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Volumn 89, Issue 3, 2006, Pages

Thioredoxin-dependent regulation of photosynthetic glyceraldehyde-3- phosphate dehydrogenase: Autonomous vs. CP12-dependent mechanisms

Author keywords

Calvin Benson cycle; Disulfide; Light dark regulation; Pyridine nucleotides; Supramolecular complex; Thioredoxin

Indexed keywords

ALGAE; CYANOBACTERIA; EMBRYOPHYTA; SPINACIA OLERACEA;

EID: 33749840484     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-006-9099-z     Document Type: Review
Times cited : (85)

References (70)
  • 1
    • 0006153497 scopus 로고
    • A new glyceraldehyde phosphate dehydrogenase from photosynthetic tissues
    • Arnon DI, Rosenberg LL, Whatley FR (1954) A new glyceraldehyde phosphate dehydrogenase from photosynthetic tissues. Nature 173:1132-1134
    • (1954) Nature , vol.173 , pp. 1132-1134
    • Arnon, D.I.1    Rosenberg, L.L.2    Whatley, F.R.3
  • 2
    • 0028010677 scopus 로고
    • Regulation of NADP-dependent glyceraldehyde 3-phosphate dehydrogenase activity in spinach chloroplasts
    • Baalmann E, Backhausen JE, Kitzmann C, Scheibe R (1994) Regulation of NADP-dependent glyceraldehyde 3-phosphate dehydrogenase activity in spinach chloroplasts. Bot Acta 107:313-320
    • (1994) Bot Acta , vol.107 , pp. 313-320
    • Baalmann, E.1    Backhausen, J.E.2    Kitzmann, C.3    Scheibe, R.4
  • 3
    • 0029583088 scopus 로고
    • Reductive modification and non-reductive activation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase
    • Baalmann E, Backhausen JE, Rak C, Vetter S, Scheibe R (1995) Reductive modification and non-reductive activation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase. Arch Biochem Biophys 324:201-208
    • (1995) Arch Biochem Biophys , vol.324 , pp. 201-208
    • Baalmann, E.1    Backhausen, J.E.2    Rak, C.3    Vetter, S.4    Scheibe, R.5
  • 5
    • 0024698882 scopus 로고
    • Cloning and sequence analysis of cDNAs encoding the cytosolic precursors of subunits GapA and GapB of chloroplast glyceraldehyde-3-phosphate dehydrogenase from pea and spinach
    • Brinkmann H, Cerff R, Salomon M, Soll J (1989) Cloning and sequence analysis of cDNAs encoding the cytosolic precursors of subunits GapA and GapB of chloroplast glyceraldehyde-3-phosphate dehydrogenase from pea and spinach. Plant Mol Biol 13:81-94
    • (1989) Plant Mol Biol , vol.13 , pp. 81-94
    • Brinkmann, H.1    Cerff, R.2    Salomon, M.3    Soll, J.4
  • 6
    • 0000765807 scopus 로고
    • Role of light in the regulation of chloroplast enzymes
    • Buchanan B (1980) Role of light in the regulation of chloroplast enzymes. Annu Rev Plant Physiol 31:341-374
    • (1980) Annu Rev Plant Physiol , vol.31 , pp. 341-374
    • Buchanan, B.1
  • 7
    • 0000570970 scopus 로고
    • Carbon dioxide assimilation in oxygenic and anoxygenic photosynthesis
    • Buchanan B (1992) Carbon dioxide assimilation in oxygenic and anoxygenic photosynthesis. Photosynth Res 33:147-162
    • (1992) Photosynth Res , vol.33 , pp. 147-162
    • Buchanan, B.1
  • 8
    • 20044367629 scopus 로고    scopus 로고
    • Redox regulation: A broadening horizon
    • Buchanan BB, Balmer Y (2005) Redox regulation: a broadening horizon. Annu Rev Plant Biol 56:187-220
    • (2005) Annu Rev Plant Biol , vol.56 , pp. 187-220
    • Buchanan, B.B.1    Balmer, Y.2
  • 9
    • 0033561407 scopus 로고    scopus 로고
    • Chloroplast NADP-malate dehydrogenase: Structural basis of light-dependent regulation of activity by thiol oxidation and reduction
