ArticleBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine2014
Iron and zinc binding activity of Escherichia coli topoisomerase I homolog YrdD.
Article in Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- Zinc Toxicity and Iron-Sulfur Cluster Biogenesis inApplied and environmental microbiology · 2019Article
- Structural basis for suppression of hypernegative DNA supercoiling by E. coli topoisomerase I.Nucleic acids research · 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
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
YrdD, a homolog of the C-terminal zinc-binding region of Escherichia coli topoisomerase I, is highly conserved among proteobacteria and enterobacteria. However, the function of YrdD remains elusive. Here we report that YrdD purified from E. coli cells grown in LB media contains both zinc and iron. Supplement of exogenous zinc in the medium abolishes the iron binding of YrdD in E. coli cells, indicating that iron and zinc may compete for the same metal binding sites in the protein. While the zinc-bound YrdD is able to bind single-stranded (ss) DNA and protect ssDNA from the DNase I digestion in vitro, the iron-bound YrdD has very little or no binding activity for ssDNA, suggesting that the zinc-bound YrdD may have an important role in DNA repair by interacting with ssDNA in cells.
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Registered trials
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