메뉴 건너뛰기




Volumn 75, Issue 1, 2003, Pages 11-27

Rubisco activase - Rubisco's catalytic chaperone

Author keywords

Activase; Chaperone; Enzyme regulation; Photosynthesis; Protein protein interaction; Rubisco; Temperature stress

Indexed keywords

ARABIDOPSIS;

EID: 0037232721     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1022458108678     Document Type: Short Survey
Times cited : (481)

References (113)
  • 2
    • 0000191368 scopus 로고
    • Photosynthetic response and adaptation to temperature in higher plants
    • Berry JA and Bjorkman O (1980) Photosynthetic response and adaptation to temperature in higher plants. Annu Rev Plant Physiol 31: 491-543
    • (1980) Annu Rev Plant Physiol , vol.31 , pp. 491-543
    • Berry, J.A.1    Bjorkman, O.2
  • 4
    • 0000770694 scopus 로고
    • Rubisco activase modifies the appearance of Rubisco in the electron microscope
    • Murata N (ed) Research in Photosynthesis. Nagoya, Japan, August 30-September 4, 1992. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Büchen-Osmond C, Portis AR Jr and Andrews TJ (1992) Rubisco activase modifies the appearance of Rubisco in the electron microscope. In: Murata N (ed) Research in Photosynthesis, Vol III, pp 653-656. IXth International Congress On Photosynthesis, Nagoya, Japan, August 30-September 4, 1992. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • (1992) IXth International Congress On Photosynthesis , vol.3 , pp. 653-656
    • Büchen-Osmond, C.1    Portis A.R., Jr.2    Andrews, T.J.3
  • 6
    • 0034477160 scopus 로고    scopus 로고
    • Effect of heat stress on the inhibition and recovery of the ribulose-1,5-bisphosphate carboxylase/oxygenase activation state
    • Crafts-Brandner SJ and Law RD (2000) Effect of heat stress on the inhibition and recovery of the ribulose-1,5-bisphosphate carboxylase/oxygenase activation state. Planta 212: 67-74
    • (2000) Planta , vol.212 , pp. 67-74
    • Crafts-Brandner, S.J.1    Law, R.D.2
  • 8
    • 0031400786 scopus 로고    scopus 로고
    • The two forms of ribulose-1,5-bisphosphate carboxylase-oxygenase activase differ in sensitivity to elevated temperature
    • Crafts-Brandner SJ, van de Loo FJ and Salvucci ME (1997) The two forms of ribulose-1,5-bisphosphate carboxylase-oxygenase activase differ in sensitivity to elevated temperature. Plant Physiol 114: 439-344
    • (1997) Plant Physiol , vol.114 , pp. 439-344
    • Crafts-Brandner, S.J.1    Van De Loo, F.J.2    Salvucci, M.E.3
  • 9
    • 0034685616 scopus 로고    scopus 로고
    • The transition between the open and closed states of Rubisco is triggered by the inter-phosphate distance of the bound bisphosphate
    • Duff AP, Andrews TJ and Curmi PMG (2000) The transition between the open and closed states of Rubisco is triggered by the inter-phosphate distance of the bound bisphosphate. J Mol Biol 298: 903-916
    • (2000) J Mol Biol , vol.298 , pp. 903-916
    • Duff, A.P.1    Andrews, T.J.2    Curmi, P.M.G.3
  • 10
    • 0031040836 scopus 로고    scopus 로고
    • Heat denaturation profiles of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and Rubisco activase and the inability of Rubisco activase to restore activity of heat-denatured Rubisco
    • Eckardt NA and Portis AR Jr (1997) Heat denaturation profiles of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and Rubisco activase and the inability of Rubisco activase to restore activity of heat-denatured Rubisco. Plant Physiol 113: 243-248
    • (1997) Plant Physiol , vol.113 , pp. 243-248
    • Eckardt, N.A.1    Portis A.R., Jr.2
  • 11
    • 0031079693 scopus 로고    scopus 로고
    • Growth and photosynthesis under high and low irradiance of Arabidopsis thaliana antisense mutants with reduced ribulose-1,5-bisphosphate carboxylase/oxygenase activase content
    • Eckardt NA, Snyder GW, Portis AR Jr and Ogren WL (1997) Growth and photosynthesis under high and low irradiance of Arabidopsis thaliana antisense mutants with reduced ribulose-1,5-bisphosphate carboxylase/oxygenase activase content. Plant Physiol 113: 575-586
    • (1997) Plant Physiol , vol.113 , pp. 575-586
    • Eckardt, N.A.1    Snyder, G.W.2    Portis A.R., Jr.3    Ogren, W.L.4
  • 12
    • 0001041057 scopus 로고
    • Slow inactivation of ribulosebisphosphate carboxylase during catalysis is caused by accumulation of a slow, tight-binding inhibitor at the catalytic site
    • Edmondson DL, Badger MR and Andrews TJ (1990a) Slow inactivation of ribulosebisphosphate carboxylase during catalysis is caused by accumulation of a slow, tight-binding inhibitor at the catalytic site. Plant Physiol 93: 1390-1397
    • (1990) Plant Physiol , vol.93 , pp. 1390-1397
    • Edmondson, D.L.1    Badger, M.R.2    Andrews, T.J.3
  • 13
    • 0012535188 scopus 로고
    • Slow inactivation of ribulosebisphosphate carboxylase is not due to decarbamylation of the catalytic site
    • Edmondson DL, Badger MR and Andrews TJ (1990b) Slow inactivation of ribulosebisphosphate carboxylase is not due to decarbamylation of the catalytic site. Plant Physiol 93: 1383-1389
    • (1990) Plant Physiol , vol.93 , pp. 1383-1389
    • Edmondson, D.L.1    Badger, M.R.2    Andrews, T.J.3
  • 14
    • 0342561548 scopus 로고    scopus 로고
    • Differential effects of N- and C-terminal deletions on the two activities of Rubisco activase
    • Esau BD, Snyder GW and Portis AR Jr (1996) Differential effects of N- and C-terminal deletions on the two activities of Rubisco activase. Arch Biochem Biophys 326: 100-105
    • (1996) Arch Biochem Biophys , vol.326 , pp. 100-105
    • Esau, B.D.1    Snyder, G.W.2    Portis A.R., Jr.3
  • 15
    • 0032424758 scopus 로고    scopus 로고
    • Activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) with chimeric activase proteins
    • Esau BD, Snyder GW and Portis AR Jr (1998) Activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) with chimeric activase proteins. Photosynth Res 58: 175-181
    • (1998) Photosynth Res , vol.58 , pp. 175-181
