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Primary Structure of a Proline-Rich Zein and Its cDNA

Department of Biology, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061

Eighty-five cDNA clones for -zein (proline-rich zein) from a cDNA expression library were isolated using specific antibody and cDNA probes. Nucleotide sequences of seven independent clones were determined and found to be identical in regions where they overlapped. The primary structure of the mature protein, determined from the sequence of one near full-length clone, consists of 204 amino acids. It has a molecular weight of 21,824 daltons, about 5 kilodaltons less than that estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The N-terminal one-half of the sequence contained eight essentially identical tandem repeats of the hexapeptide Pro-Pro-Pro-Val-His-Leu and two of the octapeptide Gln-Pro-His-Pro-Cys-Pro-Cys-Gln. The codon specifying the third proline in the hexapeptide repeating units is identical (CCG) in all of the eight repeats. The coding region has a very high G-C content (69.8%). The multiple charge components of -zein detected by isoelectric focusing do not seem to be encoded by members of a multigene family. Moreover, it was found that the codon preference in -zein is, in fact, the base preference in the wobble position. A codon usage value was devised to express this phenomenon.