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Decrease in carbamylation of rubisco by high CO2 concentration is due to decrease of rubisco activase in kidney bean

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Abstract

Decrease in rubisco activation at high CO2 concentration was caused by decrease in carbamylation of rubisco (Rohet al., 1996). However, it is unclear whether decrease in carbamylation rate at high CO2 concentration is due to decrease in activity itself or content of rubisco activase. To clarify this ambiguity, investigation was performed to determine effects of CO2 concentration on rubisco activase with kidney bean (Phaseolus vulgaris L.) leaves grown at normal CO2 (350 ppm) and high CO2 (650 ppm) concentration. The analysis of Western blotting showed that the 50 and 14.5 kl) polypeptides were identified immunochemically as the large and small subunits of rubisco in the preparation, respectively. For the 14.5 kD small subunit, the degree of intensity at high CO2 concentration was similar to that at normal CO2 concentration. For the 50 kD large sububit, however, the intensity of a band at high CO, concentration was significantly higher than that at normal CO2 concentration, indicating that only the large subunit is affected by high CO2 concentration. The analysis of Western immunoblotting showed two major polypeptides at 46 and 42 kD which were identified as rubisco activase subunits. The intensities of two bands were shown to be higher at normal CO2 than high CO2 concentration. These data indicate that decrease of carbamylation resulting from increase of CO2 concentration was caused by rubisco activase. Finally, by employing ATP hydrolysis assay and ELISA, we also observed a significant decrease in both activity and content of rubisco activase as CO2 concentration was raised from normal to high CO2 concentration. These results suggest that decrease in rubisco carbamylation at high CO2 concentration is caused by activity itself and/or content of rubisco activase.

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Literature Cited

  • Andrews, T.J. and G.H. Lorimer. 1987. Rubisco: Structure, mechanisms, and prospects for improvements.In Biochemistry of Plants. M.D. Hatch and N.K. Boardmaan (ed.s.), Vol. 10, Academic Press, New York pp. 131–218.

    Google Scholar 

  • Bowes, G. 1991. Growth at elavated CO2: Photosynthetic responses mediated through rubisco.Plant Cell Environ. 14: 759–806.

    Article  Google Scholar 

  • Bradford, M.M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding.Anal. Biochem. 72: 248–254.

    Article  PubMed  CAS  Google Scholar 

  • Campbell, W.J. and W.L. Ogren. 1990. Electron transport through photosystem I stimulates light activation of ribulose bisphosphate carboxylase/oxygenase (rubisco) by rubisco activasc.Plant Physiol. 94: 479–484.

    Article  PubMed  CAS  Google Scholar 

  • Campbell, W.J. and W.L. Ogren. 1992. Light activation of rubisco by rubisco activase and thylakoid membranes.Plant Cell Physiol. 33: 751–756.

    CAS  Google Scholar 

  • Downton, W.J.S., O. Bjorkman and C.S. Pike. 1980 Consequences of increased atmospheric concentrations of carbon dioxide for growth and photosynthesis of higher plant.In Carbon Dioxide and Climate: Australian Research. G.I. Pearman (ed.). Australian Academy of Science, Canberra, pp. 143–151.

    Google Scholar 

  • Harlow, E. and D. Lane. 1988. Antibodies. A Laboratory manual. Cold Spring Harbor Laboratory.

  • Hartman, F.C. and M.R. Harpel. 1994. Structure, function, regulation and assembly of D-ribulose-l,5-bisphosphate carboxylase/oxygenase.Ann. Rev. Biochem. 63: 197–234.

    Article  PubMed  CAS  Google Scholar 

  • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of the hacteriophage T4.Nature 227: 680–685.

    Article  PubMed  CAS  Google Scholar 

  • Lilley, R.McC. and A.R. Portis, Jr. 1990. Activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) by rubisco activase. Effects of some sugar phosphates.Plant Physiol. 94: 245–250.

