Substrate recognition by mitochondrial processing peptidase toward the malate dehydrogenase precursor

Journal of Biochemistry
K ShimokataAkio Ito

Abstract

Mitochondrial processing peptidase (MPP) cleaves the extension peptides of precursor proteins newly imported into the mitochondria. Using synthetic oligopeptides modeled on the extension peptide of malate dehydrogenase, the critical elements of the substrate for the processing of MPP were determined [Niidome, T., Kitada, S., Shimokata, K., Ogishima, T., and Ito, A. (1994) J. Biol. Chem. 269, 24719-24722; Ogishima, T., Niidome, T., Shimokata, K., Kitada, S., and Ito, A. (1995) ibid. 270, 30322-30326]. In the present study, we constructed mutant precursors and compared the processing reaction with that of the peptide substrates to confirm the validity of use of peptide substrates. In both cases, the arginine residue presents at a proximal (-2) position relative to the processing site proved to be important for the processing. The distal arginine residue at position 7 was replaceable with alanine with no significant loss in cleavage efficiency if the precursor protein contained two consecutive arginine residues at a proximal position, although the arginine residue at a position 7 was indispensable in the model peptide. The proline residue, lying between the distal and proximal arginine residues, which is assumed to break a continu...Continue Reading

Citations

Dec 22, 1999·Biochemical and Biophysical Research Communications·A Ito
Oct 8, 1999·Molecular Biology of the Cell·U Fünfschilling, S Rospert
Aug 23, 2002·Biochimica Et Biophysica Acta·Oleksandr GakhGrazia Isaya
Oct 14, 2000·The Journal of Biological Chemistry·K KojimaA Ito
Sep 17, 1998·The Journal of Biological Chemistry·K ShimokataA Ito

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