ArticleBiochimica et biophysica acta2012
The ScoI homologue SenC is a copper binding protein that interacts directly with the cbb₃-type cytochrome oxidase in Rhodobacter capsulatus.
Article in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 40 citations in OpenAlex.
- The Escherichia coli MFS-type transporter genes yhjE, ydiM, and yfcJ are required to produce an active bo3 quinol oxidase.PloS one · 2023Article
- Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- The Response Regulator RegA Is a Copper Binding Protein That Covalently Dimerizes When Exposed to Oxygen.Microorganisms · 2022Article
- The CopA2-Type PFrontiers in microbiology · 2021Article
- Maturation ofFrontiers in microbiology · 2021Article
- Article
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- Comparative differential cuproproteomes of Rhodobacter capsulatus reveal novel copper homeostasis related proteins.Metallomics : integrated biometal science · 2020Article
- Noncompetitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome inThe Journal of biological chemistry · 2019Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Biochemistry of Copper Site Assembly in Heme-Copper Oxidases: A Theme with Variations.International journal of molecular sciences · 2019Review
- The regulation of oxidative phosphorylation pathway on Vibrio alginolyticus adhesion under adversities.MicrobiologyOpen · 2019Article
- The Cu chaperone CopZ is required for Cu homeostasis in Rhodobacter capsulatus and influences cytochrome cbbMolecular microbiology · 2019Article
- Characterization and effect of metal ions on the formation of the Thermus thermophilus Sco mixed disulfide intermediate.Protein science : a publication of the Protein Society · 2018Article
- A Copper Relay System Involving Two Periplasmic Chaperones Drives cbbACS chemical biology · 2018Article
- Methanobactins: Maintaining copper homeostasis in methanotrophs and beyond.The Journal of biological chemistry · 2018Review
- The interaction network of the YidC insertase with the SecYEG translocon, SRP and the SRP receptor FtsY.Scientific reports · 2018Article
- Article
- Copper homeostasis networks in the bacteriumThe Journal of biological chemistry · 2017Article
- Absence of Thiol-Disulfide Oxidoreductase DsbA ImpairsFrontiers in microbiology · 2017Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Sco proteins are widespread assembly factors for the Cu(A) centre of aa₃-type cytochrome oxidases in eukaryotic and prokaryotic organisms. However, Sco homologues are also found in bacteria like Rhodobacter capsulatus which lack aa₃-type cytochrome oxidases and instead use a cbb₃-type cytochrome oxidase (cbb₃ Cox) without a Cu(A) centre as a terminal oxidase. In the current study, we have analyzed the role of Sco (SenC) during cbb₃ Cox assembly in R. capsulatus. In agreement with earlier works, we found a strong cbb₃ Cox defect in the absence of SenC that impairs the steady-state stability of the CcoN, CcoO and CcoP core subunits, without the accumulation of detectable assembly intermediates. In vivo cross-linking results demonstrate that SenC is in close proximity to the CcoP and CcoH subunits of cbb₃ Cox, suggesting that SenC interacts directly with cbb₃ Cox during its assembly. SenC binds copper and the cbb₃ Cox assembly defect in the absence of SenC can be rescued by the addition of least 0.5μM Cu. Neither copper nor SenC influenced the transcription of the ccoNOQP operon encoding for cbb₃ Cox. Transcription of senC itself was also not influenced by Cu unless the putative Cu-export ATPase CcoI was absent. As CcoI is specifically required for the cbb₃ Cox assembly, these data provide a direct link between Cu delivery to cbb₃ Cox and SenC function.
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