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Article: Molecular interaction of flagellar export chaperone FliS and cochaperone HP1076 in Helicobacter pylori

TitleMolecular interaction of flagellar export chaperone FliS and cochaperone HP1076 in Helicobacter pylori
Authors
KeywordsBacterial motility
Protein-protein interaction
Type III secretion system
Virulence factor
Issue Date2010
PublisherFederation of American Societies for Experimental Biology. The Journal's web site is located at http://www.fasebj.org/
Citation
Faseb Journal, 2010, v. 24 n. 10, p. 4020-4032 How to Cite?
AbstractFlagellar export chaperone FliS prevents premature polymerization of flagellins and is critical for flagellar assembly and bacterial colonization. Previously, a yeast 2-hybrid study identified various FliS-associated proteins in Helicobacter pylori, but the implications of these interactions are not known. Here we demonstrate the biophysical interaction of FliS (HP0753) and the uncharacterized protein HP1076 from H. pylori. HP1076 possesses a cochaperone activity that promotes the folding and chaperone activity of FliS. We further determined the crystal structures of FliS, HP1076, and the binary complex at 2.7, 1.8, and 2.7 Å resolution, respectively. HP1076 adopts a helix-rich bundle structure and interestingly shares a similar fold with a flagellin homologue, hook-associated protein, and FliS. The FliS-HP1076 complex revealed an extensive electrostatic and hydrophobic binding interface, which is distinct from the flagellin binding pocket in FliS. The helical stacking interaction between HP1076 and FliS suggests that HP1076 stabilizes 2 α helices of FliS and therefore the overall structure of the bundle. Our findings provide new insights into flagellar export chaperones and may have implications for other secretion chaperones in the type III secretion system. © FASEB.
Persistent Identifierhttp://hdl.handle.net/10722/124506
ISSN
2015 Impact Factor: 5.299
2015 SCImago Journal Rankings: 2.775
ISI Accession Number ID
Funding AgencyGrant Number
Research Grants Council of Hong KongCUHK 4592/06M
University Grants Council of the Hong KongSEG CUHK08
Funding Information:

This work was supported by a Competitive Earmarked Research grant (CUHK 4592/06M) from the Research Grants Council of Hong Kong. The authors thank the University Grants Council of the Hong Kong Special Administrative Region One-Off Special Equipment Grant (SEG CUHK08) for the equipment used in this work. W.W.L. performed the molecular and biochemical experiments, crystallization, and data analysis and prepared the manuscript; E.J.W. contributed to the data collection and phase determination of HP1076; M.K. contributed to the data collection of the binary complex; Y.C.L. assisted in the ITC assay; W.K.T. assisted the molecular cloning; K.W.L. was involved in collaboration and discussion; and S.W.N.A. supervised the research and prepared the manuscript.

References

 

DC FieldValueLanguage
dc.contributor.authorLam, WWLen_HK
dc.contributor.authorWoo, EJen_HK
dc.contributor.authorKotaka, Men_HK
dc.contributor.authorTam, WKen_HK
dc.contributor.authorLeung, YCen_HK
dc.contributor.authorLing, TKWen_HK
dc.contributor.authorAu, SWNen_HK
dc.date.accessioned2010-10-31T10:38:16Z-
dc.date.available2010-10-31T10:38:16Z-
dc.date.issued2010en_HK
dc.identifier.citationFaseb Journal, 2010, v. 24 n. 10, p. 4020-4032en_HK
dc.identifier.issn0892-6638en_HK
dc.identifier.urihttp://hdl.handle.net/10722/124506-
dc.description.abstractFlagellar export chaperone FliS prevents premature polymerization of flagellins and is critical for flagellar assembly and bacterial colonization. Previously, a yeast 2-hybrid study identified various FliS-associated proteins in Helicobacter pylori, but the implications of these interactions are not known. Here we demonstrate the biophysical interaction of FliS (HP0753) and the uncharacterized protein HP1076 from H. pylori. HP1076 possesses a cochaperone activity that promotes the folding and chaperone activity of FliS. We further determined the crystal structures of FliS, HP1076, and the binary complex at 2.7, 1.8, and 2.7 Å resolution, respectively. HP1076 adopts a helix-rich bundle structure and interestingly shares a similar fold with a flagellin homologue, hook-associated protein, and FliS. The FliS-HP1076 complex revealed an extensive electrostatic and hydrophobic binding interface, which is distinct from the flagellin binding pocket in FliS. The helical stacking interaction between HP1076 and FliS suggests that HP1076 stabilizes 2 α helices of FliS and therefore the overall structure of the bundle. Our findings provide new insights into flagellar export chaperones and may have implications for other secretion chaperones in the type III secretion system. © FASEB.en_HK
dc.languageengen_HK
dc.publisherFederation of American Societies for Experimental Biology. The Journal's web site is located at http://www.fasebj.org/en_HK
dc.relation.ispartofFASEB Journalen_HK
dc.subjectBacterial motilityen_HK
dc.subjectProtein-protein interactionen_HK
dc.subjectType III secretion systemen_HK
dc.subjectVirulence factoren_HK
dc.subject.meshAmino Acid Sequence-
dc.subject.meshBacterial Proteins - chemistry - metabolism-
dc.subject.meshChromatography, Gel-
dc.subject.meshHelicobacter pylori - metabolism-
dc.subject.meshMolecular Chaperones - chemistry - metabolism-
dc.titleMolecular interaction of flagellar export chaperone FliS and cochaperone HP1076 in Helicobacter pylorien_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0892-6638&volume=24&issue=10&spage=4020&epage=4032&date=2010&atitle=Molecular+interaction+of+flagellar+export+chaperone+FliS+and+cochaperone+HP1076+in+Helicobacter+pylori-
dc.identifier.emailKotaka, M: masayo@hku.hken_HK
dc.identifier.authorityKotaka, M=rp00293en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1096/fj.10-155242en_HK
dc.identifier.pmid20581225en_HK
dc.identifier.scopuseid_2-s2.0-77957831516en_HK
dc.identifier.hkuros174875en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77957831516&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume24en_HK
dc.identifier.issue10en_HK
dc.identifier.spage4020en_HK
dc.identifier.epage4032en_HK
dc.identifier.eissn1530-6860-
dc.identifier.isiWOS:000285005900038-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLam, WWL=36478889000en_HK
dc.identifier.scopusauthoridWoo, EJ=7103371205en_HK
dc.identifier.scopusauthoridKotaka, M=6604073578en_HK
dc.identifier.scopusauthoridTam, WK=36704239300en_HK
dc.identifier.scopusauthoridLeung, YC=35074432700en_HK
dc.identifier.scopusauthoridLing, TKW=13310253900en_HK
dc.identifier.scopusauthoridAu, SWN=7005457819en_HK

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