Abstract
Respiratory chain complexes execute energy conversion by connecting electron transport with proton translocation over the inner mitochondrial membrane to fuel ATP synthesis. Notably, these complexes form multi-enzyme assemblies known as respiratory supercomplexes. Here we used single-particle cryo-EM to determine the structures of the yeast mitochondrial respiratory supercomplexes III2IV and III2IV2, at 3.2-Ã… and 3.5-Ã… resolutions, respectively. We revealed the overall architecture of the supercomplex, which deviates from the previously determined assemblies in mammals; obtained a near-atomic structure of the yeast complex IV; and identified the protein-protein and protein-lipid interactions implicated in supercomplex formation. Take together, our results demonstrate convergent evolution of supercomplexes in mitochondria that, while building similar assemblies, results in substantially different arrangements and structural solutions to support energy conversion.
🔬 Techniques
✨ Fluorophores
🧪 Sample Preparation
🔬 Cell Lines
🏛️ Research Organizations (ROR)
Affiliated research institutions:
📊 Figures
Figure 1.
Schematic illustration of the proposed interactions of Au03b2 with mitochondrial components and their effects on OXPHOS function. Amyloid precursor protein (APP) and its secretase complex processing p...
Figure 2.
Schematic illustration of the proposed interactions of u03b1-syn with mitochondrial components and their effects on OXPHOS function. u03b1-Synuclein monomers and oligomers can affect mitochondrial imp...
Figure 3.
Schematic illustration of the proposed interactions of SOD1 with mitochondrial components and their effects on OXPHOS function. SOD1 localizes to mitochondria, where it provides dismutase activity in ...
Figure images are served from the NIH/NLM PubMed Central Open Access Subset or Europe PMC; copyright remains with the publishers and authors.
💬 Discussion
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