Abstract
A protein with molecular mass of 67 kilodaltons is immunoprecipitated from in vitro translated products obtained from rabbit reticulocyte lysate primed with polyadenylated RNA from nitrate treated illuminated pea seedlings. This protein resembles the native nitrite reductase because of its competitive elimination when immunoprecipitation of in vitro translated products was carried out in the presence of cold unlabeled nitrite reductase or in vivo labeled pea leaf extract. This protein is of slightly higher molecular weight than that of the native nitrite reductase. Proteinaceous extracts from chloroplasts convert the in vitro product to the same molecular weight as the native peptide. The conversion appears to occur in two steps. Polyadenylated RNA from nitrate deficient plants or from nitrate-treated plants transferred to darkness do not support the synthesis of nitrite reductase. It is concluded that nitrate and light modulate the synthesis of the enzyme nitrite reductase by regulating the availability of mRNA for the enzyme.