    • Carr P, Verger D, Ashton AR, Ollis D (1999) Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction. Structure 7:461-475
    • (1999) Structure , vol.7 , pp. 461-475
    • Carr, P.1    Verger, D.2    Ashton, A.R.3    Ollis, D.4
  • 10
    • 0030893657 scopus 로고    scopus 로고
    • NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding
    • Carugo O, Argos P (1997) NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding. Proteins: Struct.Funct Genet 28:10-28
    • (1997) Proteins: Struct Funct Genet , vol.28 , pp. 10-28
    • Carugo, O.1    Argos, P.2
  • 11
    • 0013287649 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase (NADP) from Sinapis alba: Steady state kinetics
    • Cerff R (1978) Glyceraldehyde-3-phosphate dehydrogenase (NADP) from Sinapis alba: steady state kinetics. Phytochemistry 17:2061-2067
    • (1978) Phytochemistry , vol.17 , pp. 2061-2067
    • Cerff, R.1
  • 12
    • 0018786983 scopus 로고
    • Subunit structure of higher plant glyceraldehyde-3-phosphate dehydrogenases
    • 2Cerff R, Chambers S (1979) Subunit structure of higher plant glyceraldehyde-3-phosphate dehydrogenases. J Biol Chem 254:6094-6098
    • (1979) J Biol Chem , vol.254 , pp. 6094-6098
    • Cerff, R.1    Chambers, S.2
  • 13
    • 0020357309 scopus 로고
    • Structural diversity and differential light control of mRNAs coding for angiosperm glyceraldehyde-3-phosphate dehydrogenases
    • Cerff R, Kloppstech K (1982) Structural diversity and differential light control of mRNAs coding for angiosperm glyceraldehyde-3-phosphate dehydrogenases. Proc Natl Acad Sci USA 79:7624-7628
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 7624-7628
    • Cerff, R.1    Kloppstech, K.2
  • 14
    • 27144540627 scopus 로고    scopus 로고
    • NADK2, an Arabidopsis chloroplastic NAD kinase, plays a vital role in both chlorophyll synthesis and chloroplast protection
    • Chai MF, Chen QJ, An R, Chen YM, Chen J, Wang XC (2005) NADK2, an Arabidopsis chloroplastic NAD kinase, plays a vital role in both chlorophyll synthesis and chloroplast protection. Plant Mol Biol 59:553-564
    • (2005) Plant Mol Biol , vol.59 , pp. 553-564
    • Chai, M.F.1    Chen, Q.J.2    An, R.3    Chen, Y.M.4    Chen, J.5    Wang, X.C.6
  • 16
    • 0027770363 scopus 로고
    • Effects of blue and red light on expression of nuclear genes encoding chloroplast glyceraldehyde-3-phosphate dehydrogenase of Arabidopsis thaliana
    • Dewdney J, Conley TR, Shih M-C, Goodman H (1993) Effects of blue and red light on expression of nuclear genes encoding chloroplast glyceraldehyde-3- phosphate dehydrogenase of Arabidopsis thaliana. Plant Physiol 103:1115-1121
    • (1993) Plant Physiol , vol.103 , pp. 1115-1121
    • Dewdney, J.1    Conley, T.R.2    Shih, M.-C.3    Goodman, H.4
  • 17
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6:197-208
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 20
    • 0025080896 scopus 로고
    • Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): Amino acid sequence of the subunits from isoenzyme I and structural relationship with isoenzyme II
    • Ferri G, Stoppini M, Meloni ML, Zapponi MC, Iadarola P (1990) Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): amino acid sequence of the subunits from isoenzyme I and structural relationship with isoenzyme II. Biochim Biophys Acta 1041:36-42
    • (1990) Biochim Biophys Acta , vol.1041 , pp. 36-42
    • Ferri, G.1    Stoppini, M.2    Meloni, M.L.3    Zapponi, M.C.4    Iadarola, P.5
  • 21
    • 0032949947 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase gene diversity in eubacteria and eukaryotes: Evidence for intra- and inter-kingdom gene transfer