    • Esau, B.D.1    Snyder, G.W.2    Portis A.R., Jr.3
  • 16
    • 0001569341 scopus 로고    scopus 로고
    • Moderately high temperatures inhibit ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase-mediated activation of Rubisco
    • Feller U, Crafts-Brandner SJ and Salvucci ME (1998) Moderately high temperatures inhibit ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase-mediated activation of Rubisco. Plant Physiol 116: 539-546
    • (1998) Plant Physiol , vol.116 , pp. 539-546
    • Feller, U.1    Crafts-Brandner, S.J.2    Salvucci, M.E.3
  • 17
    • 0027368491 scopus 로고
    • Rubisco but not Rubisco activase is clustered in the carboxysomes of the cyanobacterium Synechococcus sp. PCC 7942: Mud-induced carboxysomeless mutants
    • Friedberg D, Jager KM, Kessel M, Silman NJ and Bergman B (1993) Rubisco but not Rubisco activase is clustered in the carboxysomes of the cyanobacterium Synechococcus sp. PCC 7942: Mud-induced carboxysomeless mutants. Mol Microbiol 9: 1193-1201
    • (1993) Mol Microbiol , vol.9 , pp. 1193-1201
    • Friedberg, D.1    Jager, K.M.2    Kessel, M.3    Silman, N.J.4    Bergman, B.5
  • 18
    • 0030666224 scopus 로고    scopus 로고
    • Crystal structure of the δ' subunit of the clamp-loader complex of E. coli DNA polymerase III
    • Guenther B, Onrust R, Sali A, O'Donnell M and Kuriyan J (1997) Crystal structure of the δ' subunit of the clamp-loader complex of E. coli DNA polymerase III. Cell 91: 335-345
    • (1997) Cell , vol.91 , pp. 335-345
    • Guenther, B.1    Onrust, R.2    Sali, A.3    O'Donnell, M.4    Kuriyan, J.5
  • 19
    • 7144226594 scopus 로고    scopus 로고
    • Regulation of Rubisco activation in antisense plants of tobacco containing reduced levels of Rubisco activase
    • Hammond ET, Andrews TJ, Mott KA and Woodrow IE (1998a) Regulation of Rubisco activation in antisense plants of tobacco containing reduced levels of Rubisco activase. Plant J 14: 101-110
    • (1998) Plant J , vol.14 , pp. 101-110
    • Hammond, E.T.1    Andrews, T.J.2    Mott, K.A.3    Woodrow, I.E.4
  • 20
    • 0000435087 scopus 로고    scopus 로고
    • Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase by carbamylation and 2-carboxyarabinitol 1-phosphate in tobacco: Insights from studies of antisense plants containing reduced amounts of Rubisco activase
    • Hammond ET, Andrews TJ and Woodrow IE (1998b) Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase by carbamylation and 2-carboxyarabinitol 1-phosphate in tobacco: insights from studies of antisense plants containing reduced amounts of Rubisco activase. Plant Physiol 118: 1463-1471
    • (1998) Plant Physiol , vol.118 , pp. 1463-1471
    • Hammond, E.T.1    Andrews, T.J.2    Woodrow, I.E.3
  • 21
    • 0028245595 scopus 로고
    • Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase-oxygenase
    • Hartman FC and Harpel MR (1994) Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase-oxygenase. Annual Review of Biochemistry 63: 197-234
    • (1994) Annual Review of Biochemistry , vol.63 , pp. 197-234
    • Hartman, F.C.1    Harpel, M.R.2
  • 22
    • 0031401470 scopus 로고    scopus 로고
    • Ribulose-1,5-bisphosphate carboxylase/oxygenase activase deficiency delays senescence of ribulose-1,5-bisphosphate carboxylase/oxygenase but progressively impairs its catalysis during tobacco leaf development
    • He ZL, von Caemmerer S, Hudson GS, Price GD, Badger MR and Andrews TJ (1997) Ribulose-1,5-bisphosphate carboxylase/oxygenase activase deficiency delays senescence of ribulose-1,5-bisphosphate carboxylase/oxygenase but progressively impairs its catalysis during tobacco leaf development. Plant Physiol 115: 1569-1580
    • (1997) Plant Physiol , vol.115 , pp. 1569-1580
    • He, Z.L.1    Von Caemmerer, S.2    Hudson, G.S.3    Price, G.D.4    Badger, M.R.5    Andrews, T.J.6
  • 23
    • 0033942099 scopus 로고    scopus 로고
    • Alteration of the adenine nucleotide response and increased Rubisco activation activity of Arabidopsis Rubisco activase by site-directed mutagenesis
    • Kallis RP, Ewy RG and Portis AR Jr (2000) Alteration of the adenine nucleotide response and increased Rubisco activation activity of Arabidopsis Rubisco activase by site-directed mutagenesis. Plant Physiol 123: 1077-1086
    • (2000) Plant Physiol , vol.123 , pp. 1077-1086
    • Kallis, R.P.1    Ewy, R.G.2    Portis A.R., Jr.3
  • 24
    • 0002393676 scopus 로고
    • Influences of leaf temperature on photosynthetic carbon metabolism in wheat
    • Kobza J and Edwards GE (1987) Influences of leaf temperature on photosynthetic carbon metabolism in wheat. Plant Physiol 83: 69-74
    • (1987) Plant Physiol , vol.83 , pp. 69-74
    • Kobza, J.1    Edwards, G.E.2
  • 25
    • 0029959968 scopus 로고    scopus 로고
    • Rice gibberellin-binding phosphoprotein structurally related to ribulose-1,5-bisphosphate carboxylase-oxygenase activase
    • Komatsu S, Masuda T and Hirano H (1996) Rice gibberellin-binding phosphoprotein structurally related to ribulose-1,5-bisphosphate carboxylase-oxygenase activase. FEBS Lett 384: 167-171
    • (1996) FEBS Lett , vol.384 , pp. 167-171
    • Komatsu, S.1    Masuda, T.2    Hirano, H.3
  • 26
    • 0000990523 scopus 로고
    • m values for ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase using the spectrophotometric assay of Rubisco activity
    • m values for ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase using the spectrophotometric assay of Rubisco activity. Plant Physiol 95: 604-609
    • (1991) Plant Physiol , vol.95 , pp. 604-609
    • Lan, Y.1    Mott, K.A.2
  • 28
    • 0030764617 scopus 로고    scopus 로고
    • Specificity for activase is changed by a Pro-89 to Arg substitution in the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Larson EM, O'Brien CM, Zhu GH, Spreitzer RJ and Portis AR Jr (1997) Specificity for activase is changed by a Pro-89 to Arg substitution in the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase. J Biol Chem 272: 17033-17037
