ArticlePLoS genetics2022
Periplasmic oxidized-protein repair during copper stress in E. coli: A focus on the metallochaperone CusF.
Article in PLoS genetics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
9 citing papers in PubMed, 18 citations in OpenAlex.
- Operonic architecture of bacterial metal response: envelope constraints, evolutionary mobility, and bioremediation design rules.World journal of microbiology & biotechnology · 2026Review
- A short peptide derived from late embryogenesis abundant proteins enhances acid tolerance in Escherichia coli via modulation of two-component regulatory systems.The FEBS journal · 2026Article
- Copper stress upregulates oxidative stress response, histidine production, and iron acquisition genes inFEMS microbes · 2026Article
- Systematic and synthetic biology insights into copper homeostasis in Escherichia coli.iScience · 2025Article
- Role of the Multicopper Oxidase CueO in Copper Homeostasis Under Anaerobic Conditions in Enterobacteria.Molecular microbiology · 2025Article
- Beyond anaerobic respiration-new physiological roles for DmsABC and other S-/N-oxide reductases inJournal of bacteriology · 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
- Thioredoxin TRXo1 is involved in ABA perception via PYR1 redox regulation.Redox biology · 2023Article
- Correction: Periplasmic oxidized-protein repair during copper stress in E. coli: A focus on the metallochaperone CusF.PLoS genetics · 2022Article
Corrections and comments
- Erratum issued
Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methionine residues are particularly sensitive to oxidation by reactive oxygen or chlorine species (ROS/RCS), leading to the appearance of methionine sulfoxide in proteins. This post-translational oxidation can be reversed by omnipresent protein repair pathways involving methionine sulfoxide reductases (Msr). In the periplasm of Escherichia coli, the enzymatic system MsrPQ, whose expression is triggered by the RCS, controls the redox status of methionine residues. Here we report that MsrPQ synthesis is also induced by copper stress via the CusSR two-component system, and that MsrPQ plays a role in copper homeostasis by maintaining the activity of the copper efflux pump, CusCFBA. Genetic and biochemical evidence suggest the metallochaperone CusF is the substrate of MsrPQ and our study reveals that CusF methionines are redox sensitive and can be restored by MsrPQ. Thus, the evolution of a CusSR-dependent synthesis of MsrPQ allows conservation of copper homeostasis under aerobic conditions by maintenance of the reduced state of Met residues in copper-trafficking proteins.
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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.