    • Figge RM, Schubert M, Brinkmann H, Cerff R (1999) Glyceraldehyde-3- phosphate dehydrogenase gene diversity in eubacteria and eukaryotes: evidence for intra- and inter-kingdom gene transfer. Mol Biol Evol 16:429-440
    • (1999) Mol Biol Evol , vol.16 , pp. 429-440
    • Figge, R.M.1    Schubert, M.2    Brinkmann, H.3    Cerff, R.4
  • 23
    • 0001237873 scopus 로고
    • Subcellular metabolite levels in spinach leaves
    • Gerhardt R, Stitt M, Heldt HW (1987) Subcellular metabolite levels in spinach leaves. Plant Physiol 83:399-407
    • (1987) Plant Physiol , vol.83 , pp. 399-407
    • Gerhardt, R.1    Stitt, M.2    Heldt, H.W.3
  • 24
    • 0037220140 scopus 로고    scopus 로고
    • 4 glyceraldehyde 3-phosphate dehydrogenase. Kinetic evidence for confromation changes upon association with the small protein CP12
    • 4 glyceraldehyde 3-phosphate dehydrogenase. Kinetic evidence for confromation changes upon association with the small protein CP12. Eur J Biochem 270:129-136
    • (2003) Eur J Biochem , vol.270 , pp. 129-136
    • Graciet, E.1    Lebreton, S.2    Camadro, J.M.3    Gontero, B.4
  • 26
    • 2942692516 scopus 로고    scopus 로고
    • Emergence of new regulatory mechanisms in the Benson-Calvin pathway via protein-protein interactions: A glyceraldehyde-3-phosphate dehydrogenase/CP12/ phosphoribulokinase complex
    • Graciet E, Lebreton S, Gontero B (2004a) Emergence of new regulatory mechanisms in the Benson-Calvin pathway via protein-protein interactions: a glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase complex. J Exp Bot 55:1245-1254
    • (2004) J Exp Bot , vol.55 , pp. 1245-1254
    • Graciet, E.1    Lebreton, S.2    Gontero, B.3
  • 29
    • 0040799938 scopus 로고    scopus 로고
    • Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin:thioredoxin reductase, and thioredoxin f regulated enzymes
    • Hirasawa M, Schürmann P, Jacquot J-P, Manieri W, Jacquot P, Keryer E, Hartman F, Knaff D (1999) Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin:thioredoxin reductase, and thioredoxin f regulated enzymes. Biochemistry 38:5200-5205
    • (1999) Biochemistry , vol.38 , pp. 5200-5205
    • Hirasawa, M.1    Schürmann, P.2    Jacquot, J.-P.3    Manieri, W.4    Jacquot, P.5    Keryer, E.6    Hartman, F.7    Knaff, D.8
  • 30
    • 0034612325 scopus 로고    scopus 로고
    • Differential effects of chilling-induced photooxidation on the redox regulation of photosynthetic enzymes
    • Hutchison RS, Groom Q, Ort DR (2000) Differential effects of chilling-induced photooxidation on the redox regulation of photosynthetic enzymes. Biochemistry 6:6679-6688
    • (2000) Biochemistry , vol.6 , pp. 6679-6688
    • Hutchison, R.S.1    Groom, Q.2    Ort, D.R.3
  • 32
    • 0031909505 scopus 로고    scopus 로고
    • Genetic and biochemical evidence for distinct key functions of two highly divergent GAPDH genes in catabolic and anabolic carbon flow of the cyanobacterium Synechocystis sp. PCC 6803
    • Koksharova O, Schubert M, Shestakov S, Cerff R (1998) Genetic and biochemical evidence for distinct key functions of two highly divergent GAPDH genes in catabolic and anabolic carbon flow of the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol Biol 36:183-194
    • (1998) Plant Mol Biol , vol.36 , pp. 183-194
    • Koksharova, O.1    Schubert, M.2    Shestakov, S.3    Cerff, R.4
  • 34
    • 0038362749 scopus 로고    scopus 로고
    • Modulation via protein-protein interactions of glyceraldehyde-3-phosphate dehydrogenase activity through redox phosphoribulokinase regulation
