Structure and function of the<i>S. pombe</i>III–IV–cyt<i>c</i>supercomplex

Moe, Agnes; Dimogkioka, Anna-Roza; Rapaport, Doron; Öjemyr, Linda Näsvik; Brzezinski, Peter

doi:10.1073/pnas.2307697120

Cited by 5 publications

(1 citation statement)

References 92 publications

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“…Examination of the III:IV interface (Fig. 2a) shows that it is formed by six apicomplexan subunits of CIV, COX31, 33, 34, 36, 39 and COX40, and two canonical subunits, COX2B and COX6B, making the interface substantially larger than in previously reported III-IV SC structures [17][18][19][20][21] . Most of the interactions formed by the apicomplexan subunits are in the intermembrane space (IMS) between a single CIV copy and one CIII monomer (Fig.…”

Section: Structural Characterisation Of the Ii2-iii2-iv2 Mitochondria...mentioning

confidence: 77%

Structure of the II2-III2-IV2 mitochondrial supercomplex from the parasitePerkinsus marinus

Wú,

Mühleip,

Gruhl

et al. 2024

Preprint

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Respiratory complexes have co-evolved into supercomplexes in different clades to sustain energy production at the basis of eukaryotic life. In this study, using cryogenic electron microscopy, we determined the 2.1 Angstrom resolution structure of a 104-subunit II2-III2-IV2 supercomplex from the parasite Perkinsus marinus, related to Apicomplexa, capable of complete electron transport from succinate to molecular oxygen. A feature of the parasite is the association of two copies of complex II via the apicomplexan subunit SDHG that interacts with both complexes III and IV and bridge the supercomplex. In the c1 state, we identified two protein factors, ISPR1 and ISPR2 bound on the surface of complex III, where Cytochrome c docks, acting as negative regulators. The acquisition of 15 specific subunits to complex IV results in its lateral offset, increasing the distance between the Cytochrome c electron donor and acceptor sites. The domain homologous to canonical mitochondria-encoded transmembrane subunit COX2 is made of three separate polypeptides encoded in the nucleus, and their correct assembly is a prerequisite for electron transport in the supercomplex. Subunits Cytochrome b and COX1 comprise a +2 frameshift introduced during protein synthesis by the mitoribosome. Among 114 modelled endogenous lipids, we detect a direct contribution to the formation of the divergent supercomplex and its functional sites, including assembly of CII and ubiquinone binding. Together, our findings expose the uniqueness of the principal components of bioenergetics in the mitochondria of parasites.

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Section: Structural Characterisation Of the Ii2-iii2-iv2 Mitochondria...mentioning

confidence: 77%

Structure of the II2-III2-IV2 mitochondrial supercomplex from the parasitePerkinsus marinus

Wú,

Mühleip,

Gruhl

et al. 2024

Preprint

View full text Add to dashboard Cite

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Schizosaccharomyces pombe as a fundamental model for research on mitochondrial gene expression: Progress, achievements and outlooks

Dinh,

Bonnefoy

2023

IUBMB Life

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Schizosaccharomyces pombe (fission yeast) is an attractive model for mitochondrial research. The organism resembles human cells in terms of mitochondrial inheritance, mitochondrial transport, sugar metabolism, mitogenome structure and dependence of viability on the mitogenome (the petite‐negative phenotype). Transcriptions of these genomes produce only a few polycistronic transcripts, which then undergo processing as per the tRNA punctuation model. In general, the machinery for mitochondrial gene expression is structurally and functionally conserved between fission yeast and humans. Furthermore, molecular research on S. pombe is supported by a considerable number of experimental techniques and database resources. Owing to these advantages, fission yeast has significantly contributed to biomedical and fundamental research. Here, we review the current state of knowledge regarding S. pombe mitochondrial gene expression, and emphasise the pertinence of fission yeast as both a model and tool, especially for studies on mitochondrial translation.

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Mitochondrial respiratory supercomplexes of the yeast Saccharomyces cerevisiae

Eldeeb,

Camacho Lopez,

Fontanesi

2024

IUBMB Life

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The functional and structural relationship among the individual components of the mitochondrial respiratory chain constitutes a central aspect of our understanding of aerobic catabolism. This interplay has been a subject of intense debate for over 50 years. It is well established that individual respiratory enzymes associate into higher‐order structures known as respiratory supercomplexes, which represent the evolutionarily conserved organizing principle of the mitochondrial respiratory chain. In the yeast Saccharomyces cerevisiae, supercomplexes are formed by a complex III homodimer flanked by one or two complex IV monomers, and their high‐resolution structures have been recently elucidated. Despite the wealth of structural information, several proposed supercomplex functions remain speculative and our understanding of their physiological relevance is still limited. Recent advances in the field were made possible by the construction of yeast strains where the association of complex III and IV into supercomplexes is impeded, leading to diminished respiratory capacity and compromised cellular competitive fitness. Here, we discuss the experimental evidence and hypotheses relative to the functional roles of yeast respiratory supercomplexes. Moreover, we review the current models of yeast complex III and IV assembly in the context of supercomplex formation and highlight the data scattered throughout the literature suggesting the existence of cross talk between their biogenetic processes.

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Structure and function of theS. pombeIII–IV–cytcsupercomplex

Cited by 5 publications

References 92 publications

Structure of the II2-III2-IV2 mitochondrial supercomplex from the parasitePerkinsus marinus

Structure of the II2-III2-IV2 mitochondrial supercomplex from the parasitePerkinsus marinus

Schizosaccharomyces pombe as a fundamental model for research on mitochondrial gene expression: Progress, achievements and outlooks

Mitochondrial respiratory supercomplexes of the yeast Saccharomyces cerevisiae

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