopus 로고    scopus 로고
    • Characterization of nitrate reductase from light- and dark-exposed leaves
    • Lillo C, Kazazaic S, Ruoff P, Meyer C (1997) Characterization of nitrate reductase from light- and dark-exposed leaves. Plant Physiol 114: 1377-1383
    • (1997) Plant Physiol , vol.114 , pp. 1377-1383
    • Lillo, C.1    Kazazaic, S.2    Ruoff, P.3    Meyer, C.4
  • 32
    • 0029670085 scopus 로고    scopus 로고
    • Phosphorylation of IκBα in the C-terminal PEST domain by casein kinase II affects protein stability
    • Lin R, Beauparlant P, Makris C, Meloche S, Hiscott J (1996) Phosphorylation of IκBα in the C-terminal PEST domain by casein kinase II affects protein stability. Mol Cell Biol 16: 1401-1409
    • (1996) Mol Cell Biol , vol.16 , pp. 1401-1409
    • Lin, R.1    Beauparlant, P.2    Makris, C.3    Meloche, S.4    Hiscott, J.5
  • 33
    • 0026768507 scopus 로고
    • Regulation of spinach-leaf nitrate reductase by reversible phosphorylation
    • MacKintosh C (1992) Regulation of spinach-leaf nitrate reductase by reversible phosphorylation. Biochim Biophys Acta 1137: 121-126
    • (1992) Biochim Biophys Acta , vol.1137 , pp. 121-126
    • MacKintosh, C.1
  • 34
    • 0029110548 scopus 로고
    • Identification of a protein that inhibits the phosphorylated form of nitrate reductase from spinach (Spinacia oleracea) leaves
    • MacKintosh C, Douglas P, Lillo C (1995) Identification of a protein that inhibits the phosphorylated form of nitrate reductase from spinach (Spinacia oleracea) leaves. Plant Physiol 107: 451-457
    • (1995) Plant Physiol , vol.107 , pp. 451-457
    • MacKintosh, C.1    Douglas, P.2    Lillo, C.3
  • 36
    • 0029133157 scopus 로고
    • Identification by mutational analysis of four critical residues in the molybdenum cofactor domain of eukaryotic nitrate reductase
    • Meyer C, Gonneau M, Caboche M, Rouzé P (1995) Identification by mutational analysis of four critical residues in the molybdenum cofactor domain of eukaryotic nitrate reductase. FEBS Lett 370: 197-202
    • (1995) FEBS Lett , vol.370 , pp. 197-202
    • Meyer, C.1    Gonneau, M.2    Caboche, M.3    Rouzé, P.4
  • 37
    • 0030250857 scopus 로고    scopus 로고
    • Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin
    • Moorhead G, Douglas P, Morrice N, Scarabel M, Aitken A, MacKintosh C (1996) Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin. Curr Biol 6: 1104-1113
    • (1996) Curr Biol , vol.6 , pp. 1104-1113
    • Moorhead, G.1    Douglas, P.2    Morrice, N.3    Scarabel, M.4    Aitken, A.5    MacKintosh, C.6
  • 38
    • 0029294012 scopus 로고
    • Post-transcriptional regulation of nitrate reductase by light is abolished by an N-terminal deletion
    • Nussaume L, Vincentz M, Meyer C, Boutin JP, Caboche M (1995) Post-transcriptional regulation of nitrate reductase by light is abolished by an N-terminal deletion. Plant Cell 7: 611-621
    • (1995) Plant Cell , vol.7 , pp. 611-621
    • Nussaume, L.1    Vincentz, M.2    Meyer, C.3    Boutin, J.P.4    Caboche, M.5
  • 39
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
    • Pearson RB, Kemp BE (1991) Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations. Methods Enzymol 200: 62-81
    • (1991) Methods Enzymol , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 40
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner M, Rogers SW (1996) PEST sequences and regulation by proteolysis. Trends Biochem Sci 21: 267-271
    • (1996) Trends Biochem Sci , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 41
