ArticleThe Journal of biological chemistry2012
Metallo-GTPase HypB from Helicobacter pylori and its interaction with nickel chaperone protein HypA.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 57 citations in OpenAlex.
- The HypA and HypB metallochaperones from Methanococcus maripaludis have unique metal-binding properties and a distinct nickel transfer mechanism.The Journal of biological chemistry · 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
- The zinc metalloprotein MigC impacts cell wall biogenesis through interactions with an essential Mur ligase in Acinetobacter baumannii.PLoS pathogens · 2025Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Bismuth-based drugs sensitize Pseudomonas aeruginosa to multiple antibiotics by disrupting iron homeostasis.Nature microbiology · 2024Article
- Coupling of zinc and GTP binding drives G-domain folding in Acinetobacter baumannii ZigA.Biophysical journal · 2024Article
- Article
- High Synteny and Sequence Identity between Genomes ofMicroorganisms · 2020Article
- Molecular Hydrogen Metabolism: a Widespread Trait of Pathogenic Bacteria and Protists.Microbiology and molecular biology reviews : MMBR · 2020Review
- Mechanistic Insights into the Metal-Dependent Activation of ZnInorganic chemistry · 2019Article
- Nickel Metalloregulators and Chaperones.Inorganics · 2019Article
- Metallochaperone UreG serves as a new target for design of urease inhibitor: A novel strategy for development of antimicrobials.PLoS biology · 2018Article
- Evolution of Helicobacter: Acquisition by Gastric Species of Two Histidine-Rich Proteins Essential for Colonization.PLoS pathogens · 2015Article
- Structural basis of a Ni acquisition cycle for [NiFe] hydrogenase by Ni-metallochaperone HypA and its enhancer.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- UreE-UreG complex facilitates nickel transfer and preactivates GTPase of UreG in Helicobacter pylori.The Journal of biological chemistry · 2015Article
- Dynamic HypA zinc site is essential for acid viability and proper urease maturation in Helicobacter pylori.Metallomics : integrated biometal science · 2015Article
- Relationship between Ni(II) and Zn(II) coordination and nucleotide binding by the Helicobacter pylori [NiFe]-hydrogenase and urease maturation factor HypB.The Journal of biological chemistry · 2014Article
- Nickel trafficking system responsible for urease maturation in Helicobacter pylori.World journal of gastroenterology · 2013Review
- Metal transfer within the Escherichia coli HypB-HypA complex of hydrogenase accessory proteins.Biochemistry · 2013Article
- miR-124 inhibits STAT3 signaling to enhance T cell-mediated immune clearance of glioma.Cancer research · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The maturation of [NiFe]-hydrogenase is highly dependent on a battery of chaperone proteins. Among these, HypA and HypB were proposed to exert nickel delivery functions in the metallocenter assembly process, although the detailed mechanism remains unclear. Herein, we have overexpressed and purified wild-type HypB as well as two mutants, K168A and M186L/F190V, from Helicobacter pylori. We demonstrated that all proteins bind Ni(2+) at a stoichiometry of one Ni(2+) per monomer of the proteins with dissociation constants at micromolar levels. Ni(2+) elevated GTPase activity of WT HypB, which is attributable to a lower affinity of the protein toward GDP as well as Ni(2+)-induced dimerization. The disruption of GTP-dependent dimerization has led to GTPase activities of both mutants in apo-forms almost completely abolished, compared with the wild-type protein. The GTPase activity is partially restored for HypB(M186L/F190V) mutant but not for HypB(K168A) mutant upon Ni(2+) binding. HypB forms a complex with its partner protein HypA with a low affinity (K(d) of 52.2 ± 8.8 μM). Such interactions were also observed in vivo both in the absence and presence of nickel using a GFP-fragment reassembly technique. The putative protein-protein interfaces on H. pylori HypA and HypB proteins were identified by NMR chemical shift perturbation and mutagenesis studies, respectively. Intriguingly, the unique N terminus of H. pylori HypB was identified to participate in the interaction with H. pylori HypA. These structural and functional studies provide insight into the molecular mechanism of Ni(2+) delivery during maturation of [NiFe]-hydrogenase.
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