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Volumn 193, Issue 19, 2011, Pages 5514-5519

Quantitative proteomic analysis reveals formation of an EscL-EscQ-EscN type III complex in enteropathogenic Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

EID: 80053591783     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.05235-11     Document Type: Note
Times cited : (33)

References (33)
  • 1
    • 0037053426 scopus 로고    scopus 로고
    • Intrinsic membrane targeting of the flagellar export ATPase FliI: interaction with acidic phospholipids and FliH
    • Auvray, F., A. J. Ozin, L. Claret, and C. Hughes. 2002. Intrinsic membrane targeting of the flagellar export ATPase FliI: interaction with acidic phospholipids and FliH. J. Mol. Biol. 318:941-950.
    • (2002) J. Mol. Biol. , vol.318 , pp. 941-950
    • Auvray, F.1    Ozin, A.J.2    Claret, L.3    Hughes, C.4
  • 2
    • 33646543996 scopus 로고    scopus 로고
    • Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator,YscL
    • Blaylock, B., K. E. Riordan, D. M. Missiakas, and O. Schneewind. 2006. Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator, YscL. J. Bacteriol. 188:3525-3534.
    • (2006) J. Bacteriol. , vol.188 , pp. 3525-3534
    • Blaylock, B.1    Riordan, K.E.2    Missiakas, D.M.3    Schneewind, O.4
  • 3
    • 12144289554 scopus 로고    scopus 로고
    • Dissecting virulence: systematic and functional analyses of a pathogenicity island
    • Deng, W., et al. 2004. Dissecting virulence: systematic and functional analyses of a pathogenicity island. Proc. Natl. Acad. Sci. U. S. A. 101:3597-3602.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 3597-3602
    • Deng, W.1
  • 4
    • 0031895930 scopus 로고    scopus 로고
    • The complete sequence of the locus of enterocyte effacement (LEE) from enteropathogenic Escherichia coli E2348/69
    • Elliott, S. J., et al. 1998. The complete sequence of the locus of enterocyte effacement (LEE) from enteropathogenic Escherichia coli E2348/69. Mol. Microbiol. 28:1-4.
    • (1998) Mol. Microbiol. , vol.28 , pp. 1-4
    • Elliott, S.J.1
  • 5
    • 0345827609 scopus 로고    scopus 로고
    • Structure of HrcQB-C, a conserved component of the bacterial type III secretion systems
    • Fadouloglou, V. E., et al. 2004. Structure of HrcQB-C, a conserved component of the bacterial type III secretion systems. Proc. Natl. Acad. Sci. U. S. A. 101:70-75.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 70-75
    • Fadouloglou, V.E.1
  • 6
    • 0344825097 scopus 로고    scopus 로고
    • Translocated intimin receptor and its chaperone interact with ATPase of the type III secretion apparatus of enteropathogenic Escherichia coli
    • Gauthier, A., and B. B. Finlay. 2003. Translocated intimin receptor and its chaperone interact with ATPase of the type III secretion apparatus of enteropathogenic Escherichia coli. J. Bacteriol. 185:6747-6755.
    • (2003) J. Bacteriol. , vol.185 , pp. 6747-6755
    • Gauthier, A.1    Finlay, B.B.2
  • 7
    • 0038187635 scopus 로고    scopus 로고
    • Secretin of the enteropathogenic Escherichia coli type III secretion system requires components of the type III apparatus for assembly and localization
    • Gauthier, A., J. L. Puente, and B. B. Finlay. 2003. Secretin of the enteropathogenic Escherichia coli type III secretion system requires components of the type III apparatus for assembly and localization. Infect. Immun. 71:3310- 3319.
