%0 Journal Article %1 ievaMitochondrialInnerMembrane2013 %A Ieva, Raffaele %A Heißwolf, Anna K. %A Gebert, Michael %A Vögtle, F.-Nora %A Wollweber, Florian %A Mehnert, Carola S. %A Oeljeklaus, Silke %A Warscheid, Bettina %A Meisinger, Chris %A van der Laan, Martin %A Pfanner, Nikolaus %C England %D 2013 %J Nature communications %K Acid Amino Complex Import Membranes/chemistry/metabolism,Mitochondrial Motifs,Endopeptidases/genetics/*metabolism,Membrane Multimerization,Protein Post-Translational,Protein Precursor Processing Protein Proteins,Mitochondrial Proteins/*chemistry/genetics/*metabolism,Membrane Proteins/*chemistry/genetics/*metabolism,Saccharomyces Proteins/chemistry/genetics/*metabolism,Mitochondria/chemistry/enzymology/genetics/*metabolism,Mitochondrial Proteins/genetics/*metabolism,Protein Transport Transport,Saccharomyces cerevisiae cerevisiae/chemistry/*enzymology/genetics/metabolism,to_read %P 2853 %R 10.1038/ncomms3853 %T Mitochondrial Inner Membrane Protease Promotes Assembly of Presequence Translocase by Removing a Carboxy-Terminal Targeting Sequence. %V 4 %X The presequence translocase of the inner mitochondrial membrane (TIM23 complex) is essential for importing cleavable preproteins into mitochondria. The preproteins contain amino-terminal targeting sequences that are removed by the mitochondrial processing peptidase (MPP). Some preproteins carry bipartite presequences that are cleaved twice, by MPP and the inner membrane protease (IMP). Here, we report that the TIM23 complex is altered in mitochondria lacking the IMP subunit Imp1 although none of the TIM23 components contains a bipartite presequence. We show that the TIM23 subunit Mgr2 is processed by IMP, but not by MPP. The cytosolic precursor of Mgr2 contains a carboxy-terminal sequence that promotes targeting to mitochondria, but impairs stable assembly and function of the mature TIM23 complex. IMP removes the carboxy-terminal targeting sequence and thus promotes proper assembly of the TIM23 complex. Our results reveal carboxy-terminal processing as a new mechanism in the biogenesis of the mitochondrial inner membrane.

@article{ievaMitochondrialInnerMembrane2013, abstract = {The presequence translocase of the inner mitochondrial membrane (TIM23 complex) is essential for importing cleavable preproteins into mitochondria. The preproteins contain amino-terminal targeting sequences that are removed by the mitochondrial processing peptidase (MPP). Some preproteins carry bipartite presequences that are cleaved twice, by MPP and the inner membrane protease (IMP). Here, we report that the TIM23 complex is altered in mitochondria lacking the IMP subunit Imp1 although none of the TIM23 components contains a bipartite presequence. We show that the TIM23 subunit Mgr2 is processed by IMP, but not by MPP. The cytosolic precursor of Mgr2 contains a carboxy-terminal sequence that promotes targeting to mitochondria, but impairs stable assembly and function of the mature TIM23 complex. IMP removes the carboxy-terminal targeting sequence and thus promotes proper assembly of the TIM23 complex. Our results reveal carboxy-terminal processing as a new mechanism in the biogenesis of the mitochondrial inner membrane.}, added-at = {2024-05-17T13:01:35.000+0200}, address = {England}, author = {Ieva, Raffaele and Hei{\ss}wolf, Anna K. and Gebert, Michael and V{\"o}gtle, F.-Nora and Wollweber, Florian and Mehnert, Carola S. and Oeljeklaus, Silke and Warscheid, Bettina and Meisinger, Chris and {van der Laan}, Martin and Pfanner, Nikolaus}, biburl = {https://www.bibsonomy.org/bibtex/2dc48f533c59bf77244790ac552e7fd13/warscheidlab}, doi = {10.1038/ncomms3853}, interhash = {0d5a77ce5f3e212558eda81ff7bacf41}, intrahash = {dc48f533c59bf77244790ac552e7fd13}, issn = {2041-1723}, journal = {Nature communications}, keywords = {Acid Amino Complex Import Membranes/chemistry/metabolism,Mitochondrial Motifs,Endopeptidases/genetics/*metabolism,Membrane Multimerization,Protein Post-Translational,Protein Precursor Processing Protein Proteins,Mitochondrial Proteins/*chemistry/genetics/*metabolism,Membrane Proteins/*chemistry/genetics/*metabolism,Saccharomyces Proteins/chemistry/genetics/*metabolism,Mitochondria/chemistry/enzymology/genetics/*metabolism,Mitochondrial Proteins/genetics/*metabolism,Protein Transport Transport,Saccharomyces cerevisiae cerevisiae/chemistry/*enzymology/genetics/metabolism,to_read}, langid = {english}, pages = 2853, pmid = {24287567}, timestamp = {2024-05-17T13:01:35.000+0200}, title = {Mitochondrial Inner Membrane Protease Promotes Assembly of Presequence Translocase by Removing a Carboxy-Terminal Targeting Sequence.}, volume = 4, year = 2013 }