ArticleThe Journal of biological chemistry2014
Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic chaperones: the interaction of Escherichia coli CopA and CusF.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 86 citations in OpenAlex.
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- Operonic architecture of bacterial metal response: envelope constraints, evolutionary mobility, and bioremediation design rules.World journal of microbiology & biotechnology · 2026Review
- Navigating the copper highway: bacterial strategies for cytoplasmic import.Journal of inorganic biochemistry · 2026Review
- Systematic and synthetic biology insights into copper homeostasis in Escherichia coli.iScience · 2025Article
- The exploitation of nutrient metals by bacteria for survival and infection in the gut.PLoS pathogens · 2025Review
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Linking the transcriptome to physiology: response of the proteome of Cupriavidus metallidurans to changing metal availability.Metallomics : integrated biometal science · 2024Article
- Cysteine Rich Intestinal Protein 2 is a copper-responsive regulator of skeletal muscle differentiation and metal homeostasis.PLoS genetics · 2024Article
- Metalation of Extracytoplasmic Proteins and Bacterial Cell Envelope Homeostasis.Annual review of microbiology · 2024Review
- Cysteine Rich Intestinal Protein 2 is a copper-responsive regulator of skeletal muscle differentiation.bioRxiv : the preprint server for biology · 2024Article
- Draft Genome Sequence ofEvolutionary bioinformatics online · 2024Article
- Sequence-based Functional Metagenomics Reveals Novel Natural Diversity of Functional CopA in Environmental Microbiomes.Genomics, proteomics & bioinformatics · 2023Article
- Full Copper Resistance in Cupriavidus metallidurans Requires the Interplay of Many Resistance Systems.Applied and environmental microbiology · 2023Article
- Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- Periplasmic oxidized-protein repair during copper stress in E. coli: A focus on the metallochaperone CusF.PLoS genetics · 2022Article
- Aggregates Sealed by Ions.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The mitochondrial CuFrontiers in molecular biosciences · 2022Article
- Copper Homeostatic Mechanisms and Their Role in the Virulence of Escherichia coli and Salmonella enterica.EcoSal Plus · 2021Review
- Membrane Transporters Involved in the Antimicrobial Activities of Pyrithione inMolecules (Basel, Switzerland) · 2021Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Cellular copper homeostasis requires transmembrane transport and compartmental trafficking while maintaining the cell essentially free of uncomplexed Cu(2+/+). In bacteria, soluble cytoplasmic and periplasmic chaperones bind and deliver Cu(+) to target transporters or metalloenzymes. Transmembrane Cu(+)-ATPases couple the hydrolysis of ATP to the efflux of cytoplasmic Cu(+). Cytosolic Cu(+) chaperones (CopZ) interact with a structural platform in Cu(+)-ATPases (CopA) and deliver copper into the ion permeation path. CusF is a periplasmic Cu(+) chaperone that supplies Cu(+) to the CusCBA system for efflux to the extracellular milieu. In this report, using Escherichia coli CopA and CusF, direct Cu(+) transfer from the ATPase to the periplasmic chaperone was observed. This required the specific interaction of the Cu(+)-bound form of CopA with apo-CusF for subsequent metal transfer upon ATP hydrolysis. As expected, the reverse Cu(+) transfer from CusF to CopA was not observed. Mutation of CopA extracellular loops or the electropositive surface of CusF led to a decrease in Cu(+) transfer efficiency. On the other hand, mutation of Met and Glu residues proposed to be part of the metal exit site in the ATPase yielded enzymes with lower turnover rates, although Cu(+) transfer was minimally affected. These results show how soluble chaperones obtain Cu(+) from transmembrane transporters. Furthermore, by explaining the movement of Cu(+) from the cytoplasmic pool to the extracellular milieu, these data support a mechanism by which cytoplasmic Cu(+) can be precisely directed to periplasmic targets via specific transporter-chaperone interactions.
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