ArticleThe Journal of biological chemistry2012
Copper starvation-inducible protein for cytochrome oxidase biogenesis in Bradyrhizobium japonicum.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- AccA fromChemical science · 2026Article
- A new family of TonB-dependent copper transporters linked to respiratory oxidase function.The Journal of biological chemistry · 2026Article
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- The copper-responsive regulator CsoR is indirectly involved in Bradyrhizobium diazoefficiens denitrification.FEMS microbiology letters · 2023Article
- Article
- Effect of Copper on Expression of Functional Genes and Proteins Associated withInternational journal of molecular sciences · 2022Article
- Nodulating white lupins take advantage of the reciprocal interplay between N and P nutritional responses.Physiologia plantarum · 2022Article
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- PCuThe Journal of biological chemistry · 2019Article
- Biochemistry of Copper Site Assembly in Heme-Copper Oxidases: A Theme with Variations.International journal of molecular sciences · 2019Review
- Structural basis and mechanism for metallochaperone-assisted assembly of the CuScience advances · 2019Article
- An Integrated Systems Approach Unveils New Aspects of Microoxia-Mediated Regulation inFrontiers in microbiology · 2019Article
- A Copper Relay System Involving Two Periplasmic Chaperones Drives cbbACS chemical biology · 2018Article
- Methanobactins: from genome to function.Metallomics : integrated biometal science · 2017Review
- Copper-responsive gene expression in the methanotroph Methylosinus trichosporium OB3b.Metallomics : integrated biometal science · 2016Article
- The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins.Biochemistry · 2016Article
- 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
- Transcriptomic profiling of Methylococcus capsulatus (Bath) during growth with two different methane monooxygenases.MicrobiologyOpen · 2016Article
- How periplasmic thioredoxin TlpA reduces bacterial copper chaperone ScoI and cytochrome oxidase subunit II (CoxB) prior to metallation.The Journal of biological chemistry · 2014Article
- A bacterial iron exporter for maintenance of iron homeostasis.The Journal of biological chemistry · 2014Article
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microarray analysis of Bradyrhizobium japonicum grown under copper limitation uncovered five genes named pcuABCDE, which are co-transcribed and co-regulated as an operon. The predicted gene products are periplasmic proteins (PcuA, PcuC, and PcuD), a TonB-dependent outer membrane receptor (PcuB), and a cytoplasmic membrane-integral protein (PcuE). Homologs of PcuC and PcuE had been discovered in other bacteria, namely PCu(A)C and YcnJ, where they play a role in cytochrome oxidase biogenesis and copper transport, respectively. Deletion of the pcuABCDE operon led to a pleiotropic phenotype, including defects in the aa(3)-type cytochrome oxidase, symbiotic nitrogen fixation, and anoxic nitrate respiration. Complementation analyses revealed that, under our assay conditions, the tested functions depended only on the pcuC gene and not on pcuA, pcuB, pcuD, or pcuE. The B. japonicum genome harbors a second pcuC-like gene (blr7088), which, however, did not functionally replace the mutated pcuC. The PcuC protein was overexpressed in Escherichia coli, purified to homogeneity, and shown to bind Cu(I) with high affinity in a 1:1 stoichiometry. The replacement of His(79), Met(90), His(113), and Met(115) by alanine perturbed copper binding. This corroborates the previously purported role of this protein as a periplasmic copper chaperone for the formation of the Cu(A) center on the aa(3)-type cytochrome oxidase. In addition, we provide evidence that PcuC and the copper chaperone ScoI are important for the symbiotically essential, Cu(A)-free cbb(3)-type cytochrome oxidase specifically in endosymbiotic bacteroids of soybean root nodules, which could explain the symbiosis-defective phenotype of the pcuC and scoI mutants.
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