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Article: A histidine-rich and cysteine-rich metal-binding domain at the C terminus of heat shock protein A from helicobacter pylori: Implication for nickel homeostasis and bismuth susceptibility

TitleA histidine-rich and cysteine-rich metal-binding domain at the C terminus of heat shock protein A from helicobacter pylori: Implication for nickel homeostasis and bismuth susceptibility
Authors
Issue Date2008
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2008, v. 283 n. 22, p. 15142-15151 How to Cite?
AbstractHspA, a member of the GroES chaperonin family, is a small protein found in Helicobacter pylori with a unique histidine-and cysteine-rich domain at the C terminus. In this work, we overexpressed, purified, and characterized this protein both in vitro and in vivo. The apo form of the protein binds 2.10 ± 0.07 Ni2+ or 1.98 ± 0.08 Bi3+ ions/monomer with a dissociation constant (Kd) of 1.1 or 5.9 × 10 -19 μM, respectively. Importantly, Ni2+ can reversibly bind to the protein, as the bound nickel can be released either in the presence of a chelating ligand, e.g. EDTA, or at an acidic pH (pH1?2 3.8 ± 0.2). In contrast, Bi3+ binds almost irreversibly to the protein. Both gel filtration chromatography and native electrophoresis demonstrated that apo-HspA exists as a heptamer in solution. Unexpectedly, binding of Bi3+ to the protein altered its quaternary structure from a heptamer to a dimer, indicating that bismuth may interfere with the biological functions of HspA. When cultured in Ni2+-supplemented M9 minimal medium, Escherichia coli BL21(DE3) cells expressing wild-type HspA or the C-terminal deletion mutant clearly indicated that the C terminus might protect cells from high concentrations of external Ni2+. However, an opposite phenomenon was observed when the same E. coli hosts were grown in Bi 3+-supplemented medium. HspA may therefore play a dual role: to facilitate nickel acquisition by donating Ni2+ to appropriate proteins in a nickel-deficient environment and to carry out detoxification via sequestration of excess nickel. Meanwhile, HspA can be a potential target of the bismuth antiulcer drug against H. pylori. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/70094
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorCun, Sen_HK
dc.contributor.authorLi, Hen_HK
dc.contributor.authorGe, Ren_HK
dc.contributor.authorLin, MCMen_HK
dc.contributor.authorSun, Hen_HK
dc.date.accessioned2010-09-06T06:19:39Z-
dc.date.available2010-09-06T06:19:39Z-
dc.date.issued2008en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2008, v. 283 n. 22, p. 15142-15151en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/70094-
dc.description.abstractHspA, a member of the GroES chaperonin family, is a small protein found in Helicobacter pylori with a unique histidine-and cysteine-rich domain at the C terminus. In this work, we overexpressed, purified, and characterized this protein both in vitro and in vivo. The apo form of the protein binds 2.10 ± 0.07 Ni2+ or 1.98 ± 0.08 Bi3+ ions/monomer with a dissociation constant (Kd) of 1.1 or 5.9 × 10 -19 μM, respectively. Importantly, Ni2+ can reversibly bind to the protein, as the bound nickel can be released either in the presence of a chelating ligand, e.g. EDTA, or at an acidic pH (pH1?2 3.8 ± 0.2). In contrast, Bi3+ binds almost irreversibly to the protein. Both gel filtration chromatography and native electrophoresis demonstrated that apo-HspA exists as a heptamer in solution. Unexpectedly, binding of Bi3+ to the protein altered its quaternary structure from a heptamer to a dimer, indicating that bismuth may interfere with the biological functions of HspA. When cultured in Ni2+-supplemented M9 minimal medium, Escherichia coli BL21(DE3) cells expressing wild-type HspA or the C-terminal deletion mutant clearly indicated that the C terminus might protect cells from high concentrations of external Ni2+. However, an opposite phenomenon was observed when the same E. coli hosts were grown in Bi 3+-supplemented medium. HspA may therefore play a dual role: to facilitate nickel acquisition by donating Ni2+ to appropriate proteins in a nickel-deficient environment and to carry out detoxification via sequestration of excess nickel. Meanwhile, HspA can be a potential target of the bismuth antiulcer drug against H. pylori. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.titleA histidine-rich and cysteine-rich metal-binding domain at the C terminus of heat shock protein A from helicobacter pylori: Implication for nickel homeostasis and bismuth susceptibilityen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9258&volume=283&spage=15142&epage=15151&date=2008&atitle=A+Histidine-rich+and+cysteine-rich+metal-binding+domain+at+the+C+terminus+of+heat+shock+protein+A+from+Helicobacter+pylori:+implication+for+nickel+homeostasis+and+bismuth+susceptibilityen_HK
dc.identifier.emailLin, MCM:mcllin@hkucc.hku.hken_HK
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_HK
dc.identifier.authorityLin, MCM=rp00746en_HK
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1074/jbc.M800591200en_HK
dc.identifier.pmid18364351-
dc.identifier.pmcidPMC3258894-
dc.identifier.scopuseid_2-s2.0-47249162533en_HK
dc.identifier.hkuros145154en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-47249162533&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume283en_HK
dc.identifier.issue22en_HK
dc.identifier.spage15142en_HK
dc.identifier.epage15151en_HK
dc.identifier.isiWOS:000256232000030-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridCun, S=24467307200en_HK
dc.identifier.scopusauthoridLi, H=14023043100en_HK
dc.identifier.scopusauthoridGe, R=7005525090en_HK
dc.identifier.scopusauthoridLin, MCM=7404816359en_HK
dc.identifier.scopusauthoridSun, H=7404827446en_HK
dc.identifier.citeulike3813121-

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