ArticleThe Journal of biological chemistry2015
UreE-UreG complex facilitates nickel transfer and preactivates GTPase of UreG in Helicobacter pylori.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 67 citations in OpenAlex.
- Article
- From Bovine Immune Milk Profiling to Multi-Antigen Vaccine Design: Enhanced Humoral Responses AgainstVaccines · 2026Article
- Structural investigations connect the disordered N-terminal extension of HypB to the activities of HypB and SlyD in E. coli.Protein science : a publication of the Protein Society · 2025Article
- Anti-urease therapy: a targeted approach to mitigating antibiotic resistance in Helicobacter pylori while preserving the gut microflora.Gut pathogens · 2025Review
- A metal-trap tests and refines blueprints to engineer cellular protein metalation with different elements.Nature communications · 2025Article
- New Directions inInfection and drug resistance · 2025Review
- Epiberberine: a potential rumen microbial urease inhibitor to reduce ammonia release screened by targeting UreG.Applied microbiology and biotechnology · 2024Article
- Copper regulates the host innate immune response against bacterial infection via activation of ALPK1 kinase.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Delivering a toxic metal to the active site of urease.Science advances · 2023Article
- The structure of the high-affinity nickel-binding site in the Ni,Zn-HypA•UreE2 complex.Metallomics : integrated biometal science · 2023Article
- Isolation and pan-genome analysis ofFrontiers in microbiology · 2023Article
- Protein metalation in a nutshell.FEBS letters · 2023Review
- COG0523 proteins: a functionally diverse family of transition metal-regulated G3E P-loop GTP hydrolases from bacteria to man.Metallomics : integrated biometal science · 2021Article
- Chelerythrine Chloride: A Potential Rumen Microbial Urease Inhibitor Screened by Targeting UreG.International journal of molecular sciences · 2021Article
- Metal homeostasis in pathogenic Epsilonproteobacteria: mechanisms of acquisition, efflux, and regulation.Metallomics : integrated biometal science · 2021Review
- The requirement for cobalt in vitamin BBiochimica et biophysica acta. Molecular cell research · 2021Review
- Nickel and GTP ModulateBiomolecules · 2020Article
- Targeting the Protein Tunnels of the Urease Accessory Complex: A Theoretical Investigation.Molecules (Basel, Switzerland) · 2020Article
- Mechanistic Insights into the Metal-Dependent Activation of ZnInorganic chemistry · 2019Article
- Nickel Metalloregulators and Chaperones.Inorganics · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pathogenicity of Helicobacter pylori relies heavily on urease, which converts urea to ammonia to neutralize the stomach acid. Incorporation of Ni(2+) into the active site of urease requires a battery of chaperones. Both metallochaperones UreE and UreG play important roles in the urease activation. In this study, we demonstrate that, in the presence of GTP and Mg(2+), UreG binds Ni(2+) with an affinity (Kd) of ∼0.36 μm. The GTPase activity of Ni(2+)-UreG is stimulated by both K(+) (or NH4 (+)) and HCO3 (-) to a biologically relevant level, suggesting that K(+)/NH4 (+) and HCO3 (-) might serve as GTPase elements of UreG. We show that complexation of UreE and UreG results in two protein complexes, i.e. 2E-2G and 2E-G, with the former being formed only in the presence of both GTP and Mg(2+). Mutagenesis studies reveal that Arg-101 on UreE and Cys-66 on UreG are critical for stabilization of 2E-2G complex. Combined biophysical and bioassay studies show that the formation of 2E-2G complex not only facilitates nickel transfer from UreE to UreG, but also enhances the binding of GTP. This suggests that UreE might also serve as a structural scaffold for recruitment of GTP to UreG. Importantly, we demonstrate for the first time that UreE serves as a bridge to grasp Ni(2+) from HypA, subsequently donating it to UreG. The study expands our horizons on the molecular details of nickel translocation among metallochaperones UreE, UreG, and HypA, which further extends our knowledge on the urease maturation process.
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