Abstract
The prolamin proteins of maize and its close relatives, sorghum and Coix, share common structural features. These proteins are classified as α-, β-, γ- and δ-types, based on structural homology and solubility characteristics. Each of these proteins has a distinct spatial distribution within the protein bodies, which form as accretions within the lumen of the rough endoplasmic reticulum. There is increasing evidence that several of these proteins, notably the β- and γ-zeins, play important roles in initiating and organizing the protein body. These prolamins are devoid of lysine and tryptophan, two essential amino acids for monogastric animals. Since prolamins account for approximately 70% of the seed protein, these grains are of inferior quality for human and livestock nutrition. Interest in improving the protein quality of these cereals led to the identification of several maize mutants that alter the pattern of prolamin synthesis. One of these, opaque2, corresponds to a defective transcription factor that regulates α-zein gene expression, while another, floury2, is a mutant α-zein protein. Both mutations can cause pleiotropic effects that increase the lysine content of the seed, and hence the protein quality of the grain. Another mutant, opaque15, alters the synthesis of the γ-zein protein. This reduces the number of protein bodies that form, which appears to have a major effect of the texture of the grain. By over-producing γ-zein in an opaque2 mutant, plant breeders have produced a new type of corn, “Quality Protein Maize”, which has excellent protein quality.
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Coleman, C.E., Dannenhoffer, J.M., Larkins, B.A. (1997). The Prolamin Proteins of Maize, Sorghum and Coix . In: Larkins, B.A., Vasil, I.K. (eds) Cellular and Molecular Biology of Plant Seed Development. Advances in Cellular and Molecular Biology of Plants, vol 4. Springer, Dordrecht. https://doi.org/10.1007/978-94-015-8909-3_7
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