Abstract:
:Most mitochondrial proteins are synthesized as precursors that carry N-terminal presequences. After they are imported into mitochondria, these targeting signals are cleaved off by the mitochondrial processing peptidase (MPP). Using the mitochondrial tandem protein Arg5,6 as a model substrate, we demonstrate that MPP has an additional role in preprotein maturation, beyond the removal of presequences. Arg5,6 is synthesized as a polyprotein precursor that is imported into mitochondria and subsequently separated into two distinct enzymes. This internal processing is performed by MPP, which cleaves the Arg5,6 precursor at its N-terminus and at an internal site. The peculiar organization of Arg5,6 is conserved across fungi and reflects the polycistronic arginine operon in prokaryotes. MPP cleavage sites are also present in other mitochondrial fusion proteins from fungi, plants, and animals. Hence, besides its role as a "ticket canceller" for removal of presequences, MPP exhibits a second conserved activity as an internal processing peptidase for complex mitochondrial precursor proteins.
journal_name
Mol Biol Celljournal_title
Molecular biology of the cellauthors
Friedl J,Knopp MR,Groh C,Paz E,Gould SB,Herrmann JM,Boos Fdoi
10.1091/mbc.E20-08-0524subject
Has Abstractpub_date
2020-11-15 00:00:00pages
2657-2668issue
24eissn
1059-1524issn
1939-4586journal_volume
31pub_type
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