Abstract
In higher plants subjected to anaerobic conditions due to flooding, alcoholic fermentation is essential for the supply of NAD+ to the glycolytic pathway. Matsumura et al. (1995) previously isolated a reduced ADH activity (rad) mutant in rice. ADH1 mRNA levels were comparable between the rad mutant and the wild type, but the amount of ADH1 protein was less in the rad mutant than in the wild type. The 106th nucleotide from the initiation codon in the wild type (G) was changed to A in the rad mutant, resulting in a change of the 36th residue of the deduced amino acid sequence from glutamate (E) to lysine (K). Thus, the E-to-K substitution in the rad mutant may affect the translation or stability of ADH1 protein.