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

Biochem J. 1990 Jun 15;268(3):783-9. doi: 10.1042/bj2680783.


We have isolated and characterized cDNA clones encoding the H-protein of the glycine-cleavage system of pea (Pisum sativum) leaf mitochondria. The deduced primary structure revealed that the 131-amino-acid polypeptide is cytoplasmically synthesized with a 34-amino-acid mitochondrial targeting peptide. The lipoate-binding site was assigned to be lysine-63, as deduced from a sequence comparison with several lipoate-bearing proteins. The expression of the gene encoding H-protein was shown to occur specifically in the leaf tissue, with light exerting an additional effect by increasing the mRNA levels severalfold. Two polyadenylation sites were found in the mRNA, and a single-copy gene encoding the H-protein was detected in pea genome.

MeSH terms

  • Amino Acid Oxidoreductases*
  • Amino Acid Sequence
  • Base Sequence
  • Carrier Proteins / analysis
  • Carrier Proteins / biosynthesis*
  • Carrier Proteins / genetics
  • Cloning, Molecular
  • Fabaceae / genetics
  • Fabaceae / metabolism*
  • Gene Expression
  • Glycine Decarboxylase Complex H-Protein
  • Glycine Dehydrogenase (Decarboxylating)
  • Mitochondria / metabolism*
  • Molecular Sequence Data
  • Plants, Medicinal*
  • Recombinant Proteins / analysis
  • Recombinant Proteins / biosynthesis*
  • Recombinant Proteins / genetics
  • Species Specificity


  • Carrier Proteins
  • Glycine Decarboxylase Complex H-Protein
  • Recombinant Proteins
  • Amino Acid Oxidoreductases
  • Glycine Dehydrogenase (Decarboxylating)