Abstract
During soybean (Glycine max) nodule development, induced ferritin mRNA concentration remains elevated while the protein concentration decreases 4- to 5-fold (M. Ragland and E.C. Theil [1993] Plant Mol Biol 21: 555-560). Investigation of posttranscriptional regulation of nodule ferritin during development showed that ferritin mRNA was efficiently translated based on polyribosome size in vivo, protein synthesis (0.8% of total protein) in vitro, and protein synthesis in intact nodules. Ferritin, a plastid protein, was processed in both immature and mature nodules. In chimeric mRNA, soybean ferritin mRNA sequences blocked the function of the iron regulatory element (IRE), the cis regulatory element of animal ferritin mRNA; the IRE regulates chimeric animal mRNAs. The absence of translational regulation of ferritin in plants contrasts with ferritin regulation in animals. Thus, ferritin regulation has diverged during evolution, whereas structure of the mature protein has been conserved. Ferritin in mature soybean nodules is apparently regulated after translation, possibly in analogy with such plastid proteins as chlorophyll-binding proteins D1, CP43, LHCI, and LHCII, the small subunit of ribulose-bisphosphate carboxylase, and apoplastocyanin. An autocatalytic mechanism observed in vivo for degradation of plastid protein D1 and in vitro for pea ferritin during iron release could explain the ferritin decreases in mature nodules.