ArticleBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine2011
Escherichia coli topoisomerase I is an iron and zinc binding protein.
Article in Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 12 citations in OpenAlex.
- Temperature-Controlled Hybrid Hydrogels for Reversible and Selective Zinc(II) Removal from Minimal Culture Media.ACS omega · 2026Article
- Article
- Research progress on gut microbiota in patients with gastric cancer, esophageal cancer, and small intestine cancer.Applied microbiology and biotechnology · 2021Review
- Zinc Toxicity and Iron-Sulfur Cluster Biogenesis inApplied and environmental microbiology · 2019Article
- Inhibition of Zn(II) binding type IA topoisomerases by organomercury compounds and Hg(II).PloS one · 2015Article
- Iron inhibits Escherichia coli topoisomerase I activity by targeting the first two zinc-binding sites in the C-terminal domain.Protein science : a publication of the Protein Society · 2014Article
- Iron and zinc binding activity of Escherichia coli topoisomerase I homolog YrdD.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2014Article
- Iron chelators with topoisomerase-inhibitory activity and their anticancer applications.Antioxidants & redox signaling · 2013Review
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Escherichia coli topoisomerase I (TopA) cleaves and rejoins one strand of double-stranded DNA to relax the negatively supercoiled DNA. Structurally, TopA contains an N-terminal catalytic fragment and a C-terminal zinc-binding region that is required for relaxation of the negatively supercoiled DNA. Here we report that E. coli TopA is an iron and zinc binding protein. The UV-Vis absorption measurements and metal content analyses reveal that TopA purified from E. coli cells grown in the rich LB medium contains both iron and zinc. However, TopA purified from E. coli cells grown in the M9 minimal medium has negligible amounts of zinc or iron and no topoisomerase activity. Nevertheless, supplement of exogenous zinc or iron in E. coli cells grown in the M9 minimal medium produces the zinc- or iron-bound TopA, respectively. Whereas the zinc-bound TopA is fully active to relax the negatively supercoiled DNA, the iron-bound TopA has little or no enzyme activity. Furthermore, excess iron in the M9 minimal medium is able to compete with the zinc binding in TopA in E. coli cells and attenuate the topoisomerase activity, suggesting that E. coli TopA may be modulated by iron and zinc binding in vivo.
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