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Articles

Photorespiration-Induced Reduction of Ribulose Bisphosphate Carboxylase Activation Level ¹

Department of Agronomy, University of Illinois, Urbana, Illinois 61801, Agricultural Research Service, United States Department of Agriculture, Urbana, Illinois 61801

Leaf photosynthesis and ribulose bisphosphate carboxylase activation level were inhibited in several mutants of the C₃ crucifer Arabidopsis thaliana which possess lesions in the photorespiratory pathway. This inhibition occurred when leaves were illuminated under a photorespiratory atmosphere (50% O₂, 350 microliters per liter CO₂, balance N₂), but not in nonphotorespiratory conditions (2% O₂, 350 microliters per liter CO₂, balance N₂). Inhibition of carboxylase activation level was observed in strains with deficient glycine decarboxylase, serine transhydroxymethylase, serine-glyoxylate aminotransferase, glutamate synthase, and chloroplast dicarboxylate transport activities, but inhibition did not occur in a glycolate-P phosphatase-deficient strain. Also, the photorespiration inhibitor aminoacetonitrile produced a decline in leaf and protoplast ribulose bisphosphate carboxylase activation level, but was without effect on intact chloroplasts. Fructose bisphosphatase, a light-activated enzyme which is strongly dependent on stromal pH and Mg²⁺ for regulation, was unaffected by conditions which caused inhibition of ribulose bisphosphate carboxylase. Thus, the mechanism of inhibition does not appear to involve changes in stromal Mg²⁺ and pH but rather is associated with metabolite flux through the photorespiratory pathway.

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