    • Lebreton S, Graciet E, Gontero B (2003) Modulation via protein-protein interactions of glyceraldehyde-3-phosphate dehydrogenase activity through redox phosphoribulokinase regulation. J Biol Chem 278:12078-12084
    • (2003) J Biol Chem , vol.278 , pp. 12078-12084
    • Lebreton, S.1    Graciet, E.2    Gontero, B.3
  • 35
    • 0031277449 scopus 로고    scopus 로고
    • Expression and characterization of pea chloroplastic glyceraldehyde-3- phosphate dehydrogenase composed of only the B-subunit
    • Li AD, Anderson LE (1997) Expression and characterization of pea chloroplastic glyceraldehyde-3-phosphate dehydrogenase composed of only the B-subunit. Plant Physiol 115:1201-1209
    • (1997) Plant Physiol , vol.115 , pp. 1201-1209
    • Li, A.D.1    Anderson, L.E.2
  • 36
    • 11444265790 scopus 로고    scopus 로고
    • Coordinated gene expression of photosynthetic glyceraldehyde-3-phosphate dehydrogenase, phosphoribulokinase and CP12 in Arabidopsis thaliana
    • Marri L, Sparla F, Pupillo P, Trost P (2005a) Coordinated gene expression of photosynthetic glyceraldehyde-3-phosphate dehydrogenase, phosphoribulokinase and CP12 in Arabidopsis thaliana. J Exp Bot 56:73-80
    • (2005) J Exp Bot , vol.56 , pp. 73-80
    • Marri, L.1    Sparla, F.2    Pupillo, P.3    Trost, P.4
  • 37
    • 33644840144 scopus 로고    scopus 로고
    • Reconstitution and properties of the recombinant GAPDH/CP12/PRK supramolecular complex of Arabidopsis thaliana
    • Marri L, Trost P, Pupillo P, Sparla F (2005b) Reconstitution and properties of the recombinant GAPDH/CP12/PRK supramolecular complex of Arabidopsis thaliana. Plant Physiol 139:1433-1443
    • (2005) Plant Physiol , vol.139 , pp. 1433-1443
    • Marri, L.1    Trost, P.2    Pupillo, P.3    Sparla, F.4
  • 38
    • 0030850422 scopus 로고    scopus 로고
    • The evolution of the Calvin cycle from prokaryotic to eukaryotic chromosomes: A case study of functional redundancy in ancient pathways through endosymbiosis
    • Martin W, Schnarrenberger C (1997) The evolution of the Calvin cycle from prokaryotic to eukaryotic chromosomes: a case study of functional redundancy in ancient pathways through endosymbiosis. Curr Genet 32:1-18
    • (1997) Curr Genet , vol.32 , pp. 1-18
    • Martin, W.1    Schnarrenberger, C.2
  • 39
    • 0036320250 scopus 로고    scopus 로고
    • Intrasteric inhibition in redox signalling: Light activation of NADP-malate dehydrogenase
    • Miginiac-Maslow M, Lancelin JM (2002) Intrasteric inhibition in redox signalling: light activation of NADP-malate dehydrogenase. Photosynth Res 72:1-12
    • (2002) Photosynth Res , vol.72 , pp. 1-12
    • Miginiac-Maslow, M.1    Lancelin, J.M.2
  • 40
    • 0005764576 scopus 로고
    • Light induced conversion of nicotinamide adenine dinucleotide to nicotinamide adenine phosphate in higher plants
    • Muto S, Miyachi S, Usuda H, Edwards GE, Bassham JA (1981) Light induced conversion of nicotinamide adenine dinucleotide to nicotinamide adenine phosphate in higher plants. Plant Physiol 68:324-328
    • (1981) Plant Physiol , vol.68 , pp. 324-328
    • Muto, S.1    Miyachi, S.2    Usuda, H.3    Edwards, G.E.4    Bassham, J.A.5
  • 41
    • 0023653799 scopus 로고
    • Properties of a multimeric protein complex from chloroplasts possessing potential activities of NADPH-dependent glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase
    • Nicholson S, Easterby JS, Powls (1987) Properties of a multimeric protein complex from chloroplasts possessing potential activities of NADPH-dependent glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase. Eur J Biochem 162:423-431
