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Article: Inactivation of NikR from Helicobacter pylori by a bismuth drug

TitleInactivation of NikR from Helicobacter pylori by a bismuth drug
Authors
Issue Date2019
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbio
Citation
Journal of Inorganic Biochemistry, 2019, v. 196, p. 110685 How to Cite?
AbstractThe NikR protein is an essential DNA regulator of Helicobacter pylori, a human pathogen, which infects almost half of the world's population. Herein, we comprehensively characterized the interaction of a bismuth drug with Helicobacter pylori NikR. We show that Bi(III) can occupy the high-affinity Ni(II) site of NikR. The highly-conserved residue Cys107 at this site is critical for Bi(III) binding. Importantly, such a binding disassembles physiologically functional NikR tetramer into inactive dimer, leading to abrogation of the DNA-binding capability of NikR. Bi(III)-binding also significantly disturbs regulatory function of Helicobacter pylori NikR in vivo. Therefore, NikR might serve as a potential intracellular target of a bismuth drug.
Persistent Identifierhttp://hdl.handle.net/10722/270072
ISSN
2017 Impact Factor: 3.063
2015 SCImago Journal Rankings: 0.983

 

DC FieldValueLanguage
dc.contributor.authorGuo, Y-
dc.contributor.authorGuan, CJ-
dc.contributor.authorWan, H-
dc.contributor.authorZhang, ZR-
dc.contributor.authorLi, H-
dc.contributor.authorSun, H-
dc.contributor.authorXia, W-
dc.date.accessioned2019-05-20T05:08:57Z-
dc.date.available2019-05-20T05:08:57Z-
dc.date.issued2019-
dc.identifier.citationJournal of Inorganic Biochemistry, 2019, v. 196, p. 110685-
dc.identifier.issn0162-0134-
dc.identifier.urihttp://hdl.handle.net/10722/270072-
dc.description.abstractThe NikR protein is an essential DNA regulator of Helicobacter pylori, a human pathogen, which infects almost half of the world's population. Herein, we comprehensively characterized the interaction of a bismuth drug with Helicobacter pylori NikR. We show that Bi(III) can occupy the high-affinity Ni(II) site of NikR. The highly-conserved residue Cys107 at this site is critical for Bi(III) binding. Importantly, such a binding disassembles physiologically functional NikR tetramer into inactive dimer, leading to abrogation of the DNA-binding capability of NikR. Bi(III)-binding also significantly disturbs regulatory function of Helicobacter pylori NikR in vivo. Therefore, NikR might serve as a potential intracellular target of a bismuth drug.-
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.titleInactivation of NikR from Helicobacter pylori by a bismuth drug-
dc.typeArticle-
dc.identifier.emailLi, H: hylichem@hku.hk-
dc.identifier.emailSun, H: hsun@hku.hk-
dc.identifier.authoritySun, H=rp00777-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.jinorgbio.2019.03.025-
dc.identifier.hkuros297869-
dc.identifier.volume196-
dc.identifier.spage110685-
dc.identifier.epage110685-
dc.publisher.placeUnited States-

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