Regulation of the Synthesis of Ribulose-l,5-bisphosphate Carboxylase and Its Subunits in the Flagellate Chlorogonium elongatum. II. Coordinated Synthesis of the Large and Small Subunits
نویسندگان
چکیده
Transfer of heterotrophically grown cells of the unicellular green alga Chlorogonium elongatum to autotrophic growth conditions causes a 10-15 fold increase in the amount of the chloroplastic enzyme ribulose-1,5-bisphosphate carboxylase. This increase was found to be due to de novo synthesis. The relative proportions of large and small subunits of the enzyme do not change. Their ratio is close to 3.4, the proportions in weight of the two subunits in the holoenzyme. Continous labelling with [35S]sulfate reveals that the ratios of incorporation into large and small subunits are essentially the same in autotrophic and heterotrophic cells. Pulse-chase experiments show that the subunits are degraded synchronously. The coordinated subunit synthesis cannot be uncoupled using inhibitors of protein and RNA synthesis or high temperature of cultivation of the alga. The results suggests a very tightly coordinated synthesis of the large and small subunits of ribulosebisphosphate carboxylase.
منابع مشابه
Synthesis and turnover of ribulose biphosphate carboxylase and of its subunits during the cell cycle of Chlamydomonas reinhardtii
The chloroplast enzyme ribulose-1,5-bisphosphate (Ru-1,5-P2) carboxylase (EC 4.1 1.39) is made up ot two nonidentical subunits, one synthesized in the chloroplast and the other outside. Both of these subunits of the assembled enzyme are synthesized in a stepwise manner during the synchronous cell cycle of the green alga Chlamydomonas reinhardtii. The activity of this enzyme increases in the lig...
متن کاملSynthesis and assembly of large subunits into ribulose bisphosphate carboxylase/oxygenase in chloroplast extracts.
We have developed a new system for the in vitro synthesis of large subunits and their assembly into ribulose bisphosphate carboxylase oxygenase (Rubisco) holoenzyme in extracts of higher plant chloroplasts. This differs from previously described Rubisco assembly systems because the translation of the large subunits occurs in chloroplast extracts as opposed to isolated intact chloroplasts, and t...
متن کاملLight Effects on the Synthesis of Ribulose-1,5-Bisphosphate Carboxylase in Lemna gibba L. G-3.
Placing light-grown Lemna gibba L. G-3 into the dark results in a changed pattern of protein synthesis. Although the amount of protein in the tissue and the over-all rate of incorporation of [(35)S]methionine into protein does not significantly decline during four days of darkness, the rate of synthesis of three polypeptides declines dramatically. One of these polypeptides is the chlorophyll a/...
متن کاملSynthesis of the Small Subunit of Ribulose-1,5-bisphosphate Carboxylase by Soluble Fraction Polyribosomes of Pea Leaves.
The products of amino acid incorporation by pea (Pisum sativum L.) leaf soluble fraction polyribosomes in the wheat germ system were examined by two-dimensional electrophoresis and fluorography.There are two isoelectric variants of the small subunit of ribulose bisphosphate carboxylase in this organism, and the more alkaline of these is consistently labeled in the cell-free protein-synthesizing...
متن کاملTranscriptional and post-transcriptional regulation of ribulose 1,5-bisphosphate carboxylase gene expression in light- and dark-grown amaranth cotyledons.
The regulation of expression of the genes encoding the large subunit (LSU) and small subunit (SSU) of ribulose 1,5-bisphosphate carboxylase (RuBPCase) was examined in 1- through 8-day-old, dark-grown (etiolated) and light-grown amaranth cotyledons. RuBPCase specific activity in light-grown cotyledons increased during this 8-day period to a level 15-fold higher than in dark-grown cotyledons. Und...
متن کامل