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Article: Selective interaction of Hpn-like protein with nickel, zinc and bismuth in vitro and in cells by FRET

TitleSelective interaction of Hpn-like protein with nickel, zinc and bismuth in vitro and in cells by FRET
Authors
Issue Date2015
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbio
Citation
Journal of Inorganic Biochemistry, 2015, v. 142, p. 8-14 How to Cite?
AbstractHpn-like (Hpnl) is a unique histidine- and glutamine-rich protein found only in Helicobacter pylori and plays a role on nickel homeostasis.Weconstructed the fluorescent sensor proteins CYHpnl and CYHpnl_1-48 (C-terminal glutamine-rich region truncated) using enhanced cyan and yellow fluorescent proteins (eCFP and eYFP) as the donor–acceptor pair to monitor the interactions of Hpnl with metal ions and to elucidate the role of conserved Glu-rich sequence in Hpnl by fluorescence resonance energy transfer (FRET). CYHpnl and CYHpnl_1-48 exhibited largest responses towards Ni(II) and Zn(II) over other metals studied and the binding of Bi(III) to CYHpnl was observed in the presence of an excess amount of Bi(III) ions (Kd =115±4.8 μM). Moreover, both CYHpnl and CYHpnl_1-48 showed positive FRET responses towards the binding to Ni(II) and Zn(II) in Escherichia coli cells overexpressing CYHpnl and CYHpnl_1-48, whereas a decrease in FRET upon Bi(III)-binding in E. coli cells overexpressing the latter. Our study provides clear evidence on Hpnl binding to nickel in cells, and intracellular interaction of Hpnl with Bi(III) could disrupt the protein function, thus probably contributing to the efficacy of Bi(III) drugs against H. pylori.
Persistent Identifierhttp://hdl.handle.net/10722/215150
ISSN
2015 Impact Factor: 3.205
2015 SCImago Journal Rankings: 0.983

 

DC FieldValueLanguage
dc.contributor.authorChang, YY-
dc.contributor.authorLai, YT-
dc.contributor.authorCheng, T-
dc.contributor.authorWang, H-
dc.contributor.authorYang, Y-
dc.contributor.authorSun, H-
dc.date.accessioned2015-08-21T13:16:09Z-
dc.date.available2015-08-21T13:16:09Z-
dc.date.issued2015-
dc.identifier.citationJournal of Inorganic Biochemistry, 2015, v. 142, p. 8-14-
dc.identifier.issn0162-0134-
dc.identifier.urihttp://hdl.handle.net/10722/215150-
dc.description.abstractHpn-like (Hpnl) is a unique histidine- and glutamine-rich protein found only in Helicobacter pylori and plays a role on nickel homeostasis.Weconstructed the fluorescent sensor proteins CYHpnl and CYHpnl_1-48 (C-terminal glutamine-rich region truncated) using enhanced cyan and yellow fluorescent proteins (eCFP and eYFP) as the donor–acceptor pair to monitor the interactions of Hpnl with metal ions and to elucidate the role of conserved Glu-rich sequence in Hpnl by fluorescence resonance energy transfer (FRET). CYHpnl and CYHpnl_1-48 exhibited largest responses towards Ni(II) and Zn(II) over other metals studied and the binding of Bi(III) to CYHpnl was observed in the presence of an excess amount of Bi(III) ions (Kd =115±4.8 μM). Moreover, both CYHpnl and CYHpnl_1-48 showed positive FRET responses towards the binding to Ni(II) and Zn(II) in Escherichia coli cells overexpressing CYHpnl and CYHpnl_1-48, whereas a decrease in FRET upon Bi(III)-binding in E. coli cells overexpressing the latter. Our study provides clear evidence on Hpnl binding to nickel in cells, and intracellular interaction of Hpnl with Bi(III) could disrupt the protein function, thus probably contributing to the efficacy of Bi(III) drugs against <i>H. pylori</i>.-
dc.languageeng-
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbio-
dc.relation.ispartofJournal of Inorganic Biochemistry-
dc.rights© 2015. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/-
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.titleSelective interaction of Hpn-like protein with nickel, zinc and bismuth in vitro and in cells by FRET-
dc.typeArticle-
dc.identifier.emailSun, H: hsun@hku.hk-
dc.identifier.authoritySun, H=rp00777-
dc.description.naturepostprint-
dc.identifier.doi10.1016/j.jinorgbio.2014.09.010-
dc.identifier.hkuros247650-
dc.identifier.volume142-
dc.identifier.spage8-
dc.identifier.epage14-
dc.publisher.placeUnited States-

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