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J. Biol. Chem., Vol. 269, Issue 40, 24673-24678, 10, 1994

Structural requirement for recognition of the precursor proteins by the mitochondrial processing peptidase

WJ Ou, T Kumamoto, K Mihara, S Kitada, T Niidome, A Ito and T Omura
Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka, Japan.

We examined the structural characteristics of the extension peptides responsible for the recognition by the mitochondrial processing peptidase by using preadrenodoxin, which has a long extension peptide of 58 amino acid residues, as the substrate. The deletion of various parts of the extension peptide of pre-adrenodoxin indicated that more than 40 amino acid residues and the presence of basic amino acid residues in the distal portion (20-40 amino acid residues upstream of the cleavage site) were necessary for the recognition of the precursor by the peptidase. The processing of preadrenodoxin was strongly inhibited by the synthetic peptide corresponding to the middle portion of the extension peptide, whereas the peptide corresponding to the amino-terminal portion exhibited weak inhibition of the processing. The replacement of arginine residues in the middle portion of the extension peptide with neutral amino acids resulted in a great decrease in the processing. We conclude that basic amino acids at a position distal to the cleavage site are necessary for the recognition of the precursor proteins by the processing peptidase and that basic amino acids required for the mitochondrial targeting and those for the recognition by the peptidase are separately located in the extension peptide of pre- adrenodoxin.
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