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RSS FeedsIJMS, Vol. 23, Pages 1297: Mitochondrial Processing Peptidases—Structure, Function and the Role in Human Diseases (International Journal of Molecular Sciences)

 
 

24 january 2022 15:58:03

 
IJMS, Vol. 23, Pages 1297: Mitochondrial Processing Peptidases—Structure, Function and the Role in Human Diseases (International Journal of Molecular Sciences)
 


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.


 
63 viewsCategory: Biochemistry, Biophysics, Molecular Biology
 
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