Abstract
Nitrate reductase activity was induced by nitrate in green corn (Zea mays) leaves in either light or darkness. The induction process required oxygen in darkness but not in light. A light treatment was required before the enzyme could be induced in etiolated leaves.The capacity for nitrate reductase induction by nitrate was positively correlated with the level of cytoplasmic polyribosomes under a variety of experimental conditions. (a) Light-grown leaves contained high levels of polyribosomes (84% of the total population, most of which were of the 80 S type); similarly high levels of nitrate reductase activity were induced. (b) The level of polyribosomes and the ability to form nitrate reductase activity rapidly decreased in light-grown leaves following transfer to an anaerobic environment in the dark; both parameters were maintained at a high level when light-grown leaves were kept in the light under anaerobic conditions. (c) The ability of light-grown leaves, previously placed in darkness under nitrogen to dissociate polyribosomes to monoribosomes, to form nitrate reductase activity again correlated with the level of reformed polyribosomes following transfer of the leaves back to light. (d) Etiolated leaves contained a low level of cytoplasmic polyribosomes (27%), and nitrate reductase activity was induced following exposure to light only after a lag of 2 to 4 hours. During this lag period there was a marked increase in the level of polyribosomes.The ability of leaves to form nitrate reductase activity and the level of polyribosomes also correlated with the level of in vitro incorporation of amino acids into protein by the isolated ribosome preparations. Thus, the apparent requirement of light for nitrate reductase induction in etiolated leaves seems not to be specific. Rather an influence of light upon the development of an active protein-synthesizing apparatus as evidenced by the state of polyribosomes is indicated.The results also show that energy from photosynthetic phosphorylation can be used to maintain cytoplasmic polyribosomes (and thus to drive cytoplasmic protein synthesis), at least under anaerobic conditions.
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