Synthesis of ribulose bisphosphate carboxylase in greening pea leaves

Coordination of mRNA level of two subunits


Correspondence to Y. Sasaki, Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Sakyo-ku, Kyoto-shi, Kyoto-fu, Japan 606


Ribulose bisphosphate carboxylase/oxygenase, with its large subunit encoded in the chloroplast and the small subunit in the nucleus, is induced by light. Accumulation of the enzyme, its two mRNA levels, and the synthesis rate of enzyme protein in pea leaves were followed during induction to understand the role of mRNA levels during greening subunit synthesis. The relative mRNA levels for the large and the small subunits increased coordinately up to 3–4 days, which almost corresponded to an inflection point of the accumulation profile of RuBisCO, and then the two mRNA levels gradually decreased. To obtain information of subunit synthesis, the extent of labelling of the two subunits were determined for both assembled and unassembled subunits using specific IgG. Unassembled subunits were found for both polypeptides, with a slight excess of the small one. The observed synthesis rates of the small and the large subunits were roughly coordinated without overproduction and almost stoichiometric amounts of the two polypeptides were found. The profiles of observed synthesis rate of the two subunits and the holoenzyme were similar to those of their mRNA levels. These results suggest that the synthesis of ribulose bisphosphate carboxylase/oxygenase protein and its accumulation are dependent on the coordinated change of the two mRNA levels in greening pea leaves.


ribulosebisphosphate carboxylase/oxygenase


sodium dodecyl sulfate


0.15 M sodium chloride, 0.015 M sodium citrate buffer, pH 7.0


Ribulosebisphosphate carboxylase/oxygenase (EC