ArticleJournal of bacteriology2010
The Helicobacter pylori GroES cochaperonin HspA functions as a specialized nickel chaperone and sequestration protein through its unique C-terminal extension.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 65 citations in OpenAlex.
- High salt condition alters LPS synthesis and induces the emergence of drug resistance mutations inAntimicrobial agents and chemotherapy · 2024Article
- Helicobacter pylori in the post-antibiotics era: from virulence factors to new drug targets and therapeutic agents.Archives of microbiology · 2023Review
- Identification of B-Cell Epitopes of HspA fromVaccines · 2021Article
- A novel mode of control of nickel uptake by a multifunctional metallochaperone.PLoS pathogens · 2021Article
- Review
- Live Attenuated Measles Virus Vaccine ExpressingMolecular therapy oncolytics · 2020Article
- Molecular Hydrogen Metabolism: a Widespread Trait of Pathogenic Bacteria and Protists.Microbiology and molecular biology reviews : MMBR · 2020Review
- Acid-responsive activity of theProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Genome characterization of two bile-isolated Vibrio fluvialis strains: an insight into pathogenicity and bile salt adaption.Scientific reports · 2017Article
- The Hsp60 protein of helicobacter pylori displays chaperone activity under acidic conditions.Biochemistry and biophysics reports · 2017Article
- Characterization in Helicobacter pylori of a Nickel Transporter Essential for Colonization That Was Acquired during Evolution by Gastric Helicobacter Species.PLoS pathogens · 2016Article
- Importance of the C-terminal histidine residues of Helicobacter pylori GroES for Toll-like receptor 4 binding and interleukin-8 cytokine production.Scientific reports · 2016Article
- Article
- Evolution of Helicobacter: Acquisition by Gastric Species of Two Histidine-Rich Proteins Essential for Colonization.PLoS pathogens · 2015Article
- Nickel trafficking system responsible for urease maturation in Helicobacter pylori.World journal of gastroenterology · 2013Review
- Helicobacter pylori stores nickel to aid its host colonization.Infection and immunity · 2013Article
- Common themes and unique proteins for the uptake and trafficking of nickel, a metal essential for the virulence of Helicobacter pylori.Frontiers in cellular and infection microbiology · 2013Review
- Helicobacter hepaticus NikR controls urease and hydrogenase activities via the NikABDE and HH0418 putative nickel import proteins.Microbiology (Reading, England) · 2013Article
- Hierarchical regulation of the NikR-mediated nickel response in Helicobacter pylori.Nucleic acids research · 2011Article
- Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transition metal nickel plays a central role in the human gastric pathogen Helicobacter pylori because it is required for two enzymes indispensable for colonization, the nickel metalloenzyme urease and [NiFe] hydrogenase. To sustain nickel availability for these metalloenzymes while providing protection from the metal's harmful effects, H. pylori is equipped with several specific nickel-binding proteins. Among these, H. pylori possesses a particular chaperone, HspA, that is a homolog of the highly conserved and essential bacterial heat shock protein GroES. HspA contains a unique His-rich C-terminal extension and was demonstrated to bind nickel in vitro. To investigate the function of this extension in H. pylori, we constructed mutants carrying either a complete deletion or point mutations in critical residues of this domain. All mutants presented a decreased intracellular nickel content measured by inductively coupled plasma mass spectrometry (ICP-MS) and reduced nickel tolerance. While urease activity was unaffected in the mutants, [NiFe] hydrogenase activity was significantly diminished when the C-terminal extension of HspA was mutated. We conclude that H. pylori HspA is involved in intracellular nickel sequestration and detoxification and plays a novel role as a specialized nickel chaperone involved in nickel-dependent maturation of hydrogenase.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.