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- Publisher Website: 10.1016/j.jinorgbio.2019.03.025
- Scopus: eid_2-s2.0-85064152755
- WOS: WOS:000469888100005
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Article: Inactivation of NikR from Helicobacter pylori by a bismuth drug
Title | Inactivation of NikR from Helicobacter pylori by a bismuth drug |
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Authors | |
Keywords | Bismuth drug DNA regulator Helicobacter pylori Metal-binding |
Issue Date | 2019 |
Publisher | Elsevier 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? |
Abstract | The 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 Identifier | http://hdl.handle.net/10722/270072 |
ISSN | 2023 Impact Factor: 3.8 2023 SCImago Journal Rankings: 0.614 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Guo, Y | - |
dc.contributor.author | Guan, CJ | - |
dc.contributor.author | Wan, H | - |
dc.contributor.author | Zhang, ZR | - |
dc.contributor.author | Li, H | - |
dc.contributor.author | Sun, H | - |
dc.contributor.author | Xia, W | - |
dc.date.accessioned | 2019-05-20T05:08:57Z | - |
dc.date.available | 2019-05-20T05:08:57Z | - |
dc.date.issued | 2019 | - |
dc.identifier.citation | Journal of Inorganic Biochemistry, 2019, v. 196, p. 110685 | - |
dc.identifier.issn | 0162-0134 | - |
dc.identifier.uri | http://hdl.handle.net/10722/270072 | - |
dc.description.abstract | The 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.language | eng | - |
dc.publisher | Elsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbio | - |
dc.relation.ispartof | Journal of Inorganic Biochemistry | - |
dc.subject | Bismuth drug | - |
dc.subject | DNA regulator | - |
dc.subject | Helicobacter pylori | - |
dc.subject | Metal-binding | - |
dc.title | Inactivation of NikR from Helicobacter pylori by a bismuth drug | - |
dc.type | Article | - |
dc.identifier.email | Li, H: hylichem@hku.hk | - |
dc.identifier.email | Sun, H: hsun@hku.hk | - |
dc.identifier.authority | Sun, H=rp00777 | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/j.jinorgbio.2019.03.025 | - |
dc.identifier.scopus | eid_2-s2.0-85064152755 | - |
dc.identifier.hkuros | 297869 | - |
dc.identifier.volume | 196 | - |
dc.identifier.spage | 110685 | - |
dc.identifier.epage | 110685 | - |
dc.identifier.isi | WOS:000469888100005 | - |
dc.publisher.place | United States | - |
dc.identifier.issnl | 0162-0134 | - |