    • (1997) J Biol Chem , vol.272 , pp. 17033-17037
    • Larson, E.M.1    O'Brien, C.M.2    Zhu, G.H.3    Spreitzer, R.J.4    Portis A.R., Jr.5
  • 29
    • 0032818558 scopus 로고    scopus 로고
    • Inhibition and acclimation of photosynthesis to heat stress is closely correlated with activation of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Law RD and Crafts-Brandner SJ (1999) Inhibition and acclimation of photosynthesis to heat stress is closely correlated with activation of ribulose-1,5-bisphosphate carboxylase/oxygenase. Plant Physiol 120: 173-181
    • (1999) Plant Physiol , vol.120 , pp. 173-181
    • Law, R.D.1    Crafts-Brandner, S.J.2
  • 30
    • 0035864385 scopus 로고    scopus 로고
    • High temperature stress increases the expression of wheat leaf ribulose-1,5-bisphosphate carboxylase/oxygenase activase protein
    • Law RD and Crafts-Brandner SJ (2001) High temperature stress increases the expression of wheat leaf ribulose-1,5-bisphosphate carboxylase/oxygenase activase protein. Arch Biochem Biophys 386: 261-267
    • (2001) Arch Biochem Biophys , vol.386 , pp. 261-267
    • Law, R.D.1    Crafts-Brandner, S.J.2
  • 31
    • 0035787038 scopus 로고    scopus 로고
    • Heat stress induces the synthesis of a new form of ribulose-1,5-bisphosphate carboxylase/oxygenase activase in cotton leaves
    • Law RD, Crafts-Brandner SJ and Salvucci ME (2001) Heat stress induces the synthesis of a new form of ribulose-1,5-bisphosphate carboxylase/oxygenase activase in cotton leaves. Planta 214: 117-125
    • (2001) Planta , vol.214 , pp. 117-125
    • Law, R.D.1    Crafts-Brandner, S.J.2    Salvucci, M.E.3
  • 32
    • 0027564544 scopus 로고
    • The Rubisco activase (rca) gene is located downstream from rbcS in Anabaena sp. strain CA and is detected in other Anabaena/Nostoc strains
    • Li L-A, Gibson JL and Tabita FR (1993) The Rubisco activase (rca) gene is located downstream from rbcS in Anabaena sp. strain CA and is detected in other Anabaena/Nostoc strains. Plant Mol Biol 21: 753-764
    • (1993) Plant Mol Biol , vol.21 , pp. 753-764
    • Li, L.-A.1    Gibson, J.L.2    Tabita, F.R.3
  • 33
    • 0033150311 scopus 로고    scopus 로고
    • Inactivation of the monocistronic rca gene in Anabaena variabilis suggests a physiological ribulose bisphosphate carboxylase oxygenase activase-like function in heterocystous cyanobacteria
    • Li L-A, Zianni MR and Tabita FR (1999) Inactivation of the monocistronic rca gene in Anabaena variabilis suggests a physiological ribulose bisphosphate carboxylase oxygenase activase-like function in heterocystous cyanobacteria. Plant Mol Biol 40: 467-478
    • (1999) Plant Mol Biol , vol.40 , pp. 467-478
    • Li, L.-A.1    Zianni, M.R.2    Tabita, F.R.3
  • 34
    • 0012534216 scopus 로고
    • Activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) by Rubisco activase: Effects of some sugar phosphates
    • Lilley RM and Portis AR Jr (1990) Activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) by Rubisco activase: effects of some sugar phosphates. Plant Physiol 94: 245-250
    • (1990) Plant Physiol , vol.94 , pp. 245-250
    • Lilley, R.M.1    Portis A.R., Jr.2
  • 35
    • 0031400787 scopus 로고    scopus 로고
    • +, and activase concentrations indicate a functional similarity to actin?
    • +, and activase concentrations indicate a functional similarity to actin? Plant Physiol 114: 606-613
    • (1997) Plant Physiol , vol.114 , pp. 606-613
    • Lilley, R.M.1    Portis A.R., Jr.2
  • 36
    • 0017253134 scopus 로고
    • The activation of ribulose-1,-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications
    • Lorimer GH, Badger MR and Andrews TJ (1976) The activation of ribulose-1,-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications. Biochemistry 15: 529-536
    • (1976) Biochemistry , vol.15 , pp. 529-536
    • Lorimer, G.H.1    Badger, M.R.2    Andrews, T.J.3
  • 37
    • 0034490454 scopus 로고    scopus 로고
    • Isolation of ccmKLMN genes from the marine cyanobacterium, Synechococcus sp. PCC7002 (Cyanophyceae), and evidence that CcmM is essential for carboxysome assembly
    • Ludwig M, Sültemeyer D and Price GD (2000) Isolation of ccmKLMN genes from the marine cyanobacterium, Synechococcus sp. PCC7002 (Cyanophyceae), and evidence that CcmM is essential for carboxysome assembly. J Phycol 36: 1109-1118
    • (2000) J Phycol , vol.36 , pp. 1109-1118
    • Ludwig, M.1    Sültemeyer, D.2    Price, G.D.3
  • 38
    • 0030949615 scopus 로고    scopus 로고
    • Activation and deactivation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) in three marine microalgae
    • MacIntyre HL, Sharkey TD and Geider RJ (1997) Activation and deactivation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) in three marine microalgae. Photosynth Res 51: 93-106
    • (1997) Photosynth Res , vol.51 , pp. 93-106
    • MacIntyre, H.L.1    Sharkey, T.D.2    Geider, R.J.3
  • 40
    • 0030029581 scopus 로고    scopus 로고
    • 2-assimilation rate, Rubisco carbamylation and Rubisco activase content in activase-deficient transgenic tobacco suggests a simple model of activase action
    • 2-assimilation rate, Rubisco carbamylation and Rubisco activase content in activase-deficient transgenic tobacco suggests a simple model of activase action. Planta 198: 604-613
    • (1996) Planta , vol.198 , pp. 604-613
    • Mate, C.J.1    Von Caemmerer, S.2    Evans, J.R.3    Hudson, G.S.4    Andrews, T.J.5
  • 41
    • 0002471590 scopus 로고
    • RuBisCo activase is present in the pyrenoid of green algae
    • McKay RML, Gibbs SP and Vaughn KC (1991) RuBisCo activase is present in the pyrenoid of green algae. Protoplasma 162: 38-45
    • (1991) Protoplasma , vol.162 , pp. 38-45
    • McKay, R.M.L.1    Gibbs, S.P.2    Vaughn, K.C.3
  • 42
    • 0033962766 scopus 로고    scopus 로고
    • Modelling the role of Rubisco activase in limiting non-steady-state photosynthesis
