Purification and translation of zein messenger RNA from maize endosperm protein bodies.
The messenger RNAs coding for the zein storage protein have been purified from other contaminating RNAs. The average molecular lengths are 1.1-1.2 kilobases, as determined by polyacrylamide gel electrophoresis and by electron microscopy. Products of messenger-dependent protein synthesis in vitro appear to be 1100 and 2000 daltons heavier than the native polypeptides. Zein is like secretory proteins in having a precursor with an additional amino-terminal sequence. Although only one mRNA is seen in polyacrylamide gel electrophoresis, the combined size of the polypeptide products formed exceeds the coding capacity for one message of the size determined in this study. This suggests that there are at least two mRNAs of similar sizes for the zein polypeptides rather than one dicistronic message.