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Molecular evidence of a unique lipoamide dehydrogenase in plastids: analysis of plastidic lipoamide dehydrogenase from Arabidopsis thaliana 1
Author(s) -
Lutziger Isabelle,
Oliver David J.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02116-5
Subject(s) - pyruvate dehydrogenase complex , plastid , biology , dihydrolipoamide dehydrogenase , pyruvate dehydrogenase lipoamide kinase isozyme 1 , arabidopsis thaliana , dehydrogenase , chloroplast , biochemistry , pyruvate dehydrogenase phosphatase , nadh dehydrogenase , microbiology and biotechnology , protein subunit , gene , enzyme , mutant
Lipoamide dehydrogenase is a subunit of the α‐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 copy 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.