    • Mott KA and Woodrow IE (2000) Modelling the role of Rubisco activase in limiting non-steady-state photosynthesis. J Expt Bot 51: 399-406
    • (2000) J Expt Bot , vol.51 , pp. 399-406
    • Mott, K.A.1    Woodrow, I.E.2
  • 43
    • 0031424710 scopus 로고    scopus 로고
    • Kinetics of Rubisco activation as determined from gas-exchange measurements in antisense plants of Arabidopsis thaliana containing reduced levels of Rubisco activase
    • Mott KA, Snyder GW and Woodrow IE (1997) Kinetics of Rubisco activation as determined from gas-exchange measurements in antisense plants of Arabidopsis thaliana containing reduced levels of Rubisco activase. Aust J Plant Physiol 24: 811-818
    • (1997) Aust J Plant Physiol , vol.24 , pp. 811-818
    • Mott, K.A.1    Snyder, G.W.2    Woodrow, I.E.3
  • 44
    • 0034695494 scopus 로고    scopus 로고
    • Trienoic fatty acids and plant tolerance of high temperature
    • Murakami Y, Tsuyama M, Kobayashi Y, Kodama H and Iba K (2000) Trienoic fatty acids and plant tolerance of high temperature. Science 287: 476-479
    • (2000) Science , vol.287 , pp. 476-479
    • Murakami, Y.1    Tsuyama, M.2    Kobayashi, Y.3    Kodama, H.4    Iba, K.5
  • 45
    • 0032969563 scopus 로고    scopus 로고
    • +: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • +: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res 9: 27-43
    • (1999) Genome Res , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 46
    • 0034885052 scopus 로고    scopus 로고
    • + superfamily ATPases: Common structure - Diverse function
    • + superfamily ATPases: common structure - diverse function. Genes Cells 6: 575-597
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 47
    • 0034714290 scopus 로고    scopus 로고
    • Activase region on chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase: Nonconservative substitution in the large subunit alters species specificity of protein interaction
    • Ott CM, Smith BD, Portis AR Jr and Spreitzer RJ (2000) Activase region on chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase: nonconservative substitution in the large subunit alters species specificity of protein interaction. J Biol Chem 275: 26241-26244
    • (2000) J Biol Chem , vol.275 , pp. 26241-26244
    • Ott, C.M.1    Smith, B.D.2    Portis A.R., Jr.3    Spreitzer, R.J.4
  • 49
    • 0001748327 scopus 로고
    • Light limitation of photosynthesis and activation of ribulose bisphosphate carboxylase in wheat seedlings
    • Perchorowicz JT, Raynes DA and Jensen RG (1981) Light limitation of photosynthesis and activation of ribulose bisphosphate carboxylase in wheat seedlings. Proc Natl Acad Sci USA 78: 2985-2989
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 2985-2989
    • Perchorowicz, J.T.1    Raynes, D.A.2    Jensen, R.G.3
  • 51
    • 0000384908 scopus 로고
    • Regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase activity
    • Portis AR Jr (1992) Regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase activity. Annu Rev Plant Physiol Plant Mol Biol 43: 415-437
    • (1992) Annu Rev Plant Physiol Plant Mol Biol , vol.43 , pp. 415-437
    • Portis A.R., Jr.1
  • 52
    • 0000579738 scopus 로고
    • The regulation of Rubisco by Rubisco activase
    • Portis AR Jr (1995) The regulation of Rubisco by Rubisco activase. J Expt Bot 46: 1285-1291
    • (1995) J Expt Bot , vol.46 , pp. 1285-1291
    • Portis A.R., Jr.1
  • 53
    • 0012533273 scopus 로고    scopus 로고
    • The Rubisco activase-Rubisco system: An ATPase-dependent association that regulates photosynthesis
    • McManus MT, Laing WL and Allen AC (eds). Sheffield Academic Press, Sheffield, England
    • Portis AR Jr (2001) The Rubisco activase-Rubisco system: an ATPase-dependent association that regulates photosynthesis. In: McManus MT, Laing WL and Allen AC (eds) Protein - Protein Interactions in Plant Biology, pp 30-52. Sheffield Academic Press, Sheffield, England
    • (2001) Protein - Protein Interactions in Plant Biology , pp. 30-52
    • Portis A.R., Jr.1
  • 55
    • 0029178064 scopus 로고
    • Subsaturating ribulose-1,5-bisphosphate concentration promotes inactivation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) - Studies using continuous substrate addition in the presence and absence of Rubisco activase
    • Portis AR Jr, Lilley RM and Andrews TJ (1995) Subsaturating ribulose-1,5-bisphosphate concentration promotes inactivation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) - studies using continuous substrate addition in the presence and absence of Rubisco activase. Plant Physiol 109: 1441-1451
    • (1995) Plant Physiol , vol.109 , pp. 1441-1451
    • Portis A.R., Jr.1    Lilley, R.M.2    Andrews, T.J.3
  • 56
    • 0027223239 scopus 로고
    • Analysis of a genomic DNA region from the cyanobacterium Synechococcus sp. strain PCC7942 involved in carboxysome assembly and function
    • Price GD, Howitt SM, Harrison K and Badger MR (1993) Analysis of a genomic DNA region from the cyanobacterium Synechococcus sp. strain PCC7942 involved in carboxysome assembly and function. J Bacteriol 175: 2871-2879
    • (1993) J Bacteriol , vol.175 , pp. 2871-2879
    • Price, G.D.1    Howitt, S.M.2    Harrison, K.3    Badger, M.R.4
  • 57
    • 34249918949 scopus 로고
    • Decreased ribulose-1,5-bisphosphate carboxylase-oxygenase in transgenic tobacco transformed with 'antisense' rbcS: I. Impact on photosynthesis in ambient growth conditions
    • Quick WP, Schurr U, Scheibe R, Schulze ED, Rodermel SR, Bogorad L and Stitt M (1991) Decreased ribulose-1,5-bisphosphate carboxylase-oxygenase in transgenic tobacco transformed with 'antisense' rbcS: I. Impact on photosynthesis in ambient growth conditions. Planta 183: 542-554
    • (1991) Planta , vol.183 , pp. 542-554
    • Quick, W.P.1    Schurr, U.2    Scheibe, R.3    Schulze, E.D.4    Rodermel, S.R.5    Bogorad, L.6    Stitt, M.7
  • 58
    • 0000420474 scopus 로고