    • (1987) Eur J Biochem , vol.162 , pp. 423-431
    • Nicholson, S.1    Easterby, J.S.2    Powls3
  • 43
    • 0042672742 scopus 로고    scopus 로고
    • Origin, evolution and metabolic role of a novel glycolytic GAPDH enzyme recruited by land plant plastids
    • Petersen J, Brinkmann H, Cerff R (2003) Origin, evolution and metabolic role of a novel glycolytic GAPDH enzyme recruited by land plant plastids. J Mol Evol 57:16-26
    • (2003) J Mol Evol , vol.57 , pp. 16-26
    • Petersen, J.1    Brinkmann, H.2    Cerff, R.3
  • 44
    • 33646867843 scopus 로고    scopus 로고
    • The GapA/B gene duplication marks the origin of Streptophyta (charophytes and land plants)
    • published on line ahead of print
    • Petersen J, Teich R, Becker B, Cerff R, Brinkmann H (2006) The GapA/B gene duplication marks the origin of Streptophyta (charophytes and land plants). Mol Biol Evol published on line ahead of print
    • (2006) Mol Biol Evol
    • Petersen, J.1    Teich, R.2    Becker, B.3    Cerff, R.4    Brinkmann, H.5
  • 45
    • 0030445521 scopus 로고    scopus 로고
    • CP12: A small nuclear-encoded chloroplast protein provides novel insights into higher-plant GAPDH evolution
    • Pohlmeyer K, Paap BK, Soll J, Wedel N (1996) CP12: a small nuclear-encoded chloroplast protein provides novel insights into higher-plant GAPDH evolution. Plant Mol Biol 32:969-978
    • (1996) Plant Mol Biol , vol.32 , pp. 969-978
    • Pohlmeyer, K.1    Paap, B.K.2    Soll, J.3    Wedel, N.4
  • 46
    • 0015536162 scopus 로고
    • The effect of NADP on the subunit structure and activity of spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase
    • Pupillo P, Giuliani Piccari G (1973) The effect of NADP on the subunit structure and activity of spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase. Arch Biochem Biophys 154:324-331
    • (1973) Arch Biochem Biophys , vol.154 , pp. 324-331
    • Pupillo, P.1    Giuliani Piccari, G.2
  • 47
    • 0016629875 scopus 로고
    • The reversible depolymerization of spinach chloroplast glyceraldehyde-phosphate dehydrogenase. Interaction with nucleotides and dithiothreitol
    • Pupillo P, Giuliani Piccari G (1975) The reversible depolymerization of spinach chloroplast glyceraldehyde-phosphate dehydrogenase. Interaction with nucleotides and dithiothreitol. Eur J Biochem 51:475-482
    • (1975) Eur J Biochem , vol.51 , pp. 475-482
    • Pupillo, P.1    Giuliani Piccari, G.2
  • 48
    • 0033081820 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray study of chloroplast glyceraldehyde-3-phosphate dehydrogenase
    • Sabatino P, Fermani S, Ripamonti A, Cassetta A, Scagliarini S, Trost P (1999). Crystallization and preliminary X-ray study of chloroplast glyceraldehyde-3-phosphate dehydrogenase. Acta Crystallog D55:566-567
    • (1999) Acta Crystallog , vol.D55 , pp. 566-567
    • Sabatino, P.1    Fermani, S.2    Ripamonti, A.3    Cassetta, A.4    Scagliarini, S.5    Trost, P.6
  • 49
    • 0031828075 scopus 로고    scopus 로고
    • The non-regulatory isoform of NAD(P)-glyceraldehyde-3-phosphate dehydrogenase from spinach chloroplasts
    • Scagliarini S, Trost P, Pupillo P (1998) The non-regulatory isoform of NAD(P)-glyceraldehyde-3-phosphate dehydrogenase from spinach chloroplasts. J Exp Bot 49:1307-1315
    • (1998) J Exp Bot , vol.49 , pp. 1307-1315
    • Scagliarini, S.1    Trost, P.2    Pupillo, P.3
  • 50
    • 0000788621 scopus 로고
    • Light activation and molecular-mass changes of NAD(P)-glyceraldehyde 3-phosphate dehydrogenase of spinach and maize leaves
