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

J 2018

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

KAUROV, Losif, Marie VANCOVÁ, Bernd SCHIMANSKI, Lawrence Rudy CADENA, Jiří HELLER et. al.

Základní údaje

Originální název

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

Autoři

KAUROV, Losif (203 Česká republika), Marie VANCOVÁ (203 Česká republika), Bernd SCHIMANSKI (756 Švýcarsko), Lawrence Rudy CADENA (203 Česká republika), Jiří HELLER (203 Česká republika), Tomáš BÍLÝ (203 Česká republika), David POTĚŠIL (203 Česká republika, domácí), Caludia EICHENBERGER (756 Švýcarsko), Hannah BRUCE (826 Velká Británie a Severní Irsko), Silke OELJAKLAUS (276 Německo), Bettina WARSCHEID (276 Německo), Zbyněk ZDRÁHAL (203 Česká republika, garant, domácí), Andre SCHNEIDER (756 Švýcarsko), Julius LUKEŠ (203 Česká republika) a Hassan HASHIMI (203 Česká republika)

Vydání

Current Biology, Elsevier Science, 2018, 0960-9822

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 9.193

Kód RIV

RIV/00216224:14740/18:00104829

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1016/j.cub.2018.09.008

UT WoS

000449621400022

Klíčová slova anglicky

CONTACT SITE; ORGANIZING SYSTEM; INTERMEMBRANE SPACE; INNER MEMBRANE; OUTER-MEMBRANE; MIA PATHWAY; BRUCEI; ORGANIZATION; ARCHITECTURE; BIOGENESIS

Štítky

CF PROT, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 13. 3. 2019 17:08, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

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.

Návaznosti

LM2015043, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology

LM2015062, projekt VaV

Název: Národní infrastruktura pro biologické a medicínské zobrazování

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, National research infrastructure for biological and medical imaging

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

Citovat

KAUROV, Losif, Marie VANCOVÁ, Bernd SCHIMANSKI, Lawrence Rudy CADENA, Jiří HELLER, Tomáš BÍLÝ, David POTĚŠIL, Caludia EICHENBERGER, Hannah BRUCE, Silke OELJAKLAUS, Bettina WARSCHEID, Zbyněk ZDRÁHAL, Andre SCHNEIDER, Julius LUKEŠ a Hassan HASHIMI. The Diverged Trypanosome MICOS Complex as a Hub for Mitochondrial Cristae Shaping and Protein Import. Current Biology. Elsevier Science, 2018, roč. 28, č. 21, s. 3393-3407, 20 s. ISSN 0960-9822. Dostupné z: https://dx.doi.org/10.1016/j.cub.2018.09.008.

@article{1475797,
   author = {Kaurov, Losif and Vancová, Marie and Schimanski, Bernd and Cadena, Lawrence Rudy and Heller, Jiří and Bílý, Tomáš and Potěšil, David and Eichenberger, Caludia and Bruce, Hannah and Oeljaklaus, Silke and Warscheid, Bettina and Zdráhal, Zbyněk and Schneider, Andre and Lukeš, Julius and Hashimi, Hassan},
   article_number = {21},
   doi = {http://dx.doi.org/10.1016/j.cub.2018.09.008},
   keywords = {CONTACT SITE; ORGANIZING SYSTEM; INTERMEMBRANE SPACE; INNER MEMBRANE; OUTER-MEMBRANE; MIA PATHWAY; BRUCEI; ORGANIZATION; ARCHITECTURE; BIOGENESIS},
   language = {eng},
   issn = {0960-9822},
   journal = {Current Biology},
   title = {The Diverged Trypanosome MICOS Complex as a Hub for Mitochondrial Cristae Shaping and Protein Import},
   volume = {28},
   year = {2018}
}

TY  - JOUR
ID  - 1475797
AU  - Kaurov, Losif - Vancová, Marie - Schimanski, Bernd - Cadena, Lawrence Rudy - Heller, Jiří - Bílý, Tomáš - Potěšil, David - Eichenberger, Caludia - Bruce, Hannah - Oeljaklaus, Silke - Warscheid, Bettina - Zdráhal, Zbyněk - Schneider, Andre - Lukeš, Julius - Hashimi, Hassan
PY  - 2018
TI  - The Diverged Trypanosome MICOS Complex as a Hub for Mitochondrial Cristae Shaping and Protein Import
JF  - Current Biology
VL  - 28
IS  - 21
SP  - 3393-3407
EP  - 3393-3407
PB  - Elsevier Science
SN  - 09609822
KW  - CONTACT SITE
KW  - ORGANIZING SYSTEM
KW  - INTERMEMBRANE SPACE
KW  - INNER MEMBRANE
KW  - OUTER-MEMBRANE
KW  - MIA PATHWAY
KW  - BRUCEI
KW  - ORGANIZATION
KW  - ARCHITECTURE
KW  - BIOGENESIS
N2  - 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.
ER  -

KAUROV, Losif, Marie VANCOVÁ, Bernd SCHIMANSKI, Lawrence Rudy CADENA, Jiří HELLER, Tomáš BÍLÝ, David POTĚŠIL, Caludia EICHENBERGER, Hannah BRUCE, Silke OELJAKLAUS, Bettina WARSCHEID, Zbyněk ZDRÁHAL, Andre SCHNEIDER, Julius LUKEŠ a Hassan HASHIMI. The Diverged Trypanosome MICOS Complex as a Hub for Mitochondrial Cristae Shaping and Protein Import. \textit{Current Biology}. Elsevier Science, 2018, roč.~28, č.~21, s.~3393-3407, 20 s. ISSN~0960-9822. Dostupné z: https://dx.doi.org/10.1016/j.cub.2018.09.008.

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