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Expression of a mutant alpha-zein creates the floury2 phenotype in transgenic maize

Coleman, C.E., Clore, A.M., Ranch, J.P., Higgins, R., Lopes, M.A., Larkins, B.A.
Proceedings of the National Academy of Sciences of the United States of America 1997 v.94 no.13 pp. 7094-7097
genetic transformation, gene transfer, Zea mays, phenotype, structural genes, transgenic plants, mutation, binding proteins, endosperm, mutants, zein, immunocytochemistry, endoplasmic reticulum
The maize floury2 mutation results in the formation of a soft, starchy endosperm with a reduced amount of prolamin (zein) proteins and twice the lysine content of the wild type. The mutation is semidominant and is associated with small, irregularly shaped protein bodies, elevated levels of a 70-kDa chaperone in the endoplasmic reticulum, and a novel 24-kDa polypeptide in the zein fraction. The 24-kDa polypeptide is a precursor of a 22-kDa alpha-zein protein that is not properly processed. The defect is due to an alanine-to-valine substitution at the C-terminal position of the signal peptide, which causes the protein to be anchored to the endoplasmic reticulum. We postulated that the phenotype associated with the floury2 mutation is caused by the accumulation of the 24-kDa alpha-zein protein. To test this hypothesis, we created transgenic maize plants that produce the mutant protein. We found that endosperm in seeds of these plants manifests the floury2 phenotype, thereby confirming that the mutant alpha-zein is the molecular basis of this mutation.