    • Scagliarini S, Trost P, Pupillo P, Valenti V (1993) Light activation and molecular-mass changes of NAD(P)-glyceraldehyde 3-phosphate dehydrogenase of spinach and maize leaves. Planta 190:313-319
    • (1993) Planta , vol.190 , pp. 313-319
    • Scagliarini, S.1    Trost, P.2    Pupillo, P.3    Valenti, V.4
  • 51
    • 0030570983 scopus 로고    scopus 로고
    • C-terminal truncation of spinach chloroplast NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase prevents inactivation and reaggregation
    • Scheibe R, Baalmann E, Backhausen JE, Rak C, Vetter S (1996) C-terminal truncation of spinach chloroplast NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase prevents inactivation and reaggregation. Biochim Biophys Acta 1296:228-234
    • (1996) Biochim Biophys Acta , vol.1296 , pp. 228-234
    • Scheibe, R.1    Baalmann, E.2    Backhausen, J.E.3    Rak, C.4    Vetter, S.5
  • 52
    • 0036441528 scopus 로고    scopus 로고
    • Co-existence of two regulatory NADP-glyceraldehyde 3-P dehydrogenase complexes in higher plant chloroplasts
    • Scheibe R, Wedel N, Vetter S, Emmerlich V, Sauermann SM (2002) Co-existence of two regulatory NADP-glyceraldehyde 3-P dehydrogenase complexes in higher plant chloroplasts. Eur J Biochem 269:5617-5624
    • (2002) Eur J Biochem , vol.269 , pp. 5617-5624
    • Scheibe, R.1    Wedel, N.2    Vetter, S.3    Emmerlich, V.4    Sauermann, S.M.5
  • 54
    • 0023644310 scopus 로고
    • Structure of the holo-glyceraldehydde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å of resolution
    • Skarzynski T, Moody PCE, Wonacott AJ (1987) Structure of the holo-glyceraldehydde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å of resolution. J Mol Biol 193:171-187
    • (1987) J Mol Biol , vol.193 , pp. 171-187
    • Skarzynski, T.1    Moody, P.C.E.2    Wonacott, A.J.3
  • 55
    • 0032127997 scopus 로고    scopus 로고
    • Structure of the holo-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor refined at 2.0 Å resolution
    • Song S, Li J, Lin Z (1998) Structure of the holo-glyceraldehyde-3- phosphate dehydrogenase from Palinurus versicolor refined at 2.0 Å resolution. Acta Crystallog D 54:558-569
    • (1998) Acta Crystallog D , vol.54 , pp. 558-569
    • Song, S.1    Li, J.2    Lin, Z.3
  • 58
    • 0037160071 scopus 로고    scopus 로고
    • The C-terminal extension of glyceraldehyde-3-phosphate dehydrogenase subunit B acts as an autoinhibitory domain regulated by thioredoxins and nicotinamide adenine dinucleotide
    • Sparla F, Pupillo P, Trost P (2002) The C-terminal extension of glyceraldehyde-3-phosphate dehydrogenase subunit B acts as an autoinhibitory domain regulated by thioredoxins and nicotinamide adenine dinucleotide. J Biol Chem 277:44946-44952
    • (2002) J Biol Chem , vol.277 , pp. 44946-44952
    • Sparla, F.1    Pupillo, P.2    Trost, P.3
  • 59
    • 0000245049 scopus 로고
    • Adenine nucleotide levels in the cytosol, chloroplasts, and mitochondria of wheat leaf protoplasts
    • Stitt M, Lilley RM, Heldt HW (1982) Adenine nucleotide levels in the cytosol, chloroplasts, and mitochondria of wheat leaf protoplasts. Plant Physiol 1982:971-977
    • (1982) Plant Physiol , vol.1982 , pp. 971-977
    • Stitt, M.1    Lilley, R.M.2    Heldt, H.W.3
  • 60
    • 19444376568 scopus 로고    scopus 로고
    • The Calvin cycle in cyanobacteria is regulated by CP12 via NAD(H)/NADP(H) ratio under light/dark conditions
    • Tamoi M, Myazaki T, Fukamizo T, Shigeoka S (2005) The Calvin cycle in cyanobacteria is regulated by CP12 via NAD(H)/NADP(H) ratio under light/dark conditions. Plant J 42:504-513
