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

• DOI: 10.1101/2020.07.02.183996
• Publication Date: 2020-07-03T21:17:51Z
• Authors: Jana Friedl; Michael R. Knopp; Carina Groh; Eyal Paz; Sven B. Gould; Felix Boos; Johannes M. Herrmann
• Keywords: Mitochondrial matrix; Cleavage (geology)

Abstract Most mitochondrial proteins are synthesized in the cytosol as precursors that carry N-terminal presequences. After import into mitochondria, these targeting signals cleaved off by processing peptidase MPP, giving rise to shorter mature proteins. Using tandem protein Arg5,6 a model substrate, we demonstrate MPP has an additional role preprotein maturation, beyond removal of is polyprotein precursor imported matrix and subsequently separated two distinct enzymes function arginine biogenesis. This internal performed which cleaves both at its N-terminus site between Arg5 Arg6 parts. The peculiar organization biogenesis conserved across fungi might preserve mode co-translational subunit association biosynthesis complex polycistronic operon prokaryotic ancestors. Putative cleavage sites also present junctions other fusion from fungi, plants animals. Our data suggest that, addition “ticket canceller” for presequences, exhibits second, widely activity