Copper binding in IscA inhibits iron‐sulphur cluster assembly in E scherichia coli
Open accessAbstract
Among the iron-sulphur cluster assembly proteins encoded by gene cluster iscSUA-hscBA-fdx in Escherichia coli, IscA has a unique and strong iron binding activity and can provide iron for iron-sulphur cluster assembly in proteins in vitro. Deletion of IscA and its paralogue SufA results in an E. coli mutant that fails to assemble [4Fe-4S] clusters in proteins under aerobic conditions, suggesting that IscA has a crucial role for iron-sulphur cluster biogenesis. Here we report that among the iron-sulphur cluster assembly proteins, IscA also has a strong and specific binding activity for Cu(I) in vivo and in vitro. The Cu(I) centre in IscA is stable and resistant to oxidation under aerobic conditions. Mutation of the conserved cysteine residues that are essential for the iron binding in IscA abolishes the copper binding activity, indicating that copper and iron may share the same binding site in the protein. Additional studies reveal that copper can compete with iron for the metal binding site in IscA and effectively inhibits the IscA-mediated [4Fe-4S] cluster assembly in E. coli cells. The results suggest that copper may not only attack the [4Fe-4S] clusters in dehydratases, but also block the [4Fe-4S] cluster assembly in proteins by targeting IscA in cells.
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To counteract mis-metalation, bacteria can induce the expression of metallochaperones that have higher specificity for cognate partners such as SufA in E. coli.
“To counteract mis- metalation, bacteria can induce the expression of metallochaperones that have higher specificity for cognate partners such as SufA in E. coli 151-153 .”
From Nutritional immunity: the battle for nutrient metals at the host–pathogen interface (2022) · cites this paper as [153]
The Discussion reports that CuSO4 induced expression of the sufA::lacZ operon in E. coli, supporting the induction part of the claim. It does not establish that SufA is a metallochaperone with higher specificity for cognate partners or that its induction counteracts mis-metalation. The Results instead report that SufA binds copper similarly to IscA. (LLM, conf=0.86)
Experimental — accuracy not yet measuredIn E. coli, part of this copper toxicity comes from copper binding to the FeS cluster assembly protein IscA and blocking FeS assembly.
“that in E. coli is mediated in part through binding to FeS cluster assembly protein IscA and inhibiting FeS assembly (Tan et al., 2014)”
From The Impact of Dietary Transition Metals on Host-Bacterial Interactions (2018) · cites this paper as Tan et al., 2014
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- Authors
- Tan, G., Cheng, Z., Pang, Y., Landry, A. P., Li, J., Lu, J., & Ding, H.
- Affiliations
- Louisiana State University (US)
- Wenzhou Medical University (CN)
- Laboratory of Molecular Medicine, School of Laboratory Medicine and Life Science Wenzhou Medical University Wenzhou Zhejiang 325035 China
- Corresponding author
- Ding, Huangen
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2014-07-08
- Volume
- 93
- Issue
- 4
- Pages
- 629-644
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- PMC
- PMC4132641
- OpenAlex
- W1959259592
- Cited by
- 103
- References
- 72
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 9 · 2023: 9 · 2022: 8 · 2021: 26 · 2020: 7 · 2019: 6 · 2018: 5 · 2017: 5 · 2016: 3 · 2015: 2 · 2014: 3
- FWCI
- 1.43
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Civil War Book Review (submittedVersion)
- Funders
- National Institutes of Health (CA107494)
- Chinese National Natural Science Foundation Grants (31228006, 31200587, 31100576)
- Key Science and Technology Innovation Team of Zhejiang Province (2010R50048-14)
- Natural Science Foundation of Zhejiang Province Grant (LY12C05003)
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- Isca, copper binding, [4Fe-4S] cluster, Escherichia coli, SufA, metal binding sites, iron binding, cysteine residues, metallochaperone, dehydratase
- MeSH terms
- Binding Sites, Carrier Proteins, Copper, DNA Mutational Analysis, Escherichia coli, Iron, Iron-Sulfur Proteins, Protein Binding, Mutagenesis, Site-Directed, Amino Acid Substitution, Escherichia coli Proteins
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