{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["192(5)"],"submitter":["Schauer K"],"pubmed_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 mutati"],"journal":["Journal of bacteriology"],"pagination":["1231-7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2820833"],"repository":["biostudies-literature"],"pubmed_title":["The Helicobacter pylori GroES cochaperonin HspA functions as a specialized nickel chaperone and sequestration protein through its unique C-terminal extension."],"pmcid":["PMC2820833"],"pubmed_authors":["Labigne A","Schauer K","Muller C","Cavazza C","De Reuse H","Carriere M"],"additional_accession":[]},"is_claimable":false,"name":"The Helicobacter pylori GroES cochaperonin HspA functions as a specialized nickel chaperone and sequestration protein through its unique C-terminal extension.","description":"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 mutati","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Mar","modification":"2025-04-19T06:30:51.021Z","creation":"2019-03-27T00:28:33Z"},"accession":"S-EPMC2820833","cross_references":{"pubmed":["20061471"],"doi":["10.1128/JB.01216-09","10.1128/jb.01216-09"]}}