ArticleNucleic acids research2010
Structural and mechanistic insights into Helicobacter pylori NikR activation.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Mechanistic insights into the nickel-dependent allosteric response of the Helicobacter pylori NikR transcription factor.The Journal of biological chemistry · 2023Article
- Insights into the Orchestration of Gene Transcription Regulators inInternational journal of molecular sciences · 2022Review
- Bacterial Transcriptional Regulators: A Road Map for Functional, Structural, and Biophysical Characterization.International journal of molecular sciences · 2022Review
- Allosteric control of metal-responsive transcriptional regulators in bacteria.The Journal of biological chemistry · 2020Review
- Nickel Metalloregulators and Chaperones.Inorganics · 2019Article
- Comprehensive mapping of the Helicobacter pylori NikR regulon provides new insights in bacterial nickel responses.Scientific reports · 2017Article
- On the interaction of Helicobacter pylori NikR, a Ni(II)-responsive transcription factor, with the urease operator: in solution and in silico studies.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Evolution of Macromolecular Docking Techniques: The Case Study of Nickel and Iron Metabolism in Pathogenic Bacteria.Molecules (Basel, Switzerland) · 2015Review
- Transcription factor-based biosensors enlightened by the analyte.Frontiers in microbiology · 2015Review
- Crosstalk between the HpArsRS two-component system and HpNikR is necessary for maximal activation of urease transcription.Frontiers in microbiology · 2015Article
- BioSAXS Sample Changer: a robotic sample changer for rapid and reliable high-throughput X-ray solution scattering experiments.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Streptomyces coelicolor SCO4226 is a nickel binding protein.PloS one · 2014Article
- Specific metal recognition in nickel trafficking.Biochemistry · 2012Review
- Ni(II) coordination to mixed sites modulates DNA binding of HpNikR via a long-range effect.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Hierarchical regulation of the NikR-mediated nickel response in Helicobacter pylori.Nucleic acids research · 2011Article
- Helicobacter pylori NikR protein exhibits distinct conformations when bound to different promoters.The Journal of biological chemistry · 2011Article
- In vivo recognition of the fecA3 target promoter by Helicobacter pylori NikR.Journal of bacteriology · 2011Article
- Holo-Ni(II)HpNikR is an asymmetric tetramer containing two different nickel-binding sites.Journal of the American Chemical Society · 2010Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NikR is a transcriptional metalloregulator central in the mandatory response to acidity of Helicobacter pylori that controls the expression of numerous genes by binding to specific promoter regions. NikR/DNA interactions were proposed to rely on protein activation by Ni(II) binding to high-affinity (HA) and possibly secondary external (X) sites. We describe a biochemical characterization of HpNikR mutants that shows that the HA sites are essential but not sufficient for DNA binding, while the secondary external (X) sites and residues from the HpNikR dimer-dimer interface are important for DNA binding. We show that a second metal is necessary for HpNikR/DNA binding, but only to some promoters. Small-angle X-ray scattering shows that HpNikR adopts a defined conformation in solution, resembling the cis-conformation and suggests that nickel does not trigger large conformational changes in HpNikR. The crystal structures of selected mutants identify the effects of each mutation on HpNikR structure. This study unravels key structural features from which we derive a model for HpNikR activation where: (i) HA sites and an hydrogen bond network are required for DNA binding and (ii) metallation of a unique secondary external site (X) modulates HpNikR DNA binding to low-affinity promoters by disruption of a salt bridge.
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Registered trials
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