ArticleInternational journal of molecular sciences2020
Substitution of the Native Zn(II) with Cd(II), Co(II) and Ni(II) Changes the Downhill Unfolding Mechanism of Ros87 to a Completely Different Scenario.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 15 citations in OpenAlex.
- A Glimpse in the Metal Ion Selectivity Rules: Zn(II), Cd(II) and Co(II) Interplay With Different Protein Coordination Spheres in Determining Variable Thermal Stability and Folding Scenarios.Bioinorganic chemistry and applications · 2026Article
- Platinum Stabilises a Molten-Globule Conformation of a Small Globular Cytosolic Protein SUMO1.Chemistry, an Asian journal · 2025Article
- Circular oligomeric particles formed by Ros/MucR family members mediate DNA organization in α-proteobacteria.Nucleic acids research · 2024Article
- C(P)XCG Proteins ofInternational journal of molecular sciences · 2024Article
- Copper (I) or (II) Replacement of the Structural Zinc Ion in the Prokaryotic Zinc Finger Ros Does Not Result in a Functional Domain.International journal of molecular sciences · 2022Article
- Structural characterization of the thermal unfolding pathway of human VEGFR1 D2 domain.The FEBS journal · 2022Article
- A novel of new class II bacteriocin fromFrontiers in microbiology · 2022Article
- The Physical Chemistry and Chemical Physics (PCCP) Section of theInternational journal of molecular sciences · 2021Article
- Targeting Zinc Finger Proteins with Exogenous Metals and Molecules: Lessons learned from Tristetraprolin, a CCCH type Zinc Finger.European journal of inorganic chemistry · 2021Article
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
The structural effects of zinc replacement by xenobiotic metal ions have been widely studied in several eukaryotic and prokaryotic zinc-finger-containing proteins. The prokaryotic zinc finger, that presents a bigger βββαα domain with a larger hydrophobic core with respect to its eukaryotic counterpart, represents a valuable model protein to study metal ion interaction with metallo-proteins. Several studies have been conducted on Ros87, the DNA binding domain of the prokaryotic zinc finger Ros, and have demonstrated that the domain appears to structurally tolerate Ni(II), albeit with important structural perturbations, but not Pb(II) and Hg(II), and it is in vitro functional when the zinc ion is replaced by Cd(II). We have previously shown that Ros87 unfolding is a two-step process in which a zinc binding intermediate converts to the native structure thorough a delicate downhill folding transition. Here, we explore the folding/unfolding behaviour of Ros87 coordinated to Co(II), Ni(II) or Cd(II), by UV-Vis, CD, DSC and NMR techniques. Interestingly, we show how the substitution of the native metal ion results in complete different folding scenarios. We found a two-state unfolding mechanism for Cd-Ros87 whose metal affinity
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