ArticleThe EMBO journal1997
Subunit change in cytochrome c oxidase: identification of the oxygen switch in Dictyostelium.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 18 citations in OpenAlex.
- Global characterization of Dictyostelium discoideum gene and protein expression changes under hypoxic conditions.BMC genomics · 2025Article
- Dictyostelium discoideum chemotaxis is altered by hypoxia to orient streaming toward higher oxygen levels.BMC molecular and cell biology · 2025Article
- The aerotaxis ofFrontiers in cell and developmental biology · 2023Article
- Classical and alternative components of the mitochondrial respiratory chain in pathogenic fungi as potential therapeutic targets.Journal of bioenergetics and biomembranes · 2011Review
- Large scale physiological readjustment during growth enables rapid, comprehensive and inexpensive systems analysis.BMC systems biology · 2010Article
- Extending the models for iron and sulfur oxidation in the extreme acidophile Acidithiobacillus ferrooxidans.BMC genomics · 2009Article
- Regulation of energy transduction and electron transfer in cytochrome c oxidase by adenine nucleotides.Journal of bioenergetics and biomembranes · 1998Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytochrome c oxidase (COX) has a complex modular structure in eukaryotes. Depending on growth conditions, interchangeable isoforms of selected subunits are synthesized and combined to the evolutionarily conserved catalytic core of the enzyme. In Dictyostelium this structural make-up is regulated by oxygen and involves two forms of the smallest subunit, termed VIIe and VIIs. Here we show that, in spite of a considerable sequence divergency, they are encoded by adjacent genes, linked 'tail to head' by only 800 bp. Deletion analyses reveal the presence of a short intergenic segment acting as an oxygen transcriptional switch. This structural organization and the different stability of the two subunit isoforms offer a molecular explanation for the extraordinary sensitivity to oxygen of the switching mechanism.
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Registered trials
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