ArticleJournal of bacteriology2013
The Escherichia coli CydX protein is a member of the CydAB cytochrome bd oxidase complex and is required for cytochrome bd oxidase activity.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 105 citations in OpenAlex.
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- Functional analysis and transcriptional profiling of non-coding RNAs in yeast.The Biochemical journal · 2025Review
- PIRT-Seq: a high-resolution whole-genome assay to identify protein-coding genes.Nucleic acids research · 2025Article
- Cellular function of the GndA microprotein during heat shock.bioRxiv : the preprint server for biology · 2025Article
- Complementary Ribo-seq approaches map the translatome and provide a small protein census in the foodborne pathogen Campylobacter jejuni.Nature communications · 2025Article
- Insights into the diverse roles of the terminal oxidases in Burkholderia cenocepacia H111.Scientific reports · 2025Article
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- Defects in the central metabolism prevent thymineless death in Escherichia coli, while still allowing significant protein synthesis.Genetics · 2024Article
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- A catalog of small proteins from the global microbiome.Nature communications · 2024Article
- Anaerobiosis, a neglected factor in phage-bacteria interactions.Applied and environmental microbiology · 2023Article
- Microproteins-Discovery, structure, and function.Proteomics · 2023Review
- Enhancement of acid tolerance of Escherichia coli by introduction of molecule chaperone CbpA from extremophile.World journal of microbiology & biotechnology · 2023Article
- A Small Non-Coding RNA Mediates Transcript Stability and Expression of Cytochrome bd Ubiquinol Oxidase Subunit I inInternational journal of molecular sciences · 2023Article
- Metagenomic evidence of a novel family of anammox bacteria in a subsea environment.Environmental microbiology · 2022Article
- Identification of Key Factors for Anoxic Survival ofInternational journal of molecular sciences · 2022Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Cytochrome bd oxidase operons from more than 50 species of bacteria contain a short gene encoding a small protein that ranges from ∼30 to 50 amino acids and is predicted to localize to the cell membrane. Although cytochrome bd oxidases have been studied for more than 70 years, little is known about the role of this small protein, denoted CydX, in oxidase activity. Here we report that Escherichia coli mutants lacking CydX exhibit phenotypes associated with reduced oxidase activity. In addition, cell membrane extracts from ΔcydX mutant strains have reduced oxidase activity in vitro. Consistent with data showing that CydX is required for cytochrome bd oxidase activity, copurification experiments indicate that CydX interacts with the CydAB cytochrome bd oxidase complex. Together, these data support the hypothesis that CydX is a subunit of the CydAB cytochrome bd oxidase complex that is required for complex activity. The results of mutation analysis of CydX suggest that few individual amino acids in the small protein are essential for function, at least in the context of protein overexpression. In addition, the results of analysis of the paralogous small transmembrane protein AppX show that the two proteins could have some overlapping functionality in the cell and that both have the potential to interact with the CydAB complex.
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