ArticleThe Journal of biological chemistry2016
The Tat Substrate CueO Is Transported in an Incomplete Folding State.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 41 citations in OpenAlex.
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- Role of the Multicopper Oxidase CueO in Copper Homeostasis Under Anaerobic Conditions in Enterobacteria.Molecular microbiology · 2025Article
- Regulatory Characterization of Two Cop Systems for Copper Resistance inInternational journal of molecular sciences · 2025Article
- Methionine-rich domains emerge as facilitators of copper recruitment in detoxification systems.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A gold speciation that adds a second layer to synergistic gold-copper toxicity inApplied and environmental microbiology · 2024Article
- Positive charges promote the recognition of proteins by the chaperone SlyD from Escherichia coli.PloS one · 2024Article
- Identification of novel small molecule inhibitors of twin arginine translocation (Tat) pathway and their effect on the control ofFrontiers in microbiology · 2024Article
- Full Copper Resistance in Cupriavidus metallidurans Requires the Interplay of Many Resistance Systems.Applied and environmental microbiology · 2023Article
- Article
- Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- Molecular regulation of conditioning film formation and quorum quenching in sulfate reducing bacteria.Frontiers in microbiology · 2022Review
- Copper delivery to an endospore coat protein ofFrontiers in cell and developmental biology · 2022Article
- Copper Homeostatic Mechanisms and Their Role in the Virulence of Escherichia coli and Salmonella enterica.EcoSal Plus · 2021Review
- Use of Copper as a Trigger for the in Vivo Activity of E. coli Laccase CueO: A Simple Tool for Biosynthetic Purposes.Chembiochem : a European journal of chemical biology · 2021Article
- Twin-arginine translocation (Tat) mutants inFEMS microbes · 2021Article
- Maturation ofFrontiers in microbiology · 2021Article
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- Cytosolic Copper Binding by a Bacterial Storage Protein and Interplay with Copper Efflux.International journal of molecular sciences · 2019Article
- Transport of Folded Proteins by the Tat System.The protein journal · 2019Review
- The Twin-Arginine Pathway for Protein Secretion.EcoSal Plus · 2019Review
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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
In Escherichia coli, cytoplasmic copper ions are toxic to cells even at the lowest concentrations. As a defense strategy, the cuprous oxidase CueO is secreted into the periplasm to oxidize the more membrane-permeable and toxic Cu(I) before it can enter the cytoplasm. CueO itself is a multicopper oxidase that requires copper for activity. Because it is transported by the twin-arginine translocation (Tat) pathway, which transports folded proteins, a requirement for cofactor assembly before translocation has been discussed. Here we show that CueO is transported as an apo-protein. Periplasmic CueO was readily activated by the addition of copper ions in vitro or under copper stress conditions in vivo Cytoplasmic CueO did not contain copper, even under copper stress conditions. In vitro Tat transport proved that the cofactor assembly was not required for functional Tat transport of CueO. Due to the post-translocational activation of CueO, this enzyme contributes to copper resistance not only by its cuprous oxidase activity but also by chelation of copper ions before they can enter the cytoplasm. Apo-CueO was indistinguishable from holo-CueO in terms of secondary structural elements. Importantly, the binding of copper to apo-CueO greatly stabilized the protein, indicating a transformation from an open or flexible domain arrangement with accessible copper sites to a closed structure with deeply buried copper ions. CueO is thus the first example for a natural Tat substrate of such incomplete folding state. The Tat system may need to transport flexibly folded proteins in any case when cofactor assembly or quaternary structure formation occurs after transport.
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