Light-induced de Novo Synthesis of Ribulose 1,5-Diphosphate Carboxylase in Greening Leaves of Barley.
نویسندگان
چکیده
An antibody specific for ribulose 1,5-diphosphate carboxylase was used to isolate the enzyme from greening barley (Hordeum vulgare L.) leaves. The increase in enzymatic activity during greening was due to de novo synthesis of the enzyme. Increases in enzymatic activity were accompanied by corresponding increases in enzyme protein and by incorporation of radioactive leucine, all of which were inhibited by low concentrations of cycloheximide. (14)C-Labeled amino acids were incorporated into the enzyme by covalent peptide bonding.
منابع مشابه
Evidence for in vivo Light-induced Synthesis of Ribulose-1,5-diP Carboxylase and Phosphoribulokinase in Greening Barley Leaves.
WHEN ACTINOMYCIN D, PUROMYCIN, STREPTOMYCIN, CHLORAMPHENICOL, AND CYCLOHEXIMIDE, KNOWN INHIBITORS OF PROTEIN SYNTHESIS, WERE APPLIED TO LEAVES OF INTACT SEEDLINGS OR DETACHED LEAVES OF BARLEY PRIOR TO THEIR GREENING, THE SAME GENERAL RESPONSE RESULTED: the light-induced increase in activity of ribulose 1,5-diphosphate carboxylase was prevented while that of phosphoribulokinase was only partiall...
متن کاملThe Formation of Ribulose Diphosphate Carboxylase Protein during Chloroplast Development in Barley.
Ribulose 1,5-diphosphate carboxylase is synthesized in barley leaves growing in the dark. Upon illumination there is a marked increase in the rate of synthesis of the enzyme. The specific activity of the enzyme expressed as cpm incorporated into phosphoglyceric acid per mug of fraction I protein, after isolation shows no change either during dark growth or greening. During early stages of illum...
متن کاملEvidence for lack of turnover of ribulose 1,5-diphosphate carboxylase in barley leaves.
Turnover of ribulose 1,5-diphosphate carboxylase in barley leaves (Hordeum vulgare L.) was followed over time in light and dark. The enzyme was degraded in prolonged darkness and was resynthesized after the plants were returned to light. Labeling with (14)C showed that simultaneous synthesis and degradation (turnover) did not occur in light. In contrast, the remaining soluble protein was turned...
متن کاملLoss of Ribulose 1,5-Diphosphate Carboxylase and Increase in Proteolytic Activity during Senescence of Detached Primary Barley Leaves.
Symptoms typical of senescence occurred in green detached primary barley (Hordeum vulgare L.) leaves placed in darkness and in light. Chlorophyll, total soluble protein, ribulose 1,5-diphosphate carboxylase protein and activity each progressively decreased in darkness and to a lesser extent in light. In all treatments most of the total soluble protein lost was accounted for by a decrease in rib...
متن کاملInfluence of age and illumination on distribution of several calvin cycle enzymes in greening barley leaves.
Activities of phosphoriboisomerase, phosphoribulokinase, and ribulose 1,5-diphosphate carboxylase, protein content, and chlorophyll accumulation in dark-grown barley seedlings were measured before and after illumination. Enzymatic activities, levels of soluble protein, and accumulation (upon illumination) of chlorophyll in leaves declined from tips toward the base. In response to increasing tim...
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ورودعنوان ژورنال:
- Plant physiology
دوره 46 3 شماره
صفحات -
تاریخ انتشار 1970