    • (2003) Infect. Immun. , vol.71 , pp. 3310-3319
    • Gauthier, A.1    Puente, J.L.2    Finlay, B.B.3
  • 8
    • 25844524137 scopus 로고    scopus 로고
    • Transcriptional inhibitor of virulence factors in enteropathogenic Escherichia coli
    • Gauthier, A., et al. 2005. Transcriptional inhibitor of virulence factors in enteropathogenic Escherichia coli. Antimicrob. Agents Chemother. 49:4101- 4109.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 4101-4109
    • Gauthier, A.1
  • 9
    • 33646435299 scopus 로고    scopus 로고
    • Interactions between C ring proteins and export apparatus components: a possible mechanism for facilitating type III protein export
    • González-Pedrajo, B., T. Minamino, M. Kihara, and K. Namba. 2006. Interactions between C ring proteins and export apparatus components: a possible mechanism for facilitating type III protein export. Mol. Microbiol. 60:984-998.
    • (2006) Mol. Microbiol. , vol.60 , pp. 984-998
    • González-Pedrajo, B.1    Minamino, T.2    Kihara, M.3    Namba, K.4
  • 10
    • 0033564208 scopus 로고    scopus 로고
    • Protein tyrosine kinases in bacterial pathogens are associated with virulence and production of exopolysaccharide
    • Ilan, O., et al. 1999. Protein tyrosine kinases in bacterial pathogens are associated with virulence and production of exopolysaccharide. EMBO J. 18:3241-3248.
    • (1999) EMBO J , vol.18 , pp. 3241-3248
    • Ilan, O.1
  • 11
    • 0034193707 scopus 로고    scopus 로고
    • Interactions between type III secretion apparatus components from Yersinia pestis detected using the yeast two-hybrid system
    • Jackson, M. W., and G. V. Plano. 2000. Interactions between type III secretion apparatus components from Yersinia pestis detected using the yeast two-hybrid system. FEMS Microbiol. Lett. 186:85-90.
    • (2000) FEMS Microbiol. Lett. , vol.186 , pp. 85-90
    • Jackson, M.W.1    Plano, G.V.2
  • 12
    • 0025047435 scopus 로고
    • A genetic locus of enteropathogenic Escherichia coli necessary for the production of attaching and effacing lesions on tissue culture cells
    • Jerse, A. E., J. Yu, B. D. Tall, and J. B. Kaper. 1990. A genetic locus of enteropathogenic Escherichia coli necessary for the production of attaching and effacing lesions on tissue culture cells. Proc. Natl. Acad. Sci. U. S. A. 87:7839-7843.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 7839-7843
    • Jerse, A.E.1    Yu, J.2    Tall, B.D.3    Kaper, J.B.4
  • 13
    • 41949121055 scopus 로고    scopus 로고
    • Interactions between CdsD, CdsQ, and CdsL, three putative Chlamydophila pneumoniae type III secretion proteins
    • Johnson, D. L., C. B. Stone, and J. B. Mahony. 2008. Interactions between CdsD, CdsQ, and CdsL, three putative Chlamydophila pneumoniae type III secretion proteins. J. Bacteriol. 190:2972-2980.
    • (2008) J. Bacteriol. , vol.190 , pp. 2972-2980
    • Johnson, D.L.1    Stone, C.B.2    Mahony, J.B.3
  • 14
    • 0025837193 scopus 로고
    • A wide-host-range suicide vector for improving reverse genetics in gram-negative bacteria: inactivation of the blaA gene of Yersinia enterocolitica
    • Kaniga, K., I. Delor, and G. R. Cornelis. 1991. A wide-host-range suicide vector for improving reverse genetics in gram-negative bacteria: inactivation of the blaA gene of Yersinia enterocolitica. Gene 109:137-141.
    • (1991) Gene , vol.109 , pp. 137-141
    • Kaniga, K.1    Delor, I.2    Cornelis, G.R.3
  • 15
    • 0023073670 scopus 로고
    • Adhesion of enteropathogenic Escherichia coli to human intestinal enterocytes and cultured human intestinal mucosa
    • Knutton, S., D. R. Lloyd, and A. S. McNeish. 1987. Adhesion of enteropathogenic Escherichia coli to human intestinal enterocytes and cultured human intestinal mucosa. Infect. Immun. 55:69-77.