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B, Sander C (1994) Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19: 55-72
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 42
    • 0029665597 scopus 로고    scopus 로고
    • Constitutive phosphorylation of IκBα by casein kinase II occurs preferentially at serine 293: Requirement for degradation of free IκBα
    • Schwarz EM, van Antwerp D, Verma IM (1996) Constitutive phosphorylation of IκBα by casein kinase II occurs preferentially at serine 293: requirement for degradation of free IκBα. Mol Cell Biol 16: 3554-3559
    • (1996) Mol Cell Biol , vol.16 , pp. 3554-3559
    • Schwarz, E.M.1    Van Antwerp, D.2    Verma, I.M.3
  • 43
    • 0027947784 scopus 로고
    • Partial purification of two proteins (100 kDa, 67 kDa) cooperating in the ATP-dependent inactivation of spinach leaf nitrate reductase
    • Spill D, Kaiser WM (1994) Partial purification of two proteins (100 kDa, 67 kDa) cooperating in the ATP-dependent inactivation of spinach leaf nitrate reductase. Planta 192: 183-188
    • (1994) Planta , vol.192 , pp. 183-188
    • Spill, D.1    Kaiser, W.M.2
  • 44
    • 0030095876 scopus 로고    scopus 로고
    • Identification in vitro of a post-translarional regulatory site in the hinge 1 region of Arabidopsis nitrate reductase
    • Su W, Huber SC, Crawford NM (1996) Identification in vitro of a post-translarional regulatory site in the hinge 1 region of Arabidopsis nitrate reductase. Plant Cell 8: 519-527
    • (1996) Plant Cell , vol.8 , pp. 519-527
    • Su, W.1    Huber, S.C.2    Crawford, N.M.3
  • 45
    • 0025020103 scopus 로고
    • Functional complementation of tobacco and Nicotiana plumbaginifolia nitrate reductase deficient mutants by transformation with the wild-type allele of the tobacco structural gene
    • Vaucheret H, Chabaud M, Kronenberger J, Caboche M (1990) Functional complementation of tobacco and Nicotiana plumbaginifolia nitrate reductase deficient mutants by transformation with the wild-type allele of the tobacco structural gene. Mol Gen Genet 220: 468-474
    • (1990) Mol Gen Genet , vol.220 , pp. 468-474
    • Vaucheret, H.1    Chabaud, M.2    Kronenberger, J.3    Caboche, M.4
  • 46
    • 0024636408 scopus 로고
    • Molecular cloning and characterization of the homologous genes coding for nitrate reductase in tobacco
    • Vaucheret H, Vincentz M, Kronenberger J, Caboche M, Rouzé P (1989) Molecular cloning and characterization of the homologous genes coding for nitrate reductase in tobacco. Mol Gen Genet 216: 10-15
    • (1989) Mol Gen Genet , vol.216 , pp. 10-15
    • Vaucheret, H.1    Vincentz, M.2    Kronenberger, J.3    Caboche, M.4    Rouzé, P.5
  • 47
    • 0025735599 scopus 로고
    • Constitutive expression of nitrate reductase allows normal growth and development of Nicotiana plumbaginifolia plants
    • Vincentz M, Caboche M (1991) Constitutive expression of nitrate reductase allows normal growth and development of Nicotiana plumbaginifolia plants. EMBO J 10: 1027-1035
    • (1991) EMBO J , vol.10 , pp. 1027-1035
    • Vincentz, M.1    Caboche, M.2
  • 48
    • 0027551494 scopus 로고
    • Regulation of nitrate and nitrite reductase expression of Nicotiana plumbaginifolia leaves by nitrogen and carbon metabolites
    • Vincentz M, Moureaux T, Leydecker M-T, Vaucheret H, Caboche M (1993) Regulation of nitrate and nitrite reductase expression of Nicotiana plumbaginifolia leaves by nitrogen and carbon metabolites. Plant J 3: 315-324
    • (1993) Plant J , vol.3 , pp. 315-324
    • Vincentz, M.1    Moureaux, T.2    Leydecker, M.-T.3    Vaucheret, H.4    Caboche, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.