Abstract
The Adh1-C mallele and each gene in the Adh1-FC mduplication have been cloned and restriction-mapped. Of the C mallele 6 kb was sequenced. A single amino acid substitution of aspartate for tyrosine at residue 52 accounts for the altered enzymatic properties of the C mprotein. Comparison of the nucleotide sequence to that of Adh1-1F and Adh1-1S shows structural and restriction site polymorphisms in the 3′ flanking DNA. C mlacks the insertion sequence present in 1F and 1S and contains a complex sequence composed of two direct repeats and an inverted repeat. The two genes of the duplication allele have similar restriction maps to C mand each other.
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Osterman, J.C., Dennis, E.S. Molecular analysis of the ADH1-C m allele of maize. Plant Mol Biol 13, 203–212 (1989). https://doi.org/10.1007/BF00016138
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DOI: https://doi.org/10.1007/BF00016138