    • (1987) Infect. Immun. , vol.55 , pp. 69-77
    • Knutton, S.1    Lloyd, D.R.2    McNeish, A.S.3
  • 16
    • 59449101504 scopus 로고    scopus 로고
    • Identification of a third EspA-binding protein that forms part of the type III secretion system of enterohemorrhagic Escherichia coli
    • Ku, C. P., J. C. Lio, S. H. Wang, C. N. Lin, and W. J. Syu. 2009. Identification of a third EspA-binding protein that forms part of the type III secretion system of enterohemorrhagic Escherichia coli. J. Biol. Chem. 284:1686-1693.
    • (2009) J. Biol. Chem. , vol.284 , pp. 1686-1693
    • Ku, C.P.1    Lio, J.C.2    Wang, S.H.3    Lin, C.N.4    Syu, W.J.5
  • 17
    • 79952280754 scopus 로고    scopus 로고
    • A sorting platform determines the order of protein secretion in bacterial type III systems
    • Lara-Tejero, M., J. Kato, S. Wagner, X. Liu, and J. E. Galan. 2011. A sorting platform determines the order of protein secretion in bacterial type III systems. Science 331:1188-1191.
    • (2011) Science , vol.331 , pp. 1188-1191
    • Lara-Tejero, M.1    Kato, J.2    Wagner, S.3    Liu, X.4    Galan, J.E.5
  • 18
    • 13444262384 scopus 로고    scopus 로고
    • CDD: a conserved domain database for protein classification
    • Marchler-Bauer, A., et al. 2005. CDD: a conserved domain database for protein classification. Nucleic Acids Res. 33:D192-D196.
    • (2005) Nucleic Acids Res , vol.33
    • Marchler-Bauer, A.1
  • 19
    • 33749330451 scopus 로고    scopus 로고
    • The FliNFliH interaction mediates localization of flagellar export ATPase FliI to the C ring complex
    • McMurry, J. L., J. W. Murphy, and B. Gonzalez-Pedrajo. 2006. The FliNFliH interaction mediates localization of flagellar export ATPase FliI to the C ring complex. Biochemistry 45:11790-11798.
    • (2006) Biochemistry , vol.45 , pp. 11790-11798
    • McMurry, J.L.1    Murphy, J.W.2    Gonzalez-Pedrajo, B.3
  • 20
    • 0037701404 scopus 로고    scopus 로고
    • The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH
    • Minamino, T., B. Gonzalez-Pedrajo, M. Kihara, K. Namba, and R. M. Macnab. 2003. The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH. J. Bacteriol. 185:3983-3988.
    • (2003) J. Bacteriol. , vol.185 , pp. 3983-3988
    • Minamino, T.1    Gonzalez-Pedrajo, B.2    Kihara, M.3    Namba, K.4    Macnab, R.M.5
  • 21
    • 0033779545 scopus 로고    scopus 로고
    • FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity
    • Minamino, T., and R. M. MacNab. 2000. FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity. Mol. Microbiol. 37:1494-1503.
    • (2000) Mol. Microbiol. , vol.37 , pp. 1494-1503
    • Minamino, T.1    MacNab, R.M.2
  • 22
    • 72049109167 scopus 로고    scopus 로고
    • Roles of the extreme N-terminal region of FliH for efficient localization of the FliH-FliI complex to the bacterial flagellar type III export apparatus
    • Minamino, T., et al. 2009. Roles of the extreme N-terminal region of FliH for efficient localization of the FliH-FliI complex to the bacterial flagellar type III export apparatus. Mol. Microbiol. 74:1471-1483.
    • (2009) Mol. Microbiol. , vol.74 , pp. 1471-1483
    • Minamino, T.1
  • 23
    • 33644860766 scopus 로고    scopus 로고
    • Shigella Spa33 is an essential C-ring component of type III secretion machinery
    • Morita-Ishihara, T., et al. 2006. Shigella Spa33 is an essential C-ring component of type III secretion machinery. J. Biol. Chem. 281:599-607.
