Reduced cytosolic fructose-1,6-bisphosphatase activity leads to loss of O2 sensitivity in a Flaveria linearis mutant

• Published in: Plant physiology (Bethesda) 1988-03, Vol.86 (3), p.667-671
• Main Authors: Sharkey, T.D, Kobza, J, Seemann, J.R, Brown, R.H
• Format: Article
• Language: English
• Subjects: ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; Biological and medical sciences; Chloroplasts; Classical genetics, quantitative genetics, hybrids; COMPOSITAE; Enzyme activity; Enzymes; ENZYMIC ACTIVITY; Fundamental and applied biological sciences. Psychology; Genetics of eukaryotes. Biological and molecular evolution; Leaves; Low temperature; MUTANT; MUTANTES; MUTANTS; OXIGENO; OXYGEN; OXYGENE; Phosphates; Photosynthesis; Plants; Pteridophyta, spermatophyta; RESPIRACION; RESPIRATION; Spinach; Starches; Vegetals
• ISSN: 0032-0889; 1532-2548
• DOI: 10.1104/pp.86.3.667

The mutant plant of Flaveria linearis characterized by Brown et al. (Plant Physiol. 81: 212-215) was studied to determine the cause of the reduced sensitivity to O2. Analysis of CO2 assimilation metabolites of freeze clamped leaves revealed that both 3-phosphoglycerate and ribulose 1,5-bisphosphate were high in the mutant plant relative to F. linearis with normal O2 sensitivity. The kcat of ribulose-1,5-bisphosphate carboxylase (RuBPCase) was equal in all plant material tested (range 18-22 s-1) indicating that no tight binding inhibitor was present. The degree of RuBPCase carbamylation was reduced in the mutant plant relative to the wild-type plant. Since 3-phosphoglycerate was high in the mutant plant and photosynthesis did not exhibit properties associated with RuBPCase limitations, we believe that the decarbamylation of RuBPCase was a consequence of another lesion in photosynthesis. Fructose 1,6-bisphosphate and its precursors, such as the triose phosphates, were in high concentration in the mutant plant relative to the wild type. The concentrations of the product of the fructose 1,6-bisphosphatase reaction, fructose 6-phosphate, and its isomer, glucose 6-phosphate, were the same in both plants. We found that the mutant plant had up to 75% less cytosolic fructose 1,6-bisphosphatase activity than the wild type but comparable levels of stromal fructose 1,6-bisphosphatase. We conclude that the reduced fructose-1,6-bisphosphatase activity restricts the mutant plant's capacity for sucrose synthesis and this leads to reduced or reversed O2 sensitivity.