cDNA cloning, primary structure and gene expression for H-protein, a component of the glycine-cleavage system (glycine decarboxylase) of pea (Pisum sativum) leaf mitochondria

Macherel, D.; Lebrun, M.; Gagnon, J.; Neuburger, M.; Douce, R.

Biochemical Journal 268(3): 783-789

1990


ISSN/ISBN: 0264-6021
PMID: 2363710
DOI: 10.1042/bj2680783
Accession: 001768798

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Abstract
The deduced primary structure of cDNA clones revealed that the 131-amino-acid polypeptide is cytoplasmically synthesized with a 34-amino-acid mitochondrial targeting peptide. The lipoate-binding site was thought to be lysine-63, as deduced from a sequence comparison with several lipoate-bearing proteins. Expression of the gene encoding H-protein was shown to occur specifically in the leaf tissue, with light exerting an additional effect by increasing mRNA levels several-fold. Two polyadenylation sites were found in the mRNA and a single-copy gene encoding the H-protein was detected in the pea genome.