More than just a ticket canceller: the mitochondrial processing peptidase tailors complex precursor proteins at internal cleavage sites

• DOI: 10.1091/mbc.e20-08-0524
• Publication Date: 2020-09-30T16:50:42Z
• Authors: Jana Friedl; Michael R. Knopp; Carina Groh; Eyal Paz; Sven B. Gould; Johannes M. Herrmann; Felix Boos
• Keywords: Cleavage (geology)

Most mitochondrial proteins are synthesized as precursors that carry N-terminal presequences. After they imported into mitochondria, these targeting signals cleaved off by the processing peptidase (MPP). Using tandem protein Arg5,6 a model substrate, we demonstrate MPP has an additional role in preprotein maturation, beyond removal of is polyprotein precursor mitochondria and subsequently separated two distinct enzymes. This internal performed MPP, which cleaves at its N-terminus site. The peculiar organization conserved across fungi reflects polycistronic arginine operon prokaryotes. cleavage sites also present other fusion from fungi, plants, animals. Hence, besides "ticket canceller" for presequences, exhibits second activity complex proteins.