{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T18:43:33Z","timestamp":1791917013852,"version":"4.3.4"},"reference-count":49,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2009,8,15]]},"abstract":"<jats:p>The persistence of Helicobacter pylori in the hostile environment of the human stomach is ensured by the activity of urease. The essentiality of Ni2+ for this enzyme demands proper intracellular trafficking of this metal ion. The metallo-chaperone UreE promotes Ni2+ insertion into the apo-enzyme in the last step of urease maturation while facilitating concomitant GTP hydrolysis. The present study focuses on the metal-binding properties of HpUreE (Helicobacter pylori UreE) and its interaction with the related accessory protein HpUreG, a GTPase involved in the assembly of the urease active site. ITC (isothermal titration calorimetry) showed that HpUreE binds one equivalent of Ni2+ (Kd=0.15\u00a0\u03bcM) or Zn2+ (Kd=0.49\u00a0\u03bcM) per dimer, without modification of the protein oligomeric state, as indicated by light scattering. Different ligand environments for Zn2+ and Ni2+, which involve crucial histidine residues, were revealed by site-directed mutagenesis, suggesting a mechanism for discriminating metal-ion-specific binding. The formation of a HpUreE\u2013HpUreG protein complex was revealed by NMR spectroscopy, and the thermodynamics of this interaction were established using ITC. A role for Zn2+, and not for Ni2+, in the stabilization of this complex was demonstrated using size-exclusion chromatography, light scattering, and ITC experiments. A calculated viable structure for the complex suggested the presence of a novel binding site for Zn2+, actually detected using ITC and site-directed mutagenesis. The results are discussed in relation to available evidence of a UreE\u2013UreG functional interaction in vivo. A possible role for Zn2+ in the Ni2+-dependent urease system is envisaged.<\/jats:p>","DOI":"10.1042\/bj20090434","type":"journal-article","created":{"date-parts":[[2009,5,29]],"date-time":"2009-05-29T09:19:16Z","timestamp":1243588756000},"page":"91-100","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":97,"title":["<i>Helicobacter pylori<\/i>\n                    UreE, a urease accessory protein: specific Ni2+- and Zn2+-binding properties and interaction with its cognate UreG"],"prefix":"10.1042","volume":"422","author":[{"given":"Matteo","family":"Bellucci","sequence":"first","affiliation":[{"name":"Laboratory of Bioinorganic Chemistry, Department of Agro-Environmental Science and Technology, University of Bologna, Via Giuseppe Fanin 40, I-40127 Bologna, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Barbara","family":"Zambelli","sequence":"additional","affiliation":[{"name":"Laboratory of Bioinorganic Chemistry, Department of Agro-Environmental Science and Technology, University of Bologna, Via Giuseppe Fanin 40, I-40127 Bologna, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francesco","family":"Musiani","sequence":"additional","affiliation":[{"name":"Laboratory of Bioinorganic Chemistry, Department of Agro-Environmental Science and Technology, University of Bologna, Via Giuseppe Fanin 40, I-40127 Bologna, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paola","family":"Turano","sequence":"additional","affiliation":[{"name":"CERM (Centre for Magnetic Resonance), University of Florence, Via Luigi Sacconi 6, I-50019 Sesto Fiorentino, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefano","family":"Ciurli","sequence":"additional","affiliation":[{"name":"Laboratory of Bioinorganic Chemistry, Department of Agro-Environmental Science and Technology, University of Bologna, Via Giuseppe Fanin 40, I-40127 Bologna, Italy"},{"name":"CERM (Centre for Magnetic Resonance), University of Florence, Via Luigi Sacconi 6, I-50019 Sesto Fiorentino, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2009,7,29]]},"reference":[{"key":"2021112214150988900_B1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1523-5378.2008.00631.x","article-title":"Epidemiology of Helicobacter pylori infection","volume":"13","author":"Bruce","year":"2008","journal-title":"Helicobacter"},{"key":"2021112214150988900_B2","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1111\/j.1523-5378.2008.00633.x","article-title":"Helicobacter and gastric malignancies","volume":"13","author":"Ferreira","year":"2008","journal-title":"Helicobacter"},{"key":"2021112214150988900_B3","doi-asserted-by":"crossref","first-page":"10828","DOI":"10.1021\/ja0525399","article-title":"The burden borne by urease","volume":"127","author":"Callahan","year":"2005","journal-title":"J. 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