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Linkage of the alcohol dehydrogenase structural genes in pearl millet (Pennisetum typhoides)
Authors:Flora Banuett-Bourrillon
Affiliation:(1) Department of Biology, University of Oregon, 97403 Eugene, Oregon;(2) Present address: Department of Biochemistry and Biophysics, School of Medicine, University of California, 94143 San Francisco, California
Abstract:Pearl millet produces three ADH isozymes, Sets I, II, and III. Naturally occurring ADH electrophoretic variants affecting Sets I and II isozymes but not III have been previously described. Analysis of such variants led to the identification of the Adh1 structural gene. The existence of a second Adh structural gene was inferred from dissociation-reassociation studies of Set II. In the present report, a naturally occurring variant affecting the electrophoretic mobility of Sets III and II but not Set I is described. Analysis of this variant confirms the existence of a second structural gene, Adh2. Crosses utilizing this Adh2 marker reveal a dissimilarity with maize and other plants such as sunflower and narrow-leafed lupins. Adh1 and Adh2 of pearl millet do not segregate independently; indeed, no recombinants have been observed. This is the first major difference encountered in an otherwise remarkably similar genetic and environmental control of the ADH isozymes in maize and millet. The organization of the Adh genes of pearl millet may reflect a more primitive arrangement than that of maize.This work was supported by a PHS National Research Service Award Training Grant in Genetics to the Biology Department of the University of Oregon.
Keywords:alcohol dehydrogenase  isozymes  pearl millet  genetic linkage
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