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Article: Metal-binding properties of an Hpn-like histidine-rich protein

TitleMetal-binding properties of an Hpn-like histidine-rich protein
Authors
Keywordsbinding sites
Helicobacter pylori
nickel
proteins
thermodynamics
Issue Date2011
PublisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/chemistry
Citation
Chemistry - A European Journal, 2011, v. 17 n. 21, p. 5852-5860 How to Cite?
AbstractThe Hpn-like protein (Hpnl), a histidine- and glutamine-rich protein, is critical for Helicobacter pylori colonization in human gastric muscosa. In this study, the thermodynamic properties of Ni II, Cu II, Co II, and Zn II toward Hpnl were studied by isothermal titration calorimetry (ITC). We found that Hpnl exhibits two independent binding sites for Ni II as opposed to one site for Cu II, Co II, and Zn II. Protease digestion and chemical denaturation analysis further revealed that Ni II confers a higher stability upon Hpnl than other divalent metal ions. The potential Ni II binding sites are localized in the His-rich domain of Hpnl as confirmed by mutagenesis in combination with modification of histidine residues of the protein. We also demonstrated that the single mutants (H29A and H31A) and tetrameric mutant (H29-32A) cut nearly half of the binding capacity of Hpnl towards nickel ions, whereas other histidine residues (His30, 32, 38, 39, 40, and 41) are nonessential for nickel coordination. Escherichia coli cells that harbored H29A, H31A, and H29-32A mutant genes exhibited less tolerance toward high concentrations of extracellular nickel ions than those with the wild-type gene. Our combined data indicated that the conserved histidine residues, His29 and His31 in the His-rich domain of Hpnl, are critical for nickel binding, and such a binding is important for Hpnl protein to fulfill its biological functions. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Persistent Identifierhttp://hdl.handle.net/10722/137220
ISSN
2015 Impact Factor: 5.771
2015 SCImago Journal Rankings: 2.323
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZeng, YBen_HK
dc.contributor.authorYang, Nen_HK
dc.contributor.authorSun, Hen_HK
dc.date.accessioned2011-08-26T14:19:14Z-
dc.date.available2011-08-26T14:19:14Z-
dc.date.issued2011en_HK
dc.identifier.citationChemistry - A European Journal, 2011, v. 17 n. 21, p. 5852-5860en_HK
dc.identifier.issn0947-6539en_HK
dc.identifier.urihttp://hdl.handle.net/10722/137220-
dc.description.abstractThe Hpn-like protein (Hpnl), a histidine- and glutamine-rich protein, is critical for Helicobacter pylori colonization in human gastric muscosa. In this study, the thermodynamic properties of Ni II, Cu II, Co II, and Zn II toward Hpnl were studied by isothermal titration calorimetry (ITC). We found that Hpnl exhibits two independent binding sites for Ni II as opposed to one site for Cu II, Co II, and Zn II. Protease digestion and chemical denaturation analysis further revealed that Ni II confers a higher stability upon Hpnl than other divalent metal ions. The potential Ni II binding sites are localized in the His-rich domain of Hpnl as confirmed by mutagenesis in combination with modification of histidine residues of the protein. We also demonstrated that the single mutants (H29A and H31A) and tetrameric mutant (H29-32A) cut nearly half of the binding capacity of Hpnl towards nickel ions, whereas other histidine residues (His30, 32, 38, 39, 40, and 41) are nonessential for nickel coordination. Escherichia coli cells that harbored H29A, H31A, and H29-32A mutant genes exhibited less tolerance toward high concentrations of extracellular nickel ions than those with the wild-type gene. Our combined data indicated that the conserved histidine residues, His29 and His31 in the His-rich domain of Hpnl, are critical for nickel binding, and such a binding is important for Hpnl protein to fulfill its biological functions. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.en_HK
dc.languageengen_US
dc.publisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/chemistryen_HK
dc.relation.ispartofChemistry - A European Journalen_HK
dc.subjectbinding sitesen_HK
dc.subjectHelicobacter pylorien_HK
dc.subjectnickelen_HK
dc.subjectproteinsen_HK
dc.subjectthermodynamicsen_HK
dc.subject.meshBacterial Proteins - chemistry - metabolism-
dc.subject.meshHelicobacter pylori - chemistry - metabolism-
dc.subject.meshHistidine - chemistry-
dc.subject.meshNickel - chemistry-
dc.subject.meshProteins - chemistry - metabolism-
dc.titleMetal-binding properties of an Hpn-like histidine-rich proteinen_HK
dc.typeArticleen_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/chem.201100279en_HK
dc.identifier.pmid21520306-
dc.identifier.scopuseid_2-s2.0-79955782347en_HK
dc.identifier.hkuros189545en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79955782347&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume17en_HK
dc.identifier.issue21en_HK
dc.identifier.spage5852en_HK
dc.identifier.epage5860en_HK
dc.identifier.isiWOS:000291594800013-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridZeng, YB=7402981405en_HK
dc.identifier.scopusauthoridYang, N=36633600500en_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK

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