Differential expression of a gene for a methionine-rich storage protein in maize |
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Authors: | Julie Anderson Kirihara John P. Hunsperger Walter C. Mahoney Joachim W. Messing |
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Affiliation: | (1) Waksman Institute, Rutgers, The State University, 08855 Piscataway, NJ, USA;(2) Department of Genetics and Cell Biology, University of Minnesota, 55108 St. Paul, MN, USA;(3) Present address: Kallestad, A Division of Erbamont, 1000 Lake Hazeltine Dr., 55318 Chaska, MN, USA |
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Abstract: | Summary A methionine-rich 10 kDa zein storage protein from maize was isolated and the sequence of the N-terminal 30 amino acids was determined. Based on the amino acid sequence, two mixed oligonucleotides were synthesized and used to probe a maize endosperm cDNA library. A fulllength cDNA clone encoding the 10 kDa zein was isolated by this procedure. The nucleotide sequence of the cDNA clone predicts a polypeptide of 129 amino acids, preceded by a signal peptide of 21 amino acids. The predicted polypeptide is unique in its extremely high content of methionine (22.5%). The maize inbred line BSSS-53, which has increased seed methionine due to overproduction of this protein, was compared to W23, a standard inbred line. Northern blot analysis showed that the relative RNA levels for the 10 kDa zein were enhanced in developing seeds of BSSS-53, providing a molecular basis for the overproduction of the protein. Southern blot analysis indicated that there are one or two 10 kDa zein genes in the maize genome. |
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Keywords: | Zein Zea mays Gene expression Seed development High methionine protein |
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