Abstract A low stringency screening of a wheat ( Triticum aestivum L.) genomic library produced three types of γ gliadin clones. The sequence of one clone, λ10–20, encoded a γ gliadin of 34.3 kDa. Comparisons of this protein with the proteins encoded by other γ gliadin DNA sequences revealed a general γ gliadin structure: a 19-residue signal peptide; 12-residue mature amino terminus; 12–16 copies of a proline- and glutamine-rich heptapeptide repeat; a 76-residue region high in glutamine containing most of the cyysteines and charged residues: a 6–16-residue polyglutamine region; and the 41-residue carboxyl terminus. Comparisons of the 5′ and 3′ flanking regions of several γ gliadins reveals the high homology and general structure of γ gliadin genes. A further comparison of the 5′ flanking regions with the 5′ flanking regions of other prolamin genes showed that γ gliadin genes contain three copies of a conserved sequence seen within approx. 600 b.p. upstream of the translation start sites of prolamin genes.