ArticleEMBO reports2022
CG7630 is the Drosophila melanogaster homolog of the cytochrome c oxidase subunit COX7B.
Article in EMBO reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 14 citations in OpenAlex.
- Structural rather than catalytic role for mitochondrial respiratory chain supercomplexes.eLife · 2023Article
- Comparative Clustering (CompaCt) of eukaryote complexomes identifies novel interactions and sheds light on protein complex evolution.PLoS computational biology · 2023Article
- Mitochondrial Neurodegeneration: Lessons fromBiomolecules · 2023Review
- COX7B Is a New Prognostic Biomarker and Correlates with Tumor Immunity in Esophageal Carcinoma.Mediators of inflammation · 2023Article
- CG7630 is the Drosophila melanogaster homolog of the cytochrome c oxidase subunit COX7B.EMBO reports · 2022Article
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Authors and funding
11 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mitochondrial respiratory chain (MRC) is composed of four multiheteromeric enzyme complexes. According to the endosymbiotic origin of mitochondria, eukaryotic MRC derives from ancestral proteobacterial respiratory structures consisting of a minimal set of complexes formed by a few subunits associated with redox prosthetic groups. These enzymes, which are the "core" redox centers of respiration, acquired additional subunits, and increased their complexity throughout evolution. Cytochrome c oxidase (COX), the terminal component of MRC, has a highly interspecific heterogeneous composition. Mammalian COX consists of 14 different polypeptides, of which COX7B is considered the evolutionarily youngest subunit. We applied proteomic, biochemical, and genetic approaches to investigate the COX composition in the invertebrate model Drosophila melanogaster. We identified and characterized a novel subunit which is widely different in amino acid sequence, but similar in secondary and tertiary structures to COX7B, and provided evidence that this object is in fact replacing the latter subunit in virtually all protostome invertebrates. These results demonstrate that although individual structures may differ the composition of COX is functionally conserved between vertebrate and invertebrate species.
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Registered trials
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