Plant Physiology 80:655-659 (1986)
© 1986 American Society of Plant Biologists
Articles
Light and CO2 Response of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Activation in Arabidopsis Leaves
Michael E. Salvucci1,
Archie R. Portis, Jr. and
William L. Ogren
United States Department of Agriculture, Agricultural Research Service, Urbana, Illinois 61801
The requirements for activation of ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) were investigated in leaves of Arabidopsis wild-type and a mutant incapable of light activating rubisco in vivo. Upon illumination with saturating light intensities, the activation state of rubisco increased 2-fold in the wild-type and decreased in the mutant. Activation of fructose 1,6-bisphosphate phosphatase was unaffected by the mutation. Under low light, rubisco deactivated in both the wild-type and the mutant. Deactivation of rubisco in the mutant under high and low light led to the accumulation of high concentrations of ribulose 1,5-bisphosphate. Inhibiting photosynthesis with methyl viologen prevented ribulose 1,5-bisphosphate accumulation but was ineffective in restoring rubisco activation to the mutant. Net photosynthesis and the rubisco activation level were closely correlated and saturated at a lower light intensity in the mutant than in wild-type. At CO2 concentrations between 100 and 2000 microliters per liter, the activation state was a function of the CO2 concentration in the dark but was independent of CO2 concentration in the light. High CO2 concentration (1%) suppressed activation in the wild-type and deactivation in the mutant. These results support the concept that rubisco activation in vivo is not a spontaneous process but is catalyzed by a specific protein. The absence of this protein, rubisco activase, is responsible for the altered characteristics of rubisco activation in the mutant.
1 Present address: USDA-ARS, Agronomy Department, University of Kentucky, N222, ASC-N, Lexington, KY 40546.
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