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.

Basic information

Original name

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

Authors

KAUROV, Losif (203 Czech Republic), Marie VANCOVÁ (203 Czech Republic), Bernd SCHIMANSKI (756 Switzerland), Lawrence Rudy CADENA (203 Czech Republic), Jiří HELLER (203 Czech Republic), Tomáš BÍLÝ (203 Czech Republic), David POTĚŠIL (203 Czech Republic, belonging to the institution), Caludia EICHENBERGER (756 Switzerland), Hannah BRUCE (826 United Kingdom of Great Britain and Northern Ireland), Silke OELJAKLAUS (276 Germany), Bettina WARSCHEID (276 Germany), Zbyněk ZDRÁHAL (203 Czech Republic, guarantor, belonging to the institution), Andre SCHNEIDER (756 Switzerland), Julius LUKEŠ (203 Czech Republic) and Hassan HASHIMI (203 Czech Republic)

Edition

Current Biology, Elsevier Science, 2018, 0960-9822

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 9.193

RIV identification code

RIV/00216224:14740/18:00104829

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

000449621400022

Keywords in English

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

Abstract

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.

Links

LM2015043, research and development project

Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)

Investor: Ministry of Education, Youth and Sports of the CR

LM2015062, research and development project

Name: Národní infrastruktura pro biologické a medicínské zobrazování

Investor: Ministry of Education, Youth and Sports of the CR

LQ1601, research and development project

Name: CEITEC 2020 (Acronym: CEITEC2020)

Investor: Ministry of Education, Youth and Sports of the CR

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 and Hassan HASHIMI. The Diverged Trypanosome MICOS Complex as a Hub for Mitochondrial Cristae Shaping and Protein Import. Current Biology. Elsevier Science, 2018, vol. 28, No 21, p. 3393-3407, 20 pp. ISSN 0960-9822. Available from: 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 and Hassan HASHIMI. The Diverged Trypanosome MICOS Complex as a Hub for Mitochondrial Cristae Shaping and Protein Import. \textit{Current Biology}. Elsevier Science, 2018, vol.~28, No~21, p.~3393-3407, 20 pp. ISSN~0960-9822. Available from: https://dx.doi.org/10.1016/j.cub.2018.09.008.

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