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Mitochondrial Processing Peptidases—Structure, Function and the Role in Human Diseases

Department of Biochemistry and Protein Structure, Institute of Molecular Biology, Slovak Academy of Sciences, Dúbravská Cesta 21, 845 51 Bratislava, Slovakia
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Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editor: Salvatore Passarella
Int. J. Mol. Sci. 2022, 23(3), 1297; https://doi.org/10.3390/ijms23031297
Received: 28 December 2021 / Revised: 21 January 2022 / Accepted: 22 January 2022 / Published: 24 January 2022
(This article belongs to the Special Issue Mitochondrial Transport and Energy Metabolism in Health and Diseases)
Mitochondrial proteins are encoded by both nuclear and mitochondrial DNA. While some of the essential subunits of the oxidative phosphorylation (OXPHOS) complexes responsible for cellular ATP production are synthesized directly in the mitochondria, most mitochondrial proteins are first translated in the cytosol and then imported into the organelle using a sophisticated transport system. These proteins are directed mainly by targeting presequences at their N-termini. These presequences need to be cleaved to allow the proper folding and assembly of the pre-proteins into functional protein complexes. In the mitochondria, the presequences are removed by several processing peptidases, including the mitochondrial processing peptidase (MPP), the inner membrane processing peptidase (IMP), the inter-membrane processing peptidase (MIP), and the mitochondrial rhomboid protease (Pcp1/PARL). Their proper functioning is essential for mitochondrial homeostasis as the disruption of any of them is lethal in yeast and severely impacts the lifespan and survival in humans. In this review, we focus on characterizing the structure, function, and substrate specificities of mitochondrial processing peptidases, as well as the connection of their malfunctions to severe human diseases. View Full-Text
Keywords: mitochondrial processing peptidases; MPP; MIP; IMP; mitochondrial rhomboid protease; mitochondrial disease mitochondrial processing peptidases; MPP; MIP; IMP; mitochondrial rhomboid protease; mitochondrial disease
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MDPI and ACS Style

Kunová, N.; Havalová, H.; Ondrovičová, G.; Stojkovičová, B.; Bauer, J.A.; Bauerová-Hlinková, V.; Pevala, V.; Kutejová, E. Mitochondrial Processing Peptidases—Structure, Function and the Role in Human Diseases. Int. J. Mol. Sci. 2022, 23, 1297. https://doi.org/10.3390/ijms23031297

AMA Style

Kunová N, Havalová H, Ondrovičová G, Stojkovičová B, Bauer JA, Bauerová-Hlinková V, Pevala V, Kutejová E. Mitochondrial Processing Peptidases—Structure, Function and the Role in Human Diseases. International Journal of Molecular Sciences. 2022; 23(3):1297. https://doi.org/10.3390/ijms23031297

Chicago/Turabian Style

Kunová, Nina, Henrieta Havalová, Gabriela Ondrovičová, Barbora Stojkovičová, Jacob A. Bauer, Vladena Bauerová-Hlinková, Vladimir Pevala, and Eva Kutejová. 2022. "Mitochondrial Processing Peptidases—Structure, Function and the Role in Human Diseases" International Journal of Molecular Sciences 23, no. 3: 1297. https://doi.org/10.3390/ijms23031297

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