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Metabolism and Enzymology

A Starch Deficient Mutant of Arabidopsis thaliana with Low ADPglucose Pyrophosphorylase Activity Lacks One of the Two Subunits of the Enzyme ¹

Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824, DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824

A starch deficient mutant of Arabidopsis thaliana (L.) Heynh. has been isolated in which leaf extracts contain only about 5% as much activity of ADPglucose pyrophosphorylase (EC 2.7.7.27) as the wild type. A single, nuclear mutation at a previously undescribed locus designated adg2 is responsible for the mutant phenotype. Although the mutant contained only 5% as much ADPglucose pyrophosphorylase activity as the wild type, it accumulated 40% as much starch when grown in a 12 hour photoperiod. The mutant also contained about 40% as much starch as the wild type when grown in continuous light, suggesting that the rate of synthesis regulates its steady state accumulation. Immunological analysis of leaf extracts using antibodies against the spinach 54 and 51 kilodalton (kD) ADPglucose pyrophosphorylase subunits indicated that the mutant is deficient in a cross-reactive 54 kD polypeptide and has only about 4% as much as the wild type of a cross-reactive 51 kD polypeptide. This result and genetic studies suggested that adg2 is a structural gene which codes for the 54 kD polypeptide, and provides the first functional evidence that the 54 kD polypeptide is a required component of the native ADPglucose pyrophosphorylase enzyme.

³ Present address: USDA Plant Gene Expression Center; 800 Buchanan Street; Albany, CA 94710.

¹ This work was supported in part by grants from the U.S. Department of Energy (DE-AC02-76ER01338) and the U.S. Department of Agriculture (86-CRCR-1-2046) to C. S., the National Science Foundation (DMB86-10319) to J. P., and the McKnight Foundation. T. C. was the recipient of a National Science Foundation Graduate Fellowship.

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