ArticleMolecular biology of the cell2020
More than just a ticket canceller: the mitochondrial processing peptidase tailors complex precursor proteins at internal cleavage sites.
Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Phosphomimetic Experiments Do Not Support a Causal Role for TFAM Phosphorylation in mtDNA Elimination in Sperm.Journal of molecular biology · 2025Article
- Proteolytic cleavage activates the mitochondrial isoform of TOP3A.Nucleic acids research · 2025Article
- Comprehensive review on alcohol-induced protein modifications in hepatic mitochondrial membranes and their functional implications.Molecular biology reports · 2025Review
- ACAD10 and ACAD11 allow entry of 4-hydroxy fatty acids into β-oxidation.Cellular and molecular life sciences : CMLS · 2024Article
- Organelle-dependent polyprotein designs enable stoichiometric expression of nitrogen fixation components targeted to mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- In-Depth Characterization of Apoptosis N-Terminome Reveals a Link Between Caspase-3 Cleavage and Posttranslational N-Terminal Acetylation.Molecular & cellular proteomics : MCP · 2023Review
- Cell-Based Sensors for the Detection of EGF and EGF-Stimulated CaBiosensors · 2023Article
- MTSviewer: A database to visualize mitochondrial targeting sequences, cleavage sites, and mutations on protein structures.PloS one · 2023Article
- Mitochondrial Processing Peptidases-Structure, Function and the Role in Human Diseases.International journal of molecular sciences · 2022Review
- Protein Processing in Plant Mitochondria Compared to Yeast and Mammals.Frontiers in plant science · 2022Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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