Screening and characterization of a rice mutant lacking phospholipase D in mature seeds.

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Deterioration of rice grains during the storage is a serious problem which reduces the quality of stored grains, and the degradation of lipids is responsible for these changes during the storage. Phospholipase D (PLD) which catalyses the terminal phosphodiester bonds in various diester glycerophospholipids. In rice bran, PLD would be responsible for the hydrolysis of spherosome (oil body) membrane phospholipids, which causes triacylglycerol leakage out of spherosomes and subsequent degradation. Using anti-PLD antibody, we screened a rice mutant "03-sl08" lacking PLD in mature seeds. Furthermore, the specific activity of "03-s108" was very low, less than one % of that of Nipponbare. The mode of inheritance of PLD-null character was analyzed by crossing "03-s108" with a normal PLD activity "Koshihikari". The distribution of F2 phenotypes for the presence or absence of PLD from selfed Fl plants was 3:1, supporting the hypothesis that the absence of PLD is recessive to the presence of PLD. Thus, we isolated a rice mutant "03-s108" lacking PLD in mature seeds. This mutant "03-s108" should be useful in breeding programs designed to produce rice of a high storability and in understanding physiologic and genetic mechanisms of lipids metabolism in bran fractions.