ArticleMetallomics : integrated biometal science2015
Dynamic HypA zinc site is essential for acid viability and proper urease maturation in Helicobacter pylori.
Article in Metallomics : integrated biometal science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Moving metals: How microbes deliver metal cofactors to metalloproteins.Molecular microbiology · 2023Article
- The structure of the high-affinity nickel-binding site in the Ni,Zn-HypA•UreE2 complex.Metallomics : integrated biometal science · 2023Article
- Metal homeostasis in pathogenic Epsilonproteobacteria: mechanisms of acquisition, efflux, and regulation.Metallomics : integrated biometal science · 2021Review
- Flavodoxins as Novel Therapeutic Targets againstInternational journal of molecular sciences · 2020Review
- The Metallochaperone Encoding GeneMicroorganisms · 2019Article
- Nickel Metalloregulators and Chaperones.Inorganics · 2019Article
- Structure and dynamics of Helicobacter pylori nickel-chaperone HypA: an integrated approach using NMR spectroscopy, functional assays and computational tools.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- The Helicobacter pylori HypA·UreEBiochemistry · 2018Article
- Glutamate Ligation in the Ni(II)- and Co(II)-Responsive Escherichia coli Transcriptional Regulator, RcnR.Inorganic chemistry · 2017Article
- Metallochaperones and metalloregulation in bacteria.Essays in biochemistry · 2017Review
- Nickel Ligation of the N-Terminal Amine of HypA Is Required for Urease Maturation in Helicobacter pylori.Biochemistry · 2017Article
- Structure-function analyses of metal-binding sites of HypA reveal residues important for hydrogenase maturation in Helicobacter pylori.PloS one · 2017Article
- Nutrition and Helicobacter pylori: Host Diet and Nutritional Immunity Influence Bacterial Virulence and Disease Outcome.Gastroenterology research and practice · 2016Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Helicobacter pylori requires urease activity in order to survive in the acid environment of the human stomach. Urease is regulated in part by nickelation, a process that requires the HypA protein, which is a putative nickel metallochaperone that is generally associated with hydrogenase maturation. However, in H. pylori, HypA plays a dual role. In addition to an N-terminal nickel binding site, HypA proteins also contain a structural zinc site that is coordinated by two rigorously conserved CXXC sequences, which in H. pylori are flanked by His residues. These structural Zn sites are known to be dynamic, converting from Zn(Cys)4 centers at pH 7.2 to Zn(Cys)2(His)2 centers at pH 6.3 in the presence of Ni(ii) ions. In this study, mutant strains of H. pylori that express zinc site variants of the HypA protein are used to show that the structural changes in the zinc site are important for the acid viability of the bacterium, and that a reduction in acid viability in these variants can be traced in large measure to deficient urease activity. This in turn leads to a model that connects the Zn(Cys)4 coordination to urease maturation.
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Registered trials
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