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Plant Physiology 87:558-561 (1988)
© 1988 American Society of Plant Biologists

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Metabolism and Enzymology

Regulation of Ribulose-1,5-Bisphosphate Carboxylase Activity by the Activase System in Lysed Spinach Chloroplasts

Martin A. J. Parry, Alfred J. Keys, Christine H. Foyer, Robert T. Furbank1 and David A. Walker

AFRC Institute of Arable Crops Research, Rothamsted Experimental Station, Harpenden, Hertfordshire, United Kingdom, AL5 2JQ, Research Institute for Photosynthesis, University of Sheffield, Sheffield, United Kingdom, S10 2TN

Ribulose-1,5-bisphosphate (RuBP) carboxylase in lysed spinach (Spinacia oleracea L. cv virtuosa) chloroplasts that had been partly inactivated at low CO2 and Mg2+ by incubating in darkness with 4 millimolar partially purified RuBP was reactivated by light. If purified RuBP was used to inhibit dark activation of the enzyme, reactivation by light was not observed unless fructose-1,6-bisphosphate, ATP, or ADP plus inorganic phosphate were also added. Presumably, ADP plus inorganic phosphate acted as an ATP-generating system with a requirement for the generation of {Delta}pH across the thylakoid membrane. When the RuBP obtained from Sigma Chemical Co. was used, light did not reactivate the enzyme. There was no direct correlation between {Delta}pH and activation. Therefore, thylakoids are required in the ribulose-1,5-bisphosphate carboxylase activase system largely to synthesize ATP. Inactivation of RuBP carboxylase in isolated chloroplasts or in the lysed chloroplast system was not promoted simply by a transition from light to dark conditions but was caused by low CO2 and Mg2+.

1 Present address: CSIRO, Division of Plant Industry, P. O. Box 1600, Canberra 2601 ACT, Australia.




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Copyright © 1988 by the American Society of Plant Biologists