    Article  PubMed  CAS  Google Scholar 

  • Lorimer, G.H. andH.M. Miziorko. 1980. Carbamate formation on the ɛ-amino group of a lysyl residue as the basis for the activation of ribulose bisphosphate carboxylase by CO2 and Mg2+.Biochemistry 19: 5321–5328.

    Article  PubMed  CAS  Google Scholar 

  • Majeau, N. and J.R. Coleman. 1996. Effect CO2 of concentration on carbonic anhydrase and ribulose-1,5-bisphosphate carboxylase/oxygenase expression in pea.Plant Physiol. 112: 569–574.

    PubMed  CAS  Google Scholar 

  • Micallef, B.J., K.A. Haskins, P.J. Vanderveer, K.S. Roh, C.K. Shewmaker and T.D. Sharkey. 1995 Altered photosynthesis, flowering, and fruiting in transgenic tomato plants that have an increased capacity for sucrose synthesis.Planta 196: 327–334.

    Article  CAS  Google Scholar 

  • Miziorko, H.M. and G.H. Lorimer. 1983. Ribulose-1,5-bisphosphate carboxylase-oxygenase.Ann. Rev. Biochem. 52: 507–535.

    Article  PubMed  CAS  Google Scholar 

  • Morin, F., M. Andre and T. Betsche. 1992. Growth kinetics, carbohydrate and leaf phosphate content of clover(Trifolium subterraneum L.) after transfer to a high CO2 atmosphere or to high light and ambient air. CO2 and ribulose bisphosphate concentrations by rubisco activase.Plant Physiol. 99: 89–95.

    Article  PubMed  CAS  Google Scholar 

  • Perchorowicz, J.T., D.A. Raynes and R.G. Jensen. 1981. Light limitation of photosynthesis and activation of ribulose bisphosphate carboxylase in wheat seedings.Proc. Natl. Acad. Sci. USA 78: 2985–2989.

    Article  PubMed  CAS  Google Scholar 

  • Portis, A.R. Jr. 1990. Rubisco activase.Biochim. Biophys. Acta 1015: 15–28.

    Article  PubMed  CAS  Google Scholar 

  • Portis, A.R. Jr. 1992, Regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase activity.Annu. Rev. Plant Physiol. Plant Mol. Biol. 43: 415–437.

    Article  CAS  Google Scholar 

  • Portis, A.R. Jr.,M.E. Salvucci and W.L. Ogren. 1986 Activation of ribulose bisphosphate carboxylase/oxygenase at physiological CO2 and ribulose bisphosphale concentrations by Rubisco activase.Plant Physiol. 82: 967–971.

    Article  PubMed  CAS  Google Scholar 

  • Robinson, S.P. and A.R. Portis, Jr. 1989a. Adenosine triphosphate hydrolysis by purified rubisco activase.Arch. Biochem. Biophys. 268: 93–99.

    Article  PubMed  CAS  Google Scholar 

  • Robinson, S.P. and A.R. Portis, Jr. 1989b. Ribulose-1,5-bisphosphate carboxylase/oxygenase activase protein prevents thein vitro decline in activity of ribulose-1,5-bisphosphate carboxylase/oxygenase.Plant Physiol. 90: 968–971.

    Article  PubMed  CAS  Google Scholar 

  • Robinson, S.P., V.J. Streusand, J.M. Chatrield and A.R. Portis, Jr. 1988. Purification and assay of rubisco activase from leaves.Plant Physiol. 88: 1008–1014.

    Article  PubMed  CAS  Google Scholar 

  • Roh, K.S., J.K. Kim, S.D. Song, H.S. Chung and J.S. Song. 1996. Decrease of the activation and carbamylation of rubisco by high CO2 in kidney bean.Korean J. Biotechnol. Bioeng. 11: 295–302.

    Google Scholar 

  • Salvucci, M.E. 1989. Regulation of rubisco activityin vivo.Physiol. Plant 77: 164–171.

