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Molecular evidence of a unique lipoamide dehydrogenase in plastids:: analysis of plastidic lipoamide dehydrogenase from Arabidopsis thaliana

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FEBS LETTERS
卷 484, 期 1, 页码 12-16

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ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(00)02116-5

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lipoamide dehydrogenase; pyruvate dehydrogenase complex; glycine decarboxylase complex; acetyl-CoA; Arabidopsis thaliana

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Lipoamide dehydrogenase is a subunit of the alpha -ketoacid dehydrogenases and the glycine decarboxylase complex in mitochondria, and the pyruvate dehydrogenase complex in plastids. We report here the unexpected finding of two plastidic isoforms of lipoamide dehydrogenase from Arabidopsis thaliana that are different from the mitochondrial form of the enzyme. The cDNA clones were confirmed by sequence alignment analysis and their location verified by chloroplast import assay. They are single cop! genes that appear to be expressed in parallel in different tissues with highest level in developing siliques, Phylogenetic analysis gives further exemplary evidence for the plastidic evolution derived from cyanobacteria. (C) 2000 Federation of European Biochemical Societies, Published by Elsevier Science B.V. All rights reserved.

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