    • (2005) Plant J , vol.42 , pp. 504-513
    • Tamoi, M.1    Myazaki, T.2    Fukamizo, T.3    Shigeoka, S.4
  • 61
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • Tompa P, Szasz C, Buday L (2005) Structural disorder throws new light on moonlighting. Trends Biochem Sci 30:484-489
    • (2005) Trends Biochem Sci , vol.30 , pp. 484-489
    • Tompa, P.1    Szasz, C.2    Buday, L.3
  • 62
    • 0000435332 scopus 로고
    • Activation of spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase: Effect of glycerate 1,3-bisphosphate
    • Trost P, Scagliarini S, Valenti V, Pupillo P (1993) Activation of spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase: effect of glycerate 1,3-bisphosphate. Planta 190:320-326
    • (1993) Planta , vol.190 , pp. 320-326
    • Trost, P.1    Scagliarini, S.2    Valenti, V.3    Pupillo, P.4
  • 63
    • 0002564767 scopus 로고
    • Activation of glyceraldehyde-phosphate dehydrogenase (NADP) and phosphoribulokinase in Phaseolus vulgaris leaf extracts involves the dissociation of oligomers
    • Wara-Aswapati O, Kemble RJ, Bradbeer JW (1980) Activation of glyceraldehyde-phosphate dehydrogenase (NADP) and phosphoribulokinase in Phaseolus vulgaris leaf extracts involves the dissociation of oligomers. Plant Physiol 66:34-39
    • (1980) Plant Physiol , vol.66 , pp. 34-39
    • Wara-Aswapati, O.1    Kemble, R.J.2    Bradbeer, J.W.3
  • 64
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337:635-645
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 65
    • 0032482983 scopus 로고    scopus 로고
    • Evolutionary conserved light regulation of Calvin cycle activity by NADPH-mediated reversible phosphoribulokinase-CP12-glyceraldehyde-3-phosphate dehydrogenase complex dissociation
    • Wedel N, Soll J (1998) Evolutionary conserved light regulation of Calvin cycle activity by NADPH-mediated reversible phosphoribulokinase-CP12- glyceraldehyde-3-phosphate dehydrogenase complex dissociation. Proc Natl Acad Sci USA 95:9699-9704
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9699-9704
    • Wedel, N.1    Soll, J.2
  • 66
    • 0030924125 scopus 로고    scopus 로고
    • CP12 provides a new mode of light regulation of Clavin cycle activity in higher plants
    • Wedel N, Soll J, Paap BK (1997) CP12 provides a new mode of light regulation of Clavin cycle activity in higher plants. Proc Natl Acad Sci USA 94:10479-10484
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10479-10484
    • Wedel, N.1    Soll, J.2    Paap, B.K.3
  • 68
    • 0017105323 scopus 로고
    • Studies on the regulation of chloroplast NADP-linked glyceraldehyde 3-phosphate dehydrogenase
    • Wolosiuk RA, Buchanan BB (1976) Studies on the regulation of chloroplast NADP-linked glyceraldehyde 3-phosphate dehydrogenase. J Biol Chem 251:6456-6461
    • (1976) J Biol Chem , vol.251 , pp. 6456-6461
    • Wolosiuk, R.A.1    Buchanan, B.B.2
  • 69
    • 0000168597 scopus 로고
    • Activation of chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by the ferredoxin/thioredoxin system
    • Wolosiuk RA, Buchanan BB (1978) Activation of chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by the ferredoxin/thioredoxin system. Plant Physiol 61:669-671
    • (1978) Plant Physiol , vol.61 , pp. 669-671
    • Wolosiuk, R.A.1    Buchanan, B.B.2
  • 70
    • 0000474564 scopus 로고
    • +-abhängige Glycerinaldehyd-3-phosphat-dehydrogenase
    • +-abhängige Glycerinaldehyd-3-phosphat-dehydrogenase. Planta 65:369-380
    • (1965) Planta , vol.65 , pp. 369-380
    • Ziegler, H.1    Ziegler, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.