Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Molecular Cloning and Expression Analysis of the Mitochondrial Pyruvate Dehydrogenase from Maize1

Jay J. Thelen, Jan A. Miernyk, and Douglas D. Randall*

Department of Biological Sciences (J.J.T.), and Department of Biochemistry (D.D.R., J.A.M.), University of Missouri, Columbia, Missouri 65211; and University of Missouri, Columbia, Missouri 65211Mycotoxin Research Unit, United States Department of Agriculture-Agricultural Research Service, National Center for Agricultural Utilization Research, Peoria, Illinois 61604 (J.A.M.)

Four cDNAs, one encoding an alpha -subunit and three encoding beta -subunits of the mitochondrial pyruvate dehydrogenase, were isolated from maize (Zea mays L.) libraries. The deduced amino acid sequences of both alpha - and beta -subunits are approximately 80% identical with Arabidopsis and pea (Pisum sativum L.) homologs. The mature N terminus was determined for the beta -subunit by microsequencing the protein purified from etiolated maize shoot mitochondria and was resolved by two-dimensional gel electrophoresis. This single isoelectric species comprised multiple isoforms. Both alpha - and beta -subunits are encoded by multigene families in maize, as determined by Southern-blot analyses. RNA transcripts for both alpha - and beta -subunits were more abundant in roots than in young leaves or etiolated shoots. Pyruvate dehydrogenase activity was also higher in roots (5-fold) compared with etiolated shoots and leaves. Both subunits were present at similar levels in all tissues examined, indicating coordinated gene regulation. The protein levels were highest in heterotrophic organs and in pollen, which contained about 2-fold more protein than any other organ examined. The relative abundance of these proteins in nonphotosynthetic tissues may reflect a high cellular content of mitochondria, a high level of respiratory activity, or an extra plastidial requirement for acetate.

1   This research was supported by National Science Foundation grant no. IBN-9419489 and by a Maize Training Grant Fellowship awarded to J.J.T. This is journal report 12,744 from the Missouri Agricultural Experiment Station.
*   Corresponding author; e-mail bchemdr{at}showme.missouri.edu; fax 1-573-882-5635.

Plant Physiol. (1999) 119: 635-644
Copyright Clearance Center:   0032-0889/99/119//10
© 1999 American Society of Plant Physiologists




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