Mitochondrial processing peptidase: multiple-site recognition of precursor proteins

Abstract

During or shortly after import of the precursor proteins into mitochondria, the amino-terminal extension peptides are first proteolytically removed by mitochondrial processing peptidase (MPP). The peptidase is a metalloendopeptidase, classified as a member of pitrilysin family, and forms a heterodimer consisting of structurally related alpha- and beta-subunits which are homologous to core proteins, core 2 and core 1, respectively, of mitochondrial ubiquinol-cytochrome c oxidoreductase complex. The enzyme specifically recognizes a large variety of mitochondrial precursor proteins and is cleaved at a single and specific site. In this review, I will focus on recognition mechanisms of precursor proteins by MPP. Structural characteristics of the precursor responsible for the recognition by MPP, role of each subunit, and amino acid residues of MPP involved in the recognition are discussed.