    • Involvement of stromal ATP in the light activation of ribulose-1,5-bisphosphate carboxylase/oxygenase in intact isolated chloroplasts
    • Robinson SP and Portis AR Jr (1988a) Involvement of stromal ATP in the light activation of ribulose-1,5-bisphosphate carboxylase/oxygenase in intact isolated chloroplasts. Plant Physiol 86: 293-298
    • (1988) Plant Physiol , vol.86 , pp. 293-298
    • Robinson, S.P.1    Portis A.R., Jr.2
  • 59
    • 0001509985 scopus 로고
    • Release of the nocturnal inhibitor, carboxyarabinitol-1-phosphate, from ribulose bisphosphate carboxylase/oxygenase by Rubisco activase
    • Robinson SP and Portis AR Jr (1988b) Release of the nocturnal inhibitor, carboxyarabinitol-1-phosphate, from ribulose bisphosphate carboxylase/oxygenase by Rubisco activase FEBS Lett 233: 413-416
    • (1988) FEBS Lett , vol.233 , pp. 413-416
    • Robinson, S.P.1    Portis A.R., Jr.2
  • 60
    • 0024485948 scopus 로고
    • Adenosine triphosphate hydrolysis by purified Rubisco activase
    • Robinson SP and Portis AR Jr (1989a) Adenosine triphosphate hydrolysis by purified Rubisco activase. Arch Biochem Biophys 268: 93-99
    • (1989) Arch Biochem Biophys , vol.268 , pp. 93-99
    • Robinson, S.P.1    Portis A.R., Jr.2
  • 61
    • 84969903101 scopus 로고
    • Ribulose-1,5-bisphosphate carboxylase/oxygenase activase protein prevents the in vitro decline in activity of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Robinson SP and Portis AR Jr (1989b) Ribulose-1,5-bisphosphate carboxylase/oxygenase activase protein prevents the in vitro decline in activity of ribulose-1,5-bisphosphate carboxylase/oxygenase. Plant Physiol 90: 968-971
    • (1989) Plant Physiol , vol.90 , pp. 968-971
    • Robinson, S.P.1    Portis A.R., Jr.2
  • 63
    • 0001009719 scopus 로고
    • Primary structure of Chlamydomonas reinhardtii ribulose-1,5-bisphosphate carboxylase/oxygenase activase and evidence for a single polypeptide
    • Roesler KR and Ogren WL (1990) Primary structure of Chlamydomonas reinhardtii ribulose-1,5-bisphosphate carboxylase/oxygenase activase and evidence for a single polypeptide. Plant Physiol 95: 1837-1841
    • (1990) Plant Physiol , vol.95 , pp. 1837-1841
    • Roesler, K.R.1    Ogren, W.L.2
  • 64
    • 0035081121 scopus 로고    scopus 로고
    • Rubisco activase: An enzyme with a temperature-dependent dual function?
    • Rokka A, Zhang LX and Aro EM (2001) Rubisco activase: an enzyme with a temperature-dependent dual function? Plant J 25: 463-471
    • (2001) Plant J , vol.25 , pp. 463-471
    • Rokka, A.1    Zhang, L.X.2    Aro, E.M.3
  • 65
    • 0025774985 scopus 로고
    • Organization and expression of two tandemly oriented genes encoding ribulosebisphosphate carboxylase/oxygenase activase in barley
    • Rundle SJ and Zielinski RE (1991) Organization and expression of two tandemly oriented genes encoding ribulosebisphosphate carboxylase/oxygenase activase in barley. J Biol Chem 266: 4677-4685
    • (1991) J Biol Chem , vol.266 , pp. 4677-4685
    • Rundle, S.J.1    Zielinski, R.E.2
  • 66
    • 0034143622 scopus 로고    scopus 로고
    • The role of chloroplast electron transport and metabolites in modulating Rubisco activity in tobacco. Insights from transgenic plants with reduced amounts of cytochrome b/f complex or glyceraldehyde 3-phosphate dehydrogenase
    • Ruuska SA, Andrews TJ, Badger MR, Price GD and von Caemmerer 5 (2000) The role of chloroplast electron transport and metabolites in modulating Rubisco activity in tobacco. Insights from transgenic plants with reduced amounts of cytochrome b/f complex or glyceraldehyde 3-phosphate dehydrogenase. Plant Physiol 122: 491-504
    • (2000) Plant Physiol , vol.122 , pp. 491-504
    • Ruuska, S.A.1    Andrews, T.J.2    Badger, M.R.3    Price, G.D.4    Von Caemmerer, S.5
  • 67
    • 0026460010 scopus 로고
    • Subunit interactions of Rubisco activase - Polyethylene glycol promotes self-association, stimulates ATPase and activation activities, and enhances interactions with Rubisco
    • Salvucci ME (1992) Subunit interactions of Rubisco activase - polyethylene glycol promotes self-association, stimulates ATPase and activation activities, and enhances interactions with Rubisco. Arch Biochem Biophys 298: 688-696
    • (1992) Arch Biochem Biophys , vol.298 , pp. 688-696
    • Salvucci, M.E.1
  • 68
    • 0027674232 scopus 로고
    • Covalent modification of a highly reactive and essential lysine residue of ribulose-1,5-bisphosphate carboxylase-oxygenase activase
    • Salvucci ME (1993) Covalent modification of a highly reactive and essential lysine residue of ribulose-1,5-bisphosphate carboxylase-oxygenase activase. Plant Physiol 103: 501-508
    • (1993) Plant Physiol , vol.103 , pp. 501-508
    • Salvucci, M.E.1
  • 69
    • 0028172266 scopus 로고
    • Site-directed mutagenesis of a reactive lysyl residue (Lys-247) of Rubisco activase
    • Salvucci ME and Klein RR (1994) Site-directed mutagenesis of a reactive lysyl residue (Lys-247) of Rubisco activase. Arch Biochem Biophys 314: 178-185
    • (1994) Arch Biochem Biophys , vol.314 , pp. 178-185
    • Salvucci, M.E.1    Klein, R.R.2
  • 70
    • 0030047366 scopus 로고    scopus 로고
    • The mechanism of Rubisco activase: Insights from studies of the properties and structure of the enzyme
    • Salvucci ME and Ogren WL (1996) The mechanism of Rubisco activase: insights from studies of the properties and structure of the enzyme. Photosynth Res 47: 1-11
    • (1996) Photosynth Res , vol.47 , pp. 1-11
    • Salvucci, M.E.1    Ogren, W.L.2
  • 71
    • 34250112628 scopus 로고
    • A soluble chloroplast protein catalyzes ribulosebisphosphate carboxylase/oxygenase activation in vivo
    • Salvucci ME, Portis AR Jr and Ogren WL (1985) A soluble chloroplast protein catalyzes ribulosebisphosphate carboxylase/oxygenase activation in vivo. Photosynth Res 7: 193-201
    • (1985) Photosynth Res , vol.7 , pp. 193-201
    • Salvucci, M.E.1    Portis A.R., Jr.2    Ogren, W.L.3
