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First published online February 21, 2003; 10.1105/tpc.007575

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The Plant Cell, Vol. 15, 666-680, March 2003, Copyright © 2003,
American Society of Plant Biologists

Mutational Analysis of the Pullulanase-Type Debranching Enzyme of Maize Indicates Multiple Functions in Starch Metabolism

Jason R. Dinges, Christophe Colleoni, Martha G. James and Alan M. Myers1

Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011

1 To whom correspondence should be addressed. E-mail ammyers{at}iastate.edu; fax 515-294-0453

Plants contain two types of {alpha}(1->6) glucan hydrolase (starch-debranching enzyme [DBE]). Mutations that affect the pullulanase-type DBE have not been described, although defects in isoamylase-type DBE, known in many plant species, indicate a function in starch biosynthesis. We describe a null mutation of a pullulanase-type DBE gene, a Mutator insertion in maize Zpu1. Plants homozygous for the zpu1-204 mutation are impaired in transient and storage starch degradation. Thus, hydrolytic activity of pullulanase-type DBE contributes to starch catabolism. Developing zpu1-204 endosperm accumulates branched maltooligosaccharides not found in the wild type and is deficient in linear maltooligosaccharides, indicating that the pullulanase-type DBE functions in glucan hydrolysis during kernel starch formation. Furthermore, in a background deficient in isoamylase-type DBE, zpu1-204 conditions a significant accumulation of phytoglycogen in the kernel that is not seen in the wild type. Therefore, pullulanase-type DBE partially compensates for the defect in isoamylase-type DBE, suggesting a function during starch synthesis as well as degradation.




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