    Article  CAS  Google Scholar 

  • Salvucci, M.E. 1992. Subunit infractions of rubisco activase: Polyethylene glycol promotes self-association, stimulates ATPase and activation activities, and enhances interactions with rubisco.Arch. Biochem. Biophy. 298: 688–696.

    Article  CAS  Google Scholar 

  • Salvucci, M.E., A.R. Portis, Jr.and W.L. Ogren. 1985 A soluble chloroplast protein catalyzes ribulose-bisphosphate carboxylase/oxygenase activationin vivo.Photosynth. Res. 7: 191–203.

    Article  Google Scholar 

  • Salvucci, M.E., J.M. Werneke, W.L. Ogren and A.R. Portis, Jr. 1987. Purification of species distribution of rubisco activase.Plant Physiol. 84: 930–936.

    Article  PubMed  CAS  Google Scholar 

  • Somerville, C.R., A.R. Portis, Jr.and W.L. Ogren. 1982. A mutant ofArabidopsis thaliana which lacks activation of RuBP carboxylasein vivo.Plant Physiol. 70:381–387.

    Article  PubMed  CAS  Google Scholar 

  • Stitt, M. 1991. Rising CO2 levels and their potential significance for carbon flow in photosynthetic cells.Plant Cell Environ. 14: 741–762.

    Article  CAS  Google Scholar 

  • Streusand, V.J. and A.R. Portis, Jr. 1987 Rubisco activase mediates ATP-dependent activation of ribulose bisphosphate carboxylase.Plant Physiol. 85: 152–154.

    Article  PubMed  CAS  Google Scholar 

  • Vu, C.V., L.H. Allen, Jr.and G. Bowes. 1983. Effect of light and elevated atmosperic CO2 on the ribulose bisphosphate carboxylase activity and ribulose bisphosphate level soybean leavesPlant Physiol. 73: 729–734.

    Article  PubMed  CAS  Google Scholar 

  • Wang, Z.V., G.W. Snyder, B.D. Esau, A.R. Portis, Jr.and W.L. Ogren. 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.

    Article  PubMed  CAS  Google Scholar 

  • Wang, Z.V. and A.R. Portis, Jr. 1991. A fluorometric study with 1-anilinonaphthalene-8-sulfonie acid (ANS) of the interactions of ATP and ADP with rubisco activase.Biochim. Biophys. Acta 1079: 263–267.

    PubMed  CAS  Google Scholar 

  • Wang, Z.V. and A.R. Portis, 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.

    Article  PubMed  CAS  Google Scholar 

  • Woodrow, I.W. 1994. Control of steady-state photosynthesis in sunflowers growing in enhanced CO2.Plant Cell Environ. 17: 277–286.

    Article  Google Scholar 

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Authors and Affiliations

  1. Department of Biology, Keimyung University, 704-701, Taegu, Korea

    Kwang Soo Roh & In Seob Kim

  2. Department of Clinical Pathology, Kimchun College, 740-200, Kimchun, Korea

    Byung Weon Kim

  3. Department of Biology, Andong National University, 760-749, Andong, Korea

    Jong Suk Song

  4. Department of Biology, Kyungpook National University, 702-701, Taegu, Korea

    Hwa Sook Chung

  5. Department of Biological Education, Kyungpook National University, 702-701, Taegu, Korea

    Seung Dal Song

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  1. Kwang Soo Roh
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  2. In Seob Kim
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  3. Byung Weon Kim
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  4. Jong Suk Song
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  5. Hwa Sook Chung
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  6. Seung Dal Song
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Roh, K.S., Kim, I.S., Kim, B.W. et al. Decrease in carbamylation of rubisco by high CO2 concentration is due to decrease of rubisco activase in kidney bean. J. Plant Biol. 40, 73–79 (1997). https://doi.org/10.1007/BF03030237

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  • DOI: https://doi.org/10.1007/BF03030237

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