  • 72
    • 0000134277 scopus 로고
    • 2 response of ribulose-1,5-bisphosphate carboxytase/oxygenase activation in Arabidopsis leaves
    • 2 response of ribulose-1,5-bisphosphate carboxytase/oxygenase activation in Arabidopsis leaves. Plant Physiol 80: 655-659
    • (1986) Plant Physiol , vol.80 , pp. 655-659
    • Salvucci, M.E.1    Portis A.R., Jr.2    Ogren, W.L.3
  • 74
    • 0027267295 scopus 로고
    • Photoaffinity labeling of ribulose-1,5-bisphosphate carboxylase/oxygenase activase with ATP γ-benzophenone: Identification of the ATP γ-phosphate binding domain
    • Salvucci ME, Rajagopalan K, Sievert G, Haley BE and Watt DS (1993) Photoaffinity labeling of ribulose-1,5-bisphosphate carboxylase/oxygenase activase with ATP γ-benzophenone: identification of the ATP γ-phosphate binding domain. J Biol Chem 268: 14239-14244
    • (1993) J Biol Chem , vol.268 , pp. 14239-14244
    • Salvucci, M.E.1    Rajagopalan, K.2    Sievert, G.3    Haley, B.E.4    Watt, D.S.5
  • 75
    • 0028566102 scopus 로고
    • Photoaffinity labeling of the ATP binding domain of Rubisco activase and a separate domain involved in the activation of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Salvucci ME, Chavan AJ, Klein RR, Rajagopolan K and Haley BE (1994) Photoaffinity labeling of the ATP binding domain of Rubisco activase and a separate domain involved in the activation of ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry 33: 14879-14886
    • (1994) Biochemistry , vol.33 , pp. 14879-14886
    • Salvucci, M.E.1    Chavan, A.J.2    Klein, R.R.3    Rajagopolan, K.4    Haley, B.E.5
  • 76
    • 0035193658 scopus 로고    scopus 로고
    • Exceptional sensitivity of Rubisco activase to thermal denaturation in vitro and in vivo
    • Salvucci ME, Osteryoung KW, Crafts-Brandner SJ amd Vierling E (2001) Exceptional sensitivity of Rubisco activase to thermal denaturation in vitro and in vivo. Plant Physiol 127: 1053-1064
    • (2001) Plant Physiol , vol.127 , pp. 1053-1064
    • Salvucci, M.E.1    Osteryoung, K.W.2    Crafts-Brandner, S.J.3    Vierling, E.4
  • 77
    • 0028910189 scopus 로고
    • Rubisco activase, a possible new member of the molecular chaperone family
    • Sánchez de Jiménez E, Medrano L and Martínez-Barajas E (1995) Rubisco activase, a possible new member of the molecular chaperone family. Biochemistry 34: 2826-2831
    • (1995) Biochemistry , vol.34 , pp. 2826-2831
    • Sánchez De Jiménez, E.1    Medrano, L.2    Martínez-Barajas, E.3
  • 79
    • 0027371878 scopus 로고
    • Formation of the active site of ribulose-1,5-bisphosphate carboxylase-oxygenase by a disorder-order transition from the unactivated to the activated form
    • Schreuder HA, Knight S, Curmi PMG, Andersson I, Cascio D, Brändén CI and Eisenberg D (1993) Formation of the active site of ribulose-1,5-bisphosphate carboxylase-oxygenase by a disorder-order transition from the unactivated to the activated form. Proc Natl Acad Sci USA 90: 9968-9972
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9968-9972
    • Schreuder, H.A.1    Knight, S.2    Curmi, P.M.G.3    Andersson, I.4    Cascio, D.5    Brändén, C.I.6    Eisenberg, D.7
  • 81
    • 0022404626 scopus 로고
    • Regulation of ribulose bisphosphate carboxylase activity in vivo by a light-modulated inhibitor of catalysis
    • Seemann JR, Berry JA, Freas SM and Krump MA (1985) Regulation of ribulose bisphosphate carboxylase activity in vivo by a light-modulated inhibitor of catalysis. Proc Natl Acad Sci USA 82: 8024-8028
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8024-8028
    • Seemann, J.R.1    Berry, J.A.2    Freas, S.M.3    Krump, M.A.4
  • 82
    • 0000933669 scopus 로고
    • Binding of a phosphorylated inhibitor to ribulose bisphosphate carboxylase/oxygenase during the night
    • Servaites JC (1985) Binding of a phosphorylated inhibitor to ribulose bisphosphate carboxylase/oxygenase during the night. Plant Physiol 78: 834-843
    • (1985) Plant Physiol , vol.78 , pp. 834-843
    • Servaites, J.C.1
  • 83
    • 0000729240 scopus 로고
    • Evaluating the role of Rubisco regulation in photosynthesis of C3 plants
    • Sharkey TD (1989) Evaluating the role of Rubisco regulation in photosynthesis of C3 plants. Phil Trans R Soc London 323: 434-448
    • (1989) Phil Trans R Soc London , vol.323 , pp. 434-448
    • Sharkey, T.D.1
  • 84
    • 0002472386 scopus 로고
    • Feedback limitation of photosynthesis and the physiological role of ribulose bisphosphate carboxylase carbamylation
    • Sharkey TD (1990) Feedback limitation of photosynthesis and the physiological role of ribulose bisphosphate carboxylase carbamylation. Bot Mag Tokyo Special Issue 2: 87-105
    • (1990) Bot Mag Tokyo Special Issue , vol.2 , pp. 87-105
    • Sharkey, T.D.1
  • 85
    • 0034695540 scopus 로고    scopus 로고
    • Plant biology - Some like it hot
    • Sharkey TD (2000) Plant biology - some like it hot. Science 287: 435-437
    • (2000) Science , vol.287 , pp. 435-437
    • Sharkey, T.D.1
  • 87
    • 0000229121 scopus 로고    scopus 로고
    • Increased heat sensitivity of photosynthesis in tobacco plants with reduced Rubisco activase
    • Sharkey TD, Badger MR, von Caemmerer S and Andrews TJ (2001) Increased heat sensitivity of photosynthesis in tobacco plants with reduced Rubisco activase. Photosynth Res 67: 147-156
    • (2001) Photosynth Res , vol.67 , pp. 147-156
    • Sharkey, T.D.1    Badger, M.R.2    Von Caemmerer, S.3    Andrews, T.J.4
  • 88
    • 0036294223 scopus 로고    scopus 로고
    • 2+-dependent protein kinase component downstream to the gibberellin-binding phosphoprotein, RuBisCO activase, in rice
    • 2+-dependent protein kinase component downstream to the gibberellin-binding phosphoprotein, RuBisCO activase, in rice. Biochem Biophys Res Commun 290: 690-695
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 690-695
    • Sharma, A.1    Komatsu, S.2
  • 89
    • 0012535192 scopus 로고
