ArticleJournal of bacteriology2010
The putative assembly factor CcoH is stably associated with the cbb3-type cytochrome oxidase.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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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
19 citing papers in PubMed.
- Functional diversity and molecular interactions of small membrane proteins in bacteria.microLife · 2025Review
- Comparative genomic insights into habitat adaptation of coral-associatedFrontiers in microbiology · 2023Article
- Cryo-EM structures of engineered active bcNature communications · 2021Article
- The CopA2-Type PFrontiers in microbiology · 2021Article
- Genes Linking Copper Trafficking and Homeostasis to the Biogenesis and Activity of theFrontiers in microbiology · 2021Article
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- TheProceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Cu chaperone CopZ is required for Cu homeostasis in Rhodobacter capsulatus and influences cytochrome cbbMolecular microbiology · 2019Article
- A Copper Relay System Involving Two Periplasmic Chaperones Drives cbbACS chemical biology · 2018Article
- Biogenesis of the bacterialThe Journal of biological chemistry · 2018Article
- Cooperation between two periplasmic copper chaperones is required for full activity of the cbb3 -type cytochrome c oxidase and copper homeostasis in Rhodobacter capsulatus.Molecular microbiology · 2016Article
- Article
- The two transmembrane helices of CcoP are sufficient for assembly of the cbb3-type heme-copper oxygen reductase from Vibrio cholerae.Biochimica et biophysica acta · 2015Article
- Missense mutations in cytochrome c maturation genes provide new insights into Rhodobacter capsulatus cbb3-type cytochrome c oxidase biogenesis.Journal of bacteriology · 2013Article
- The ScoI homologue SenC is a copper binding protein that interacts directly with the cbb₃-type cytochrome oxidase in Rhodobacter capsulatus.Biochimica et biophysica acta · 2012Article
- Biogenesis of cbb(3)-type cytochrome c oxidase in Rhodobacter capsulatus.Biochimica et biophysica acta · 2012Review
- The roles of Rhodobacter sphaeroides copper chaperones PCu(A)C and Sco (PrrC) in the assembly of the copper centers of the aa(3)-type and the cbb(3)-type cytochrome c oxidases.Biochimica et biophysica acta · 2012Article
- Bacterial adaptation of respiration from oxic to microoxic and anoxic conditions: redox control.Antioxidants & redox signaling · 2012Review
- Article
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Authors and funding
8 authors.
Funding
Abstract
Cytochrome oxidases are perfect model substrates for analyzing the assembly of multisubunit complexes because the need for cofactor incorporation adds an additional level of complexity to their assembly. cbb(3)-type cytochrome c oxidases (cbb(3)-Cox) consist of the catalytic subunit CcoN, the membrane-bound c-type cytochrome subunits CcoO and CcoP, and the CcoQ subunit, which is required for cbb(3)-Cox stability. Biogenesis of cbb(3)-Cox proceeds via CcoQP and CcoNO subcomplexes, which assemble into the active cbb(3)-Cox. Most bacteria expressing cbb(3)-Cox also contain the ccoGHIS genes, which encode putative cbb(3)-Cox assembly factors. Their exact function, however, has remained unknown. Here we analyzed the role of CcoH in cbb(3)-Cox assembly and showed that CcoH is a single spanning-membrane protein with an N-terminus-out-C-terminus-in (N(out)-C(in)) topology. In its absence, neither the fully assembled cbb(3)-Cox nor the CcoQP or CcoNO subcomplex was detectable. By chemical cross-linking, we demonstrated that CcoH binds primarily via its transmembrane domain to the CcoP subunit of cbb(3)-Cox. A second hydrophobic stretch, which is located at the C terminus of CcoH, appears not to be required for contacting CcoP, but deleting it prevents the formation of the active cbb(3)-Cox. This suggests that the second hydrophobic domain is required for merging the CcoNO and CcoPQ subcomplexes into the active cbb(3)-Cox. Surprisingly, CcoH does not seem to interact only transiently with the cbb(3)-Cox but appears to stay tightly associated with the active, fully assembled complex. Thus, CcoH behaves more like a bona fide subunit of the cbb(3)-Cox than an assembly factor per se.
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