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Article: Important roles of the conserved linker-KKS in human neuronal growth inhibitory factor

TitleImportant roles of the conserved linker-KKS in human neuronal growth inhibitory factor
Authors
Issue Date2009
PublisherSpringer New York LLC. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0966-0844
Citation
Biometals, 2009, v. 22 n. 5, p. 817-826 How to Cite?
AbstractMetallothinein-3 (MT3), also named neuronal growth inhibitory factor (GIF), is attractive by its distinct neuronal growth inhibitory activity, which is not shared by other MT isoforms. The polypeptide chain of GIF is folded into two individual domains, which are connected by a highly conserved linker, KKS. In order to figure out the significance of the conserved segment, we constructed several mutants of human GIF (hGIF), including the K31/32A mutant, the K31/32E mutant and the KKS-SP mutant by site-directed mutagenesis. pH titration and DTNB reaction exhibited that all the three mutations made the β-domain lower in stability and looser. More significantly, change of KKS to SP also altered the general backbone conformation and metal-thiolate cluster geometry. Notably, bioassay results showed that the bioactivity of the K31/32A mutant and the K31/32E mutant decreased obviously, while the KKS-SP mutant lost inhibitory activity completely. Based on these results, we proposed that the KKS linker was a crucial factor in modulating the stability and the solvent accessibility of the Cd 3S 9 cluster in the β-domain through domain-domain interactions, thus was indispensable to the biological activity of hGIF. © 2009 Springer Science+Business Media, LLC.
Persistent Identifierhttp://hdl.handle.net/10722/168398
ISSN
2015 Impact Factor: 2.134
2015 SCImago Journal Rankings: 0.733
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorDing, ZCen_US
dc.contributor.authorTeng, XCen_US
dc.contributor.authorZheng, Qen_US
dc.contributor.authorNi, FYen_US
dc.contributor.authorCai, Ben_US
dc.contributor.authorWang, Yen_US
dc.contributor.authorZhou, GMen_US
dc.contributor.authorSun, HZen_US
dc.contributor.authorTan, XSen_US
dc.contributor.authorHuang, ZXen_US
dc.date.accessioned2012-10-08T03:18:28Z-
dc.date.available2012-10-08T03:18:28Z-
dc.date.issued2009en_US
dc.identifier.citationBiometals, 2009, v. 22 n. 5, p. 817-826en_US
dc.identifier.issn0966-0844en_US
dc.identifier.urihttp://hdl.handle.net/10722/168398-
dc.description.abstractMetallothinein-3 (MT3), also named neuronal growth inhibitory factor (GIF), is attractive by its distinct neuronal growth inhibitory activity, which is not shared by other MT isoforms. The polypeptide chain of GIF is folded into two individual domains, which are connected by a highly conserved linker, KKS. In order to figure out the significance of the conserved segment, we constructed several mutants of human GIF (hGIF), including the K31/32A mutant, the K31/32E mutant and the KKS-SP mutant by site-directed mutagenesis. pH titration and DTNB reaction exhibited that all the three mutations made the β-domain lower in stability and looser. More significantly, change of KKS to SP also altered the general backbone conformation and metal-thiolate cluster geometry. Notably, bioassay results showed that the bioactivity of the K31/32A mutant and the K31/32E mutant decreased obviously, while the KKS-SP mutant lost inhibitory activity completely. Based on these results, we proposed that the KKS linker was a crucial factor in modulating the stability and the solvent accessibility of the Cd 3S 9 cluster in the β-domain through domain-domain interactions, thus was indispensable to the biological activity of hGIF. © 2009 Springer Science+Business Media, LLC.en_US
dc.languageengen_US
dc.publisherSpringer New York LLC. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0966-0844en_US
dc.relation.ispartofBioMetalsen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCerebral Cortex - Cytology - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshMaleen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMutagenesis, Site-Directeden_US
dc.subject.meshMutationen_US
dc.subject.meshNerve Tissue Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshNeurons - Cytology - Metabolismen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Wistaren_US
dc.subject.meshSequence Homology, Amino Aciden_US
dc.titleImportant roles of the conserved linker-KKS in human neuronal growth inhibitory factoren_US
dc.typeArticleen_US
dc.identifier.emailSun, HZ:hsun@hkucc.hku.hken_US
dc.identifier.authoritySun, HZ=rp00777en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/s10534-009-9228-1en_US
dc.identifier.pmid19306065-
dc.identifier.scopuseid_2-s2.0-69249208643en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-69249208643&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume22en_US
dc.identifier.issue5en_US
dc.identifier.spage817en_US
dc.identifier.epage826en_US
dc.identifier.isiWOS:000269186300011-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridDing, ZC=14424225400en_US
dc.identifier.scopusauthoridTeng, XC=9842935500en_US
dc.identifier.scopusauthoridZheng, Q=36887872800en_US
dc.identifier.scopusauthoridNi, FY=9841840800en_US
dc.identifier.scopusauthoridCai, B=36484162900en_US
dc.identifier.scopusauthoridWang, Y=36078812500en_US
dc.identifier.scopusauthoridZhou, GM=8449295200en_US
dc.identifier.scopusauthoridSun, HZ=7404827446en_US
dc.identifier.scopusauthoridTan, XS=7202120913en_US
dc.identifier.scopusauthoridHuang, ZX=7406221847en_US
dc.identifier.citeulike4216759-

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