    • Alteration of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase activase activities by site-directed mutagenesis
    • Shen JB and Ogren WL (1992) Alteration of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase activase activities by site-directed mutagenesis. Plant Physiol 99: 1201-1207
    • (1992) Plant Physiol , vol.99 , pp. 1201-1207
    • Shen, J.B.1    Ogren, W.L.2
  • 90
    • 0025738366 scopus 로고
    • Expression of the two isoforms of spinach ribulose 1,5-bisphosphate carboxylase activase and essentiality of the conserved lysine in the consensus nucleotide-binding domain
    • Shen JB, Orozco EM and Ogren WL (1991) Expression of the two isoforms of spinach ribulose 1,5-bisphosphate carboxylase activase and essentiality of the conserved lysine in the consensus nucleotide-binding domain. J Biol Chem 266: 8963-8968
    • (1991) J Biol Chem , vol.266 , pp. 8963-8968
    • Shen, J.B.1    Orozco, E.M.2    Ogren, W.L.3
  • 91
    • 0001596719 scopus 로고
    • A mutant of Arabidopsis thaliana which lacks activation of RuBP carboxylase in vivo
    • Somerville CR, Portis AR Jr and Ogren WL (1982) A mutant of Arabidopsis thaliana which lacks activation of RuBP carboxylase in vivo. Plant Physiol 70: 381-387
    • (1982) Plant Physiol , vol.70 , pp. 381-387
    • Somerville, C.R.1    Portis A.R., Jr.2    Ogren, W.L.3
  • 92
    • 0032817398 scopus 로고    scopus 로고
    • Questions about the complexity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Spreitzer RJ (1999) Questions about the complexity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Photosynth Res 60: 29-42
    • (1999) Photosynth Res , vol.60 , pp. 29-42
    • Spreitzer, R.J.1
  • 93
    • 0037001967 scopus 로고    scopus 로고
    • RUBISCO: Structure, regulatory interactions, and possibilities for a better enzyme
    • Spreitzer RJ and Salvucci ME (2002) RUBISCO: structure, regulatory interactions, and possibilities for a better enzyme. Annu Rev Plant Biol 53: 449-485
    • (2002) Annu Rev Plant Biol , vol.53 , pp. 449-485
    • Spreitzer, R.J.1    Salvucci, M.E.2
  • 94
    • 0030064654 scopus 로고    scopus 로고
    • Structural transitions during activation and ligand binding in hexadecameric Rubisco inferred from the crystal structure of the activated unliganded spinach enzyme
    • Taylor TC and Andersson I (1996) Structural transitions during activation and ligand binding in hexadecameric Rubisco inferred from the crystal structure of the activated unliganded spinach enzyme. Nature Struct Biol 3: 95-101
    • (1996) Nature Struct Biol , vol.3 , pp. 95-101
    • Taylor, T.C.1    Andersson, I.2
  • 95
    • 0031592468 scopus 로고    scopus 로고
    • The structure of the complex between Rubisco and its natural substrate ribulose 1,5-bisphosphate
    • Taylor TC and Andersson I (1997) The structure of the complex between Rubisco and its natural substrate ribulose 1,5-bisphosphate. J Mol Biol 265: 432-444
    • (1997) J Mol Biol , vol.265 , pp. 432-444
    • Taylor, T.C.1    Andersson, I.2
  • 96
    • 0033166098 scopus 로고    scopus 로고
    • Molecular characterization of ribulose-1,5-bisphosphate carboxylase/oxygenase activase in rice leaves
    • To KY, Suen DF and Chen SCG (1999) Molecular characterization of ribulose-1,5-bisphosphate carboxylase/oxygenase activase in rice leaves. Planta 209: 66-76
    • (1999) Planta , vol.209 , pp. 66-76
    • To, K.Y.1    Suen, D.F.2    Chen, S.C.G.3
  • 97
    • 0030056076 scopus 로고    scopus 로고
    • Activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) involves Rubisco activase Trp16
    • van de Loo FJ and Salvucci ME (1996) Activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) involves Rubisco activase Trp16. Biochemistry 35: 8143-8148
    • (1996) Biochemistry , vol.35 , pp. 8143-8148
    • Van De Loo, F.J.1    Salvucci, M.E.2
  • 98
    • 0032584288 scopus 로고    scopus 로고
    • Involvement of two aspartate residues of Rubisco activase in coordination of the ATP γ-phosphate and subunit cooperativity
    • van de Loo FJ and Salvucci ME (1998) Involvement of two aspartate residues of Rubisco activase in coordination of the ATP γ-phosphate and subunit cooperativity. Biochemistry 37: 4621-4625
    • (1998) Biochemistry , vol.37 , pp. 4621-4625
    • Van De Loo, F.J.1    Salvucci, M.E.2
  • 99
    • 84981566420 scopus 로고
    • Photosynthetic induction phenomena and the light activation of ribulose diphosphate carboxylase
    • Walker DA (1973) Photosynthetic induction phenomena and the light activation of ribulose diphosphate carboxylase. New Phytol 72: 209-235
    • (1973) New Phytol , vol.72 , pp. 209-235
    • Walker, D.A.1
  • 100
    • 0000907139 scopus 로고
    • Dissociation of ribulose-1,5-bisphosphate bound to ribulose-1,5-bisphosphate carboxylase/oxygenase and its enhancement by ribulose-1,5-bisphosphate carboxylase/oxygenase activase-mediated hydrolysis of ATP
    • Wang ZY and Portis AR Jr (1992) Dissociation of ribulose-1,5-bisphosphate bound to ribulose-1,5-bisphosphate carboxylase/oxygenase and its enhancement by ribulose-1,5-bisphosphate carboxylase/oxygenase activase-mediated hydrolysis of ATP. Plant Physiol 99: 1348-1353
    • (1992) Plant Physiol , vol.99 , pp. 1348-1353
    • Wang, Z.Y.1    Portis A.R., Jr.2
  • 101
    • 0027305570 scopus 로고
    • 2+ and ATP or adenosine 5′[γ-thio]-triphosphate (ATPγS) enhances intrinsic fluorescence and induces aggregation which increases the activity of spinach Rubisco activase
    • 2+ and ATP or adenosine 5′[γ-thio]-triphosphate (ATPγS) enhances intrinsic fluorescence and induces aggregation which increases the activity of spinach Rubisco activase. Biochim Biophys Acta 1202: 47-55
    • (1993) Biochim Biophys Acta , vol.1202 , pp. 47-55
    • Wang, Z.Y.1    Ramage, R.T.2    Portis A.R., Jr.3
  • 102
    • 0001616104 scopus 로고
    • Species-dependent variation in the interaction of substrate-bound ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and Rubisco activase
