Dataset Information

Cristae architecture is determined by an interplay of the MICOS complex and the F₁F_O ATP synthase via Mic27 and Mic10.

ABSTRACT: The inner boundary and the cristae membrane are connected by pore-like structures termed crista junctions (CJs). The MICOS complex is required for CJ formation and enriched at CJs. Here, we address the roles of the MICOS subunits Mic27 and Mic10. We observe a positive genetic interaction between Mic27 and Mic60 and deletion of Mic27 results in impaired formation of CJs and altered cristae membrane curvature. Mic27 acts in an antagonistic manner to Mic60 as it promotes oligomerization of the F₁F_O-ATP synthase and partially restores CJ formation in cells lacking Mic60. Mic10 impairs oligomerization of the F₁F_O-ATP synthase similar to Mic60. Applying complexome profiling, we observed that deletion of Mic27 destabilizes the MICOS complex but does not impair formation of a high molecular weight Mic10 subcomplex. Moreover, this Mic10 subcomplex comigrates with the dimeric F₁F_O-ATP synthase in a Mic27-independent manner. Further, we observed a chemical crosslink of Mic10 to Mic27 and of Mic10 to the F₁F_O-ATP synthase subunit e. We corroborate the physical interaction of the MICOS complex and the F₁F_O-ATP synthase. We propose a model in which part of the F₁F_O-ATP synthase is linked to the MICOS complex via Mic10 and Mic27 and by that is regulating CJ formation.

SUBMITTER: Eydt K

PROVIDER: S-EPMC5568431 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature

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Cristae architecture is determined by an interplay of the MICOS complex and the F<sub>1</sub>F<sub>O</sub> ATP synthase via Mic27 and Mic10.

Eydt Katharina K Davies Karen M KM Davies Karen M KM Behrendt Christina C Wittig Ilka I Reichert Andreas S AS

Microbial cell (Graz, Austria) 20170720 8

The inner boundary and the cristae membrane are connected by pore-like structures termed crista junctions (CJs). The MICOS complex is required for CJ formation and enriched at CJs. Here, we address the roles of the MICOS subunits Mic27 and Mic10. We observe a positive genetic interaction between Mic27 and Mic60 and deletion of Mic27 results in impaired formation of CJs and altered cristae membrane curvature. Mic27 acts in an antagonistic manner to Mic60 as it promotes oligomerization of the F<su ...[more]

PMID: 28845423

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Project description:Mitochondrial cristae are polymorphic invaginations of the inner membrane that are the fabric of cellular respiration. Both the mitochondrial contact site and cristae organization system (MICOS) and the F1FO-ATP synthase are vital for sculpting cristae by opposing membrane-bending forces. While MICOS promotes negative curvature at crista junctions, dimeric F1FO-ATP synthase is crucial for positive curvature at crista rims. Crosstalk between these two complexes has been observed in baker's yeast, the model organism of the Opisthokonta supergroup. Here, we report that this property is conserved in Trypanosoma brucei, a member of the Discoba clade that separated from the Opisthokonta ∼2 billion years ago. Specifically, one of the paralogs of the core MICOS subunit Mic10 interacts with dimeric F1FO-ATP synthase, whereas the other core Mic60 subunit has a counteractive effect on F1FO-ATP synthase oligomerization. This is evocative of the nature of MICOS-F1FO-ATP synthase crosstalk in yeast, which is remarkable given the diversification that these two complexes have undergone during almost 2 eons of independent evolution. Furthermore, we identified a highly diverged, putative homolog of subunit e, which is essential for the stability of F1FO-ATP synthase dimers in yeast. Just like subunit e, it is preferentially associated with dimers and interacts with Mic10, and its silencing results in severe defects to cristae and the disintegration of F1FO-ATP synthase dimers. Our findings indicate that crosstalk between MICOS and dimeric F1FO-ATP synthase is a fundamental property impacting crista shape throughout eukaryotes. IMPORTANCE Mitochondria have undergone profound diversification in separate lineages that have radiated since the last common ancestor of eukaryotes some eons ago. Most eukaryotes are unicellular protists, including etiological agents of infectious diseases, like Trypanosoma brucei. Thus, the study of a broad range of protists can reveal fundamental features shared by all eukaryotes and lineage-specific innovations. Here, we report that two different protein complexes, MICOS and F1FO-ATP synthase, known to affect mitochondrial architecture, undergo crosstalk in T. brucei, just as in baker's yeast. This is remarkable considering that these complexes have otherwise undergone many changes during their almost 2 billion years of independent evolution. Thus, this crosstalk is a fundamental property needed to maintain proper mitochondrial structure even if the constituent players considerably diverged.

Dataset Information

Cristae architecture is determined by an interplay of the MICOS complex and the F₁F_O ATP synthase via Mic27 and Mic10.

Publications

Cristae architecture is determined by an interplay of the MICOS complex and the F<sub>1</sub>F<sub>O</sub> ATP synthase via Mic27 and Mic10.

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Dataset Information

Cristae architecture is determined by an interplay of the MICOS complex and the F1FO ATP synthase via Mic27 and Mic10.

Publications

Cristae architecture is determined by an interplay of the MICOS complex and the F<sub>1</sub>F<sub>O</sub> ATP synthase via Mic27 and Mic10.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Cristae architecture is determined by an interplay of the MICOS complex and the F₁F_O ATP synthase via Mic27 and Mic10.