The Diverged Trypanosome MICOS Complex as a Hub for Mitochondrial Cristae Shaping and Protein Import

0498713 - BC 2019 RIV GB eng J - Článek v odborném periodiku
Kaurov, Iosif - Vancová, Marie - Schimanski, B. - Cadena, L. R. - Heller, Jiří - Bílý, Tomáš - Potěšil, D. - Eichenberger, C. - Bruce, H. - Oeljeklaus, S. - Warscheid, B. - Zdráhal, Z. - Schneider, A. - Lukeš, Julius - Hashimi, Hassan
The Diverged Trypanosome MICOS Complex as a Hub for Mitochondrial Cristae Shaping and Protein Import.
Current Biology. Roč. 28, č. 21 (2018), s. 3393-3407.e5. ISSN 0960-9822. E-ISSN 1879-0445
Grant CEP: GA ČR(CZ) GA16-18699S; GA ČR GA17-24036S; GA MŠMT LL1601; GA MŠMT(CZ) EF16_019/0000759; GA MŠMT(CZ) LM2015062
Institucionální podpora: RVO:60077344
Klíčová slova: cristae * intermembrane space * micos * mitochondria * protein import * Trypanosoma brucei
Obor OECD: Genetics and heredity (medical genetics to be 3)
Impakt faktor: 9.193, rok: 2018
https://www.cell.com/current-biology/fulltext/S0960-9822(18)31203-X?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS096098221831203X%3Fshowall%3Dtrue

The mitochondrial contact site and cristae organization system (MICOS) is a multiprotein complex responsible for cristae formation. Even though cristae are found in all mitochondria capable of oxidative phosphorylation, only Mic10 and Mic60 appear to be conserved throughout eukaryotes. The remaining 4 or 5 known MICOS subunits are specific to the supergroup Opisthokonta, which includes yeast and mammals that are the only organisms in which this complex has been analyzed experimentally. We have isolated the MICOS from Trypanosoma brucei, a member of the supergroup Excavata that is profoundly diverged from opisthokonts. We show that it is required for the maintenance of the unique discoidal cristae that typify excavates, such as euglenids and kinetoplastids, the latter of which include trypanosomes. The trypanosome MICOS consists of 9 subunits, most of which are essential for normal growth. Unlike in opisthokonts, it contains two distinct Mic10 orthologs and an unconventional putative Mic60 that lacks a mitofilin domain. Interestingly, one of the essential trypanosomatid-specific MICOS subunits called TbMic20 is a thioredoxin-like protein that appears to be involved in import of intermembrane space proteins, including respiratory chain complex assembly factors. This result points to trypanosome MICOS coordinating cristae shaping and population of its membrane with proteins involved in respiration, the latter via the catalytic activity of TbMic20. Thus, trypanosome MICOS allows us to define which of its features are conserved in all eukaryotes and decipher those that represent lineage-specific adaptations. The mitochondrial contact site and cristae organizing system (MICOS) is a conserved feature of mitochondria. Kaurov et al. identify and characterize MICOS proteins outside of opisthokonts in the kinetoplastid parasite Trypanosoma brucei. TbMICOS plays a conserved role in mitochondrial cristae shaping and harbors several unique features as well.
Trvalý link: http://hdl.handle.net/11104/0290995