Evolution of the Genes Encoding Seed Storage Proteins in Sugarcane and Maize

Abstract

Prolamins, the seed storage proteins of maize, sorghum and coix were also found in sugarcane. Prolamins are grouped into structurally distinct classes termed the α-, β-, γ- and δ-prolamins. Orthologues for almost all of the α-, β-, γ- and δ-prolamins classes were identified in sugarcane. In maize, there are two molecular weight classes of α-prolamins, the 22 and 19 kD α-zeins. Sugarcane also possesses both the 22 kD and the 19 kD α-prolamins, which we denote as caneins, whereas sorghum and coix contain only the 22 kD α-prolamin (α-kafirin and α-coixin, respectively). Amino acid sequence alignments of the 22 and 19 kD α-prolamins from these plants revealed that both the 19 kD α-zein and the 19 kD α-canein lack around 20 amino acids at the sixth α-helix domain. We postulate that the 19 kD α-prolamins originated from a deletion of the sixth α-helix of a 22 kD counterpart in the saccharum lineage. Saccharum and sorghum diverged around five to nine million years ago (Mya), when only the 22 kD α-prolamins existed. The 19 kD α-canein must therefore have emerged after this time. Sorghum possesses a 19 kD α-prolamin similar to that of sugarcane and maize, but it contains the sixth α-helix domain lacking in the 19 kD α-zein and the 19 kD α-canein. This sorghum α-prolamin that we called 19 kD-like α-kafirin must be the ancestor of the 19 kD α-canein. The 19 kD-like α-kafirin could also be the ancestor of the 19 kD α-zein but it is also possible that the genes encoding the 19 kD α-zein and the 19 kD α-canein have evolved separately in these close groups.