ArticleThe Journal of biological chemistry2009
Chaperone-mediated Cu+ delivery to Cu+ transport ATPases: requirement of nucleotide binding.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 58 citations in OpenAlex.
- Effluxosomes and the evolution of metal resistance inInfection and immunity · 2026Review
- Transition metal transporting P-type ATPases: terminal metal-binding domains serve as sensors for autoinhibitory tails.The FEBS journal · 2025Article
- Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- The CopA2-Type PFrontiers in microbiology · 2021Article
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- An important role for periplasmic storage in Pseudomonas aeruginosa copper homeostasis revealed by a combined experimental and computational modeling study.Molecular microbiology · 2018Article
- Metal Selectivity of a Cd-, Co-, and Zn-Transporting PBiochemistry · 2017Article
- Bacterial Cu(+)-ATPases: models for molecular structure-function studies.Metallomics : integrated biometal science · 2016Review
- A sulfur-based transport pathway in Cu+-ATPases.EMBO reports · 2015Article
- Biochemical characterization of P-type copper ATPases.The Biochemical journal · 2014Review
- Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic chaperones: the interaction of Escherichia coli CopA and CusF.The Journal of biological chemistry · 2014Article
- Genome-wide analysis of copper, iron and zinc transporters in the arbuscular mycorrhizal fungus Rhizophagus irregularis.Frontiers in plant science · 2014Article
- Sinorhizobium meliloti Nia is a P(1B-5)-ATPase expressed in the nodule during plant symbiosis and is involved in Ni and Fe transport.Metallomics : integrated biometal science · 2013Article
- An expanding range of functions for the copper chaperone/antioxidant protein Atox1.Antioxidants & redox signaling · 2013Review
- The mechanism of Cu+ transport ATPases: interaction with CU+ chaperones and the role of transient metal-binding sites.The Journal of biological chemistry · 2013Article
- Mechanisms of copper homeostasis in bacteria.Frontiers in cellular and infection microbiology · 2013Article
- Characterization of a cobalt-specific P(1B)-ATPase.Biochemistry · 2012Article
- Biogenesis of cbb(3)-type cytochrome c oxidase in Rhodobacter capsulatus.Biochimica et biophysica acta · 2012Review
- Metal transport across biomembranes: emerging models for a distinct chemistry.The Journal of biological chemistry · 2012Review
- Toward a molecular understanding of metal transport by P(1B)-type ATPases.Current topics in membranes · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cu(+)-ATPases drive the efflux of Cu(+) from the cell cytoplasm. During their catalytic/transport cycle, cytoplasmic Cu(+)-chaperones deliver the metal to the two transmembrane metal-binding sites (TM-MBSs) responsible for Cu(+) translocation. Here, using Archaeoglobus fulgidus Cu(+)-ATPase CopA and the C-terminal Cu(+)-chaperone domain of CopZ (Ct-CopZ), we describe the mechanism of Cu(+) transfer to both TM-MBSs. In absence of other ligands, Ct-CopZ transfers Cu(+) to wild-type CopA and to various CopA constructs lacking or having mutated cytoplasmic metal-binding domains, in a fashion consistent with occupancy of a single TM-MBS. Similar experiments performed in the presence of 2.5 mm ADP-Mg(2+), stabilizing an E1.ADP, lead to full occupancy of both TM-MBSs. In both cases, the transfer is largely stoichiometric, i.e. equimolar amounts of Ct-CopZ.Cu(+) saturated the TM-MBSs. Experiments performed with CopA mutants lacking either TM-MBS showed that both sites are loaded independently, and nucleotide binding does not affect their availability. The nucleotide-induced E2-->E1 transition is structurally characterized by a large displacement of the A and N domains opening the cytoplasmic region of P-type ATPases. Then, it is apparent that, whereas the first Cu(+)-chaperone can bind an ATPase form available in the absence of ligands, the second requires the E1.nucleotide intermediary to interact and deliver the metal. Interestingly, independent of TM-MBS Cu(+) loading, nucleotide binding also prevents the regulatory interaction of the N-terminal cytoplasmic metal-binding domain with the nucleotide binding domain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.