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Journal of Experimental Botany, Vol. 52, No. 361, pp. 1739-1740, August 1, 2001
© 2001 Oxford University Press

Gene Note

ZMPP2, a novel type-2C protein phosphatase from maize

Amanda K. Broz1, Jay J. Thelen1,4, Michael G. Muszynski2, Jan A. Miernyk1,3 and Douglas D. Randall1,5

1 Department of Biochemistry, University of Missouri, Columbia, Missouri 65211, USA
2 Pioneer Hi-Bred International, Inc., Johnston, Iowa 50131-1004, USA
3 USDA, Agricultural Research Service, Plant Genetics Research Unit, Columbia, Missouri 65211, USA

Abstract

A cDNA clone was selected as a candidate for the catalytic subunit of phospho-pyruvate dehydrogenase phosphatase (PDP) by screening a Zea mays expressed sequence tag database with the bovine PDP deduced amino acid sequence. Both strands of the cDNA were completely sequenced. The maize clone contains an open reading frame of 1098 base pairs that encodes a polypeptide of 40 127 Da, ZMPP2. The deduced amino acid sequence of ZMPP2 contains the five PP2C signature domains, as does PDP. However, the expression pattern of ZMPP2, determined by reverse transcriptase-polymerase chain reaction, was different from those of the maize pyruvate dehydrogenase E1{alpha} subunit and pyruvate dehydrogenase kinase. Additionally, the predicted subcellular location of ZMPP2 is cytoplasmic, while the pyruvate dehydrogenase complex, regulated by reversible phosphorylation, is mitochondrial. Thus, ZMPP2 is a PP2C-type protein phosphatase related to but distinct from PDP.

Key words: Zea mays, PP2C, phosphatase.


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