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The highly diverged trypanosomal MICOS complex is organized in a nonessential integral membrane and an essential peripheral module

C. Eichenberger, S. Oeljeklaus, J. Bruggisser, J. Mani, B. Haenni, I. Kaurov, M. Niemann, B. Zuber, J. Lukeš, H. Hashimi, B. Warscheid, B. Schimanski, A. Schneider,

. 2019 ; 112 (6) : 1731-1743. [pub] 20191003

Jazyk angličtina Země Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc20023432
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NLK Free Medical Journals od 1997 do Před 18 měsíci
Wiley Free Content od 1997 do Před 18 měsíci

Odkazy

PubMed 31541487
DOI 10.1111/mmi.14389
Knihovny.cz E-zdroje

The mitochondrial contact site and cristae organization system (MICOS) mediates the formation of cristae, invaginations in the mitochondrial inner membrane. The highly diverged MICOS complex of the parasitic protist Trypanosoma brucei consists of nine subunits. Except for two Mic10-like and a Mic60-like protein, all subunits are specific for kinetoplastids. Here, we determined on a proteome-wide scale how ablation of individual MICOS subunits affects the levels of the other subunits. The results reveal co-regulation of TbMic10-1, TbMic10-2, TbMic16 and TbMic60, suggesting that these nonessential, integral inner membrane proteins form an interdependent network. Moreover, the ablation of TbMic34 and TbMic32 reveals another network consisting of the essential, intermembrane space-localized TbMic20, TbMic32, TbMic34 and TbMic40, all of which are peripherally associated with the inner membrane. The downregulation of TbMic20, TbMic32 and TbMic34 also interferes with mitochondrial protein import and reduces the size of the TbMic10-containing complexes. Thus, the diverged MICOS of trypanosomes contains two subcomplexes: a nonessential membrane-integrated one, organized around the conserved Mic10 and Mic60, that mediates cristae formation, and an essential membrane-peripheral one consisting of four kinetoplastid-specific subunits, that is required for import of intermembrane space proteins.

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$a Eichenberger, Claudia $u Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, Bern, CH-3012, Switzerland.
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$a The mitochondrial contact site and cristae organization system (MICOS) mediates the formation of cristae, invaginations in the mitochondrial inner membrane. The highly diverged MICOS complex of the parasitic protist Trypanosoma brucei consists of nine subunits. Except for two Mic10-like and a Mic60-like protein, all subunits are specific for kinetoplastids. Here, we determined on a proteome-wide scale how ablation of individual MICOS subunits affects the levels of the other subunits. The results reveal co-regulation of TbMic10-1, TbMic10-2, TbMic16 and TbMic60, suggesting that these nonessential, integral inner membrane proteins form an interdependent network. Moreover, the ablation of TbMic34 and TbMic32 reveals another network consisting of the essential, intermembrane space-localized TbMic20, TbMic32, TbMic34 and TbMic40, all of which are peripherally associated with the inner membrane. The downregulation of TbMic20, TbMic32 and TbMic34 also interferes with mitochondrial protein import and reduces the size of the TbMic10-containing complexes. Thus, the diverged MICOS of trypanosomes contains two subcomplexes: a nonessential membrane-integrated one, organized around the conserved Mic10 and Mic60, that mediates cristae formation, and an essential membrane-peripheral one consisting of four kinetoplastid-specific subunits, that is required for import of intermembrane space proteins.
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$a Oeljeklaus, Silke $u Department of Biochemistry and Functional Proteomics, Faculty of Biology, University of Freiburg, Freiburg, 79104, Germany. Signalling Research Centres BIOSS and CIBSS, University of Freiburg, Freiburg, 79104, Germany.
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$a Bruggisser, Julia $u Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, Bern, CH-3012, Switzerland.
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$a Haenni, Beat $u Institute of Anatomy, University of Bern, Baltzerstrasse 2, Bern, 3012, Switzerland.
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$a Kaurov, Iosif $u Institute of Parasitology, Biology Center, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic. Faculty of Science, University of South Bohemia, 370 05, České Budějovice (Budweis), Czech Republic.
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$a Niemann, Moritz $u Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, Bern, CH-3012, Switzerland.
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$a Lukeš, Julius $u Institute of Parasitology, Biology Center, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic. Faculty of Science, University of South Bohemia, 370 05, České Budějovice (Budweis), Czech Republic.
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$a Hashimi, Hassan $u Institute of Parasitology, Biology Center, Czech Academy of Sciences, České Budějovice (Budweis), Czech Republic. Faculty of Science, University of South Bohemia, 370 05, České Budějovice (Budweis), Czech Republic.
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$a Warscheid, Bettina $u Department of Biochemistry and Functional Proteomics, Faculty of Biology, University of Freiburg, Freiburg, 79104, Germany. Signalling Research Centres BIOSS and CIBSS, University of Freiburg, Freiburg, 79104, Germany.
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$a Schimanski, Bernd $u Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, Bern, CH-3012, Switzerland.
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