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Purification and Molecular Genetic Characterization of ZPU1, a Pullulanase-Type Starch-Debranching Enzyme from Maize1

Mary K. Beatty2, 3, Afroza Rahman2, Heping Cao, Wendy Woodman, Michael Lee, Alan M. Myers, and Martha G. James*

Department of Biochemistry, Biophysics, and Molecular Biology (M.K.B., A.R., H.C., A.M.M., M.G.J.), and Department of Agronomy (W.W., M.L.), Iowa State University, Ames, Iowa 50011

This study identified and purified specific isoamylase- and pullulanase-type starch-debranching enzymes (DBEs) present in developing maize (Zea mays L.) endosperm. The cDNA clone Zpu1 was isolated based on its homology with a rice (Oryza sativa L.) cDNA coding for a pullulanase-type DBE. Comparison of the protein product, ZPU1, with 18 other DBEs identified motifs common to both isoamylase- and pullulanase-type enzymes, as well as class-specific sequence blocks. Hybridization of Zpu1 to genomic DNA defined a single-copy gene, zpu1, located on chromosome 2. Zpu1 mRNA was abundant in endosperm throughout starch biosynthesis, but was not detected in the leaf or the root. Anti-ZPU1 antiserum specifically recognized the approximately 100-kD ZPU1 protein in developing endosperm, but not in leaves. Pullulanase- and isoamylase-type DBEs were purified from extracts of developing maize kernels. The pullulanase-type activity was identified as ZPU1 and the isoamylase-type activity as SU1. Mutations of the sugary1 (su1) gene are known to cause deficiencies of SU1 isoamylase and a pullulanase-type DBE. ZPU1 activity, protein level, and electrophoretic mobility were altered in su1-mutant kernels, indicating that it is the affected pullulanase-type DBE. The Zpu1 transcript levels were equivalent in nonmutant and su1-mutant kernels, suggesting that coordinated regulation of ZPU1 and SU1 occurs posttranscriptionally.

1   This work was supported by grants from the U.S. Department of Agriculture (no. 96-35301-3159 to M.G.J. and A.M.M.) and from the National Science Foundation (no. DIR-9113593 to the Iowa State University Signal Transduction Training Group). This is journal paper no. J-18035 of project no. 3418 of the Iowa Agriculture and Home Economics Experiment Station, Ames.
2   These authors contributed equally to this work.
3   Present address: Pioneer HiBred International, Inc., Johnston, IA 50131.
*   Corresponding author; e-mail mgjames{at}iastate.edu; fax 1-515- 294-0453.

Plant Physiol. (1999) 119: 255-266
Copyright Clearance Center:   0032-0889/99/119//12
© 1999 American Society of Plant Physiologists




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