ArticleProceedings of the National Academy of Sciences of the United States of America2009
The structural role of the zinc ion can be dispensable in prokaryotic zinc-finger domains.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 61 citations in OpenAlex.
- Identifying Two New Ros/MucR Proteins: An Atypical Structure with a Divergent Function.Biomolecules · 2026Article
- 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
- Cyclic-di-GMP interferes with DNA-MucR-DNA bridging to derepress genes targeted by the xenogeneic silencer MucR.Nucleic acids research · 2025Article
- OptimizedInternational journal of molecular sciences · 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
- The role of zinc in the premature brain: functions, outcomes and future research perspectives.Frontiers in pediatrics · 2024Review
- MucR fromInternational journal of molecular sciences · 2023Article
- Characterization of the zinc finger μ-protein HVO_0758 fromFrontiers in microbiology · 2023Article
- The Ros/MucR Zinc-Finger Protein Family in Bacteria: Structure and Functions.International journal of molecular sciences · 2022Review
- Resolving the zinc binding capacity of honey bee vitellogenin and locating its putative binding sites.Insect molecular biology · 2022Article
- 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
- The convergent xenogeneic silencer MucR predisposes α-proteobacteria to integrate AT-rich symbiosis genes.Nucleic acids research · 2022Article
- The zinc-finger bearing xenogeneic silencer MucR in α-proteobacteria balances adaptation and regulatory integrity.The ISME journal · 2022Article
- Article
- Structure and Function ofACS omega · 2020Article
- The change of conditions does not affect Ros87 downhill folding mechanism.Scientific reports · 2020Article
- 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.International journal of molecular sciences · 2020Article
- Arsenite Exposure Displaces Zinc from ZRANB2 Leading to Altered Splicing.Chemical research in toxicology · 2020Article
- Structural Insight of the Full-Length Ros Protein: A Prototype of the Prokaryotic Zinc-Finger Family.Scientific reports · 2020Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The recent characterization of the prokaryotic Cys(2)His(2) zinc-finger domain, identified in Ros protein from Agrobacterium tumefaciens, has demonstrated that, although possessing a similar zinc coordination sphere, this domain is structurally very different from its eukaryotic counterpart. A search in the databases has identified approximately 300 homologues with a high sequence identity to the Ros protein, including the amino acids that form the extensive hydrophobic core in Ros. Surprisingly, the Cys(2)His(2) zinc coordination sphere is generally poorly conserved in the Ros homologues, raising the question of whether the zinc ion is always preserved in these proteins. Here, we present a functional and structural study of a point mutant of Ros protein, Ros(56-142)C82D, in which the second coordinating cysteine is replaced by an aspartate, 5 previously-uncharacterized representative Ros homologues from Mesorhizobium loti, and 2 mutants of the homologues. Our results indicate that the prokaryotic zinc-finger domain, which in Ros protein tetrahedrally coordinates Zn(II) through the typical Cys(2)His(2) coordination, in Ros homologues can either exploit a CysAspHis(2) coordination sphere, previously never described in DNA binding zinc finger domains to our knowledge, or lose the metal, while still preserving the DNA-binding activity. We demonstrate that this class of prokaryotic zinc-finger domains is structurally very adaptable, and surprisingly single mutations can transform a zinc-binding domain into a nonzinc-binding domain and vice versa, without affecting the DNA-binding ability. In light of our findings an evolutionary link between the prokaryotic and eukaryotic zinc-finger domains, based on bacteria-to-eukaryota horizontal gene transfer, is discussed.
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