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- Publisher Website: 10.1096/fj.10-155242
- Scopus: eid_2-s2.0-77957831516
- PMID: 20581225
- WOS: WOS:000285005900038
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Article: Molecular interaction of flagellar export chaperone FliS and cochaperone HP1076 in Helicobacter pylori
Title | Molecular interaction of flagellar export chaperone FliS and cochaperone HP1076 in Helicobacter pylori | ||||||
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Authors | |||||||
Keywords | Bacterial motility Protein-protein interaction Type III secretion system Virulence factor | ||||||
Issue Date | 2010 | ||||||
Publisher | Federation 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? | ||||||
Abstract | Flagellar 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 Identifier | http://hdl.handle.net/10722/124506 | ||||||
ISSN | 2023 Impact Factor: 4.4 2023 SCImago Journal Rankings: 1.412 | ||||||
ISI Accession Number ID |
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 Field | Value | Language |
---|---|---|
dc.contributor.author | Lam, WWL | en_HK |
dc.contributor.author | Woo, EJ | en_HK |
dc.contributor.author | Kotaka, M | en_HK |
dc.contributor.author | Tam, WK | en_HK |
dc.contributor.author | Leung, YC | en_HK |
dc.contributor.author | Ling, TKW | en_HK |
dc.contributor.author | Au, SWN | en_HK |
dc.date.accessioned | 2010-10-31T10:38:16Z | - |
dc.date.available | 2010-10-31T10:38:16Z | - |
dc.date.issued | 2010 | en_HK |
dc.identifier.citation | Faseb Journal, 2010, v. 24 n. 10, p. 4020-4032 | en_HK |
dc.identifier.issn | 0892-6638 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/124506 | - |
dc.description.abstract | Flagellar 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.language | eng | en_HK |
dc.publisher | Federation of American Societies for Experimental Biology. The Journal's web site is located at http://www.fasebj.org/ | en_HK |
dc.relation.ispartof | FASEB Journal | en_HK |
dc.subject | Bacterial motility | en_HK |
dc.subject | Protein-protein interaction | en_HK |
dc.subject | Type III secretion system | en_HK |
dc.subject | Virulence factor | en_HK |
dc.subject.mesh | Amino Acid Sequence | - |
dc.subject.mesh | Bacterial Proteins - chemistry - metabolism | - |
dc.subject.mesh | Chromatography, Gel | - |
dc.subject.mesh | Helicobacter pylori - metabolism | - |
dc.subject.mesh | Molecular Chaperones - chemistry - metabolism | - |
dc.title | Molecular interaction of flagellar export chaperone FliS and cochaperone HP1076 in Helicobacter pylori | en_HK |
dc.type | Article | en_HK |
dc.identifier.openurl | http://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.email | Kotaka, M: masayo@hku.hk | en_HK |
dc.identifier.authority | Kotaka, M=rp00293 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1096/fj.10-155242 | en_HK |
dc.identifier.pmid | 20581225 | en_HK |
dc.identifier.scopus | eid_2-s2.0-77957831516 | en_HK |
dc.identifier.hkuros | 174875 | en_HK |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-77957831516&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 24 | en_HK |
dc.identifier.issue | 10 | en_HK |
dc.identifier.spage | 4020 | en_HK |
dc.identifier.epage | 4032 | en_HK |
dc.identifier.eissn | 1530-6860 | - |
dc.identifier.isi | WOS:000285005900038 | - |
dc.publisher.place | United States | en_HK |
dc.identifier.scopusauthorid | Lam, WWL=36478889000 | en_HK |
dc.identifier.scopusauthorid | Woo, EJ=7103371205 | en_HK |
dc.identifier.scopusauthorid | Kotaka, M=6604073578 | en_HK |
dc.identifier.scopusauthorid | Tam, WK=36704239300 | en_HK |
dc.identifier.scopusauthorid | Leung, YC=35074432700 | en_HK |
dc.identifier.scopusauthorid | Ling, TKW=13310253900 | en_HK |
dc.identifier.scopusauthorid | Au, SWN=7005457819 | en_HK |
dc.identifier.issnl | 0892-6638 | - |