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A soluble chloroplast protein catalyzes ribulosebisphosphate carboxylase/oxygenase activation in vivo

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Abstract

Ribulosebisphosphate carboxylase/oxygenase (EC 4.1.1.39) (rubisco) must be fully activated in order to catalyze the maximum rates of photosynthesis observed in plants. Activation of the isolated enzyme occurs spontaneously, but conditions required to observe full activation are inconsistent with those known to occur in illuminated chloroplasts. Genetic studies with a nutant of Arabidopsis thaliana incapable of activating rubisco linked two chloroplast polypeptides to the activation process in vivo. Using a reconstituted light activation system, it was possible to demonstrate the participation of a chloroplast protein in rubisco activation. These results indicate that a specific chloroplast enzyme, rubisco activase, catalyzes the activation of rubisco in vivo.

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References

  1. Bahr JT and Jensen RG (1978) Activation of ribulose bisphosphate carboxylase in intact chloroplasts by CO2 and light. Arch Biochem Biophys 185: 39–48

    Google Scholar 

  2. Chua N-H (1980) Electrophoretic analysis of chloroplast proteins. Meth Enzymol 69: 435–446

    Google Scholar 

  3. Covey SN and Taylor SC (1980) Rapid purification of ribulose 1,5-bis(phosphate) carboxylase from Rhodomicrobium vannielii. FEMS Microb Lett 8: 221–223

    Google Scholar 

  4. Duncan R and Hershey JWB (1984) Evaluation of isoelectric focusing running conditions during two-dimensional isoelectric focusing/sodium dodecylsulfate-polyacrylamide gel electrophoresis, variation of gel patterns with changing conditions and optimized isoelectric focusing conditions. Anal Biochem 138: 144–155

    Google Scholar 

  5. Farquhar GD, von Caemmerer S and Berry JA (1980) A biochemical model of photosynthetic CO2 assimilation in leaves of C3 plants. Planta 149: 78–90

    Google Scholar 

  6. Heber U, Takahama U, Neimanis S and Shimizu-Takahama M (1982) Transport as the basis of the Kok effect. Levels of some photosynthetic intermediates and activation of light-regulated enzymes during photosynthesis of chloroplasts and green leaf protoplasts. Biochim Biophys Acta 679: 289–299

    Google Scholar 

  7. Heldt HW and Sauer F (1971) The inner membrane of the chloroplast envelope as the site of specific metabolite transport. Biochim Biophys Acta 234: 83–91

    Google Scholar 

  8. Jordan DB and Chollet R (1983) Inhibition of ribulose bisphosphate carboxylase by substrate ribulose 1,5-bisphosphate. J Biol Chem 258: 13752–13758

    Google Scholar 

  9. Lorimer GH and Miziorko HM (1980) Carbamate formation on the ɛ-amino group of a lysyl residue as the basis for the activation of ribulosebisphosphate carboxylase by CO2 and Mg2+. Biochem 19: 5321–5328

    Google Scholar 

  10. Lorimer GH, Badger MR, Heldt HW (1983) The activation of ribulose 1,5-bisphosphate carboxylase/oxygenase. In: Photosynthetic Carbon Assimilation (Siegleman HW and Hind G eds) Plenum, New York, pp 283–306

    Google Scholar 

  11. Machler FM and Nosberger J (1980) Regulation of ribulose bisphosphate carboxylase activity in intact wheat leaves by light, CO2 and temperature. J Exp Bot 31: 1485–1491

    Google Scholar 

  12. Miziorko HM and Lorimer GH (1983) Ribulose 1,5-bisphosphate carboxylase/oxygenase. Annu Rev Biochem 52: 507–535

    Google Scholar 

  13. 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

    Google Scholar 

  14. Portis ARJr (1981) Evidence of a low stromal Mg2+ concentration in intact chloroplasts in the dark. I. Studies with the ionophore A23187. Plant Physiol 67: 985–989

    Google Scholar 

  15. Somerville CR and Ogren WL (1979) A phosphoglycolate phosphatesedeficient mutant of Arabidopsis. Nature 280: 833–836

    Google Scholar 

  16. Somerville CR, Portis AR and Ogren WL (1982) A mutant of Arabidopsis thaliana which lacks activation of RuBP carboxylase in vivo. Plant Physiol 70: 381–387

    Google Scholar 

  17. Somerville CR, Somerville SC and Ogren WL (1981) Isolation of photosynthetically active protoplasts and chloroplasts from Arabidopsis thaliana. Plant Sci Lett 21: 89–96

    Google Scholar 

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Authors and Affiliations

  1. Agricultural Research Service, United States Department of Agriculture, 1102 South Goodwin Avenue, 61801, Urbana, Illinois, USA

    Michael E. Salvucci, Archie R. Portis Jr. & William L. Ogren

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  1. Michael E. Salvucci
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  2. Archie R. Portis Jr.
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  3. William L. Ogren
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Salvucci, M.E., Portis, A.R. & Ogren, W.L. A soluble chloroplast protein catalyzes ribulosebisphosphate carboxylase/oxygenase activation in vivo. Photosynth Res 7, 193–201 (1985). https://doi.org/10.1007/BF00037012

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  • DOI: https://doi.org/10.1007/BF00037012

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