Plant Physiol. Drug Metab Dispos
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Plant Physiology 70:483-487 (1982)
© 1982 American Society of Plant Biologists

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Organelle-Bound Malate Dehydrogenase Isoenzymes Are Synthesized as Higher Molecular Weight Precursors 1

Christine Gietl and Bertold Hock

Department of Botany, Faculty of Agriculture and Horticulture, Technical University of Munich, D-8050 Freising 12, West Germany

Biosynthesis of malate dehydrogenase isoenzymes was studied in cotyledons of watermelons (Citrullus vulgaris Schrad., var. Stone Mountain). The glyoxysomal and mitochondrial isoenzymes are synthesized as higher molecular weight precursors which can be immunoprecipitated by mono-specific antibodies from the products of in vitro translation in reticulocyte lysates programed with cotyledonary mRNA and with the same size from enzyme extracts of pulse-labeled cotyledons. During translocation from the cytosol into the organelles, processing takes place. An 8 kilodalton extra sequence is cleaved from the glyoxysomal precursor and a 3.3 kilodalton extra sequence from the mitochondrial precursor producing the native subunits of 33 and 38 kilodaltons, respectively. The data support a post-translational translocation of the organelle-destined malate dehydrogenase isoenzymes. The in vitro translation of the cytosolic malate dehydrogenase I yields a product which has the same molecular weight as the subunit of the native isoenzyme (39.5 kilodaltons).

1 Supported by the Deutsche Forschungsgemeinschaft (Grant Ho 383/19).




This article has been cited by other articles:


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 Proc. Natl. Acad. Sci. USAHome page
B. Wimmer, F. Lottspeich, I. van der Klei, M. Veenhuis, and C. Gietl
The glyoxysomal and plastid molecular chaperones (70-kDa heat shock protein) of watermelon cotyledons are encoded by a single gene
PNAS, December 9, 1997; 94(25): 13624 - 13629.
[Abstract] [Full Text] [PDF]


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ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1982 by the American Society of Plant Biologists