    • (2006) J. Biol. Chem. , vol.281 , pp. 599-607
    • Morita-Ishihara, T.1
  • 24
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., et al. 2002. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1:376-386.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1
  • 25
    • 18944390249 scopus 로고    scopus 로고
    • Bioinformatics analysis of the locus for enterocyte effacement provides novel insights into type-III secretion
    • Pallen, M. J., S. A. Beatson, and C. M. Bailey. 2005. Bioinformatics analysis of the locus for enterocyte effacement provides novel insights into type-III secretion. BMC Microbiol. 5:9.
    • (2005) BMC Microbiol , vol.5 , pp. 9
    • Pallen, M.J.1    Beatson, S.A.2    Bailey, C.M.3
  • 26
    • 33645233315 scopus 로고    scopus 로고
    • Organization of FliN subunits in the flagellar motor of Escherichia coli
    • Paul, K., and D. F. Blair. 2006. Organization of FliN subunits in the flagellar motor of Escherichia coli. J. Bacteriol. 188:2502-2511.
    • (2006) J. Bacteriol. , vol.188 , pp. 2502-2511
    • Paul, K.1    Blair, D.F.2
  • 27
    • 43849108709 scopus 로고    scopus 로고
    • Identification of cognate host targets and specific ubiquitylation sites on the Salmonella SPI-1 effector SopB/SigD
    • Rogers, L. D., et al. 2008. Identification of cognate host targets and specific ubiquitylation sites on the Salmonella SPI-1 effector SopB/SigD. J. Proteomics 71:97-108.
    • (2008) J. Proteomics , vol.71 , pp. 97-108
    • Rogers, L.D.1
  • 28
    • 33845869544 scopus 로고    scopus 로고
    • Structural organization of the needle complex of the type III secretion apparatus of Shigella flexneri
    • Sani, M., et al. 2007. Structural organization of the needle complex of the type III secretion apparatus of Shigella flexneri. Micron 38:291-301.
    • (2007) Micron , vol.38 , pp. 291-301
    • Sani, M.1
  • 29
    • 77954067915 scopus 로고    scopus 로고
    • Topology and organization of the Salmonella typhimurium type III secretion needle complex components
    • Schraidt, O., et al. 2010. Topology and organization of the Salmonella typhimurium type III secretion needle complex components. PLoS Pathog. 6:e1000824.
    • (2010) PLoS Pathog , vol.6
    • Schraidt, O.1
  • 30
    • 0035949491 scopus 로고    scopus 로고
    • Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure
    • Sekiya, K., et al. 2001. Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure. Proc. Natl. Acad. Sci. U. S. A. 98:11638-11643.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11638-11643
    • Sekiya, K.1
  • 31
    • 66149092022 scopus 로고    scopus 로고
    • A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system
    • Spreter, T., et al. 2009. A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system. Nat. Struct. Mol. Biol. 16:468-476.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 468-476
    • Spreter, T.1
  • 32
    • 1642305413 scopus 로고    scopus 로고
    • Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export
    • Thomas, J., G. P. Stafford, and C. Hughes. 2004. Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export. Proc. Natl. Acad. Sci. U. S. A. 101:3945-3950.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 3945-3950
    • Thomas, J.1    Stafford, G.P.2    Hughes, C.3
  • 33
    • 25144508100 scopus 로고    scopus 로고
    • CesT is a multi-effector chaperone and recruitment factor required for the efficient type III secretion of both LEE- and non-LEE-encoded effectors of enteropathogenic Escherichia coli
    • Thomas, N. A., et al. 2005. CesT is a multi-effector chaperone and recruitment factor required for the efficient type III secretion of both LEE- and non-LEE-encoded effectors of enteropathogenic Escherichia coli. Mol. Microbiol. 57:1762-1779.
    • (2005) Mol. Microbiol. , vol.57 , pp. 1762-1779
    • Thomas, N.A.1


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