    • Wang ZY, Synder GW, Esau BD, Portis AR Jr and Ogren WL (1992) Species-dependent variation in the interaction of substrate-bound ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and Rubisco activase. Plant Physiol 100: 1858-1862
    • (1992) Plant Physiol , vol.100 , pp. 1858-1862
    • Wang, Z.Y.1    Synder, G.W.2    Esau, B.D.3    Portis A.R., Jr.4    Ogren, W.L.5
  • 103
    • 0002473289 scopus 로고
    • Reversible heat-inactivation of the Calvin cycle: A possible mechanism of the temperature regulation of photosynthesis
    • Weis E (1981a) Reversible heat-inactivation of the Calvin cycle: a possible mechanism of the temperature regulation of photosynthesis. Planta 151: 33-39
    • (1981) Planta , vol.151 , pp. 33-39
    • Weis, E.1
  • 104
    • 0000687223 scopus 로고
    • The temperature-sensitivity of dark-inactivation and light-activation of the ribulose-1,5-bisphosphate carboxylase in spinach chloroplasts
    • Weis E (1981b) The temperature-sensitivity of dark-inactivation and light-activation of the ribulose-1,5-bisphosphate carboxylase in spinach chloroplasts. FEBS Lett 129: 197-200
    • (1981) FEBS Lett , vol.129 , pp. 197-200
    • Weis, E.1
  • 105
    • 0000520645 scopus 로고
    • Plants and high temperature stress
    • Long SP and Woodward FI (eds). Society of Experimental Botany, Cambridge, UK
    • Weis E and Berry JA (1988) Plants and high temperature stress. In: Long SP and Woodward FI (eds) Plants and Temperature, pp 327-346. Society of Experimental Botany, Cambridge, UK
    • (1988) Plants and Temperature , pp. 327-346
    • Weis, E.1    Berry, J.A.2
  • 106
    • 0023953674 scopus 로고
    • Structure and expression of spinach leaf complementary DNA encoding ribulose bisphosphate carboxylase-oxygenase activase
    • Werneke JM, Zielinski RE and Ogren WL (1988) Structure and expression of spinach leaf complementary DNA encoding ribulose bisphosphate carboxylase-oxygenase activase. Proc Natl Acad Sci USA 85: 787-791
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 787-791
    • Werneke, J.M.1    Zielinski, R.E.2    Ogren, W.L.3
  • 107
    • 0024707622 scopus 로고
    • Alternative mRNA splicing generates the two ribulosebisphosphate carboxylase/oxygenase activase polypeptides in spinach and Arabidopsis
    • Werneke JM, Chatfield JM and Ogren WL (1989) Alternative mRNA splicing generates the two ribulosebisphosphate carboxylase/oxygenase activase polypeptides in spinach and Arabidopsis. Plant Cell 1: 815-825
    • (1989) Plant Cell , vol.1 , pp. 815-825
    • Werneke, J.M.1    Chatfield, J.M.2    Ogren, W.L.3
  • 108
    • 0030064802 scopus 로고    scopus 로고
    • Limitation of the rate of ribulosebisphosphate carboxylase activation by carbamylation and ribulosebisphosphate carboxylase activase activity - Development and tests of a mechanistic model
    • Woodrow IE, Kelly ME and Mott KA (1996) Limitation of the rate of ribulosebisphosphate carboxylase activation by carbamylation and ribulosebisphosphate carboxylase activase activity - development and tests of a mechanistic model. Aust J Plant Physiol 23: 141-149
    • (1996) Aust J Plant Physiol , vol.23 , pp. 141-149
    • Woodrow, I.E.1    Kelly, M.E.2    Mott, K.A.3
  • 109
    • 0026543904 scopus 로고
    • Characterization of ribulose-1,5-bisphosphate carboxylase/oxygenase carrying ribulose 1,5-bisphosphate at its regulatory sites and the mechanism of interaction of this form of the enzyme with ribulose-1,5-bisphosphate-carboxylase/oxygenase activase
    • Yokota A and Tsujimoto N (1992) Characterization of ribulose-1,5-bisphosphate carboxylase/oxygenase carrying ribulose 1,5-bisphosphate at its regulatory sites and the mechanism of interaction of this form of the enzyme with ribulose-1,5-bisphosphate-carboxylase/oxygenase activase. Eur J Biochem 204: 901-909
    • (1992) Eur J Biochem , vol.204 , pp. 901-909
    • Yokota, A.1    Tsujimoto, N.2
  • 110
    • 0033529948 scopus 로고    scopus 로고
    • Mechanism of light regulation of Rubisco: A specific role for the larger Rubisco activase isoform involving reductive activation by thioredoxin-f
    • Zhang N and Portis AR Jr (1999) Mechanism of light regulation of Rubisco: a specific role for the larger Rubisco activase isoform involving reductive activation by thioredoxin-f. Proc Natl Acad Sci USA 96: 9438-9443
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9438-9443
    • Zhang, N.1    Portis A.R., Jr.2
  • 111
    • 0037022664 scopus 로고    scopus 로고
    • Light modulation of Rubisco in Arabidopsis requires a capacity for redox regulation of the larger Rubisco activase isoform
    • Zhang N, Kallis RP, Ewy RG and Portis AR Jr (2002) Light modulation of Rubisco in Arabidopsis requires a capacity for redox regulation of the larger Rubisco activase isoform. Proc Natl Acad Sci USA 99: 3330-3334
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3330-3334
    • Zhang, N.1    Kallis, R.P.2    Ewy, R.G.3    Portis A.R., Jr.4
  • 112
    • 0034798125 scopus 로고    scopus 로고
    • Characterization of the regulatory function of the 46-kDa isoform of Rubisco activase from Arabidopsis
    • Zhang N, Schürmann P and Portis AR Jr (2001) Characterization of the regulatory function of the 46-kDa isoform of Rubisco activase from Arabidopsis. Photosynth Res 68: 29-37
    • (2001) Photosynth Res , vol.68 , pp. 29-37
    • Zhang, N.1    Schürmann, P.2    Portis A.R., Jr.3
  • 113
    • 0033814056 scopus 로고    scopus 로고
    • Molecular cloning and characterization of cDNAs encoding two isoforms of ribulose-1,5-bisphosphate carboxylase/oxygenase activase in rice (Oryza sativa L.)
    • Zhang ZL and Komatsu S (2000) Molecular cloning and characterization of cDNAs encoding two isoforms of ribulose-1,5-bisphosphate carboxylase/oxygenase activase in rice (Oryza sativa L.). J Biochem 128: 383-389
    • (2000) J Biochem , vol.128 , pp. 383-389
    • Zhang, Z.L.1    Komatsu, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.