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Volumn 193, Issue 23, 2011, Pages 6683-6700

Impact of the N-terminal secretor domain on YopD translocator function in Yersinia pseudotuberculosis type III secretion

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; HYBRID PROTEIN; UNCLASSIFIED DRUG; YERSINIA OUTER PROTEIN D; YERSINIA OUTER PROTEIN E; OUTER MEMBRANE PROTEIN; YOPD PROTEIN, YERSINIA;

EID: 84855374962     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00210-11     Document Type: Article
Times cited : (18)

References (87)
  • 1
    • 33646358945 scopus 로고    scopus 로고
    • Functional analysis of the YopE GTPase-activating protein (GAP) activity of Yersinia pseudotuberculosis
    • Aili, M., E. L. Isaksson, B. Hallberg, H. Wolf-Watz, and R. Rosqvist. 2006. Functional analysis of the YopE GTPase-activating protein (GAP) activity of Yersinia pseudotuberculosis. Cell Microbiol. 8:1020-1033.
    • (2006) Cell Microbiol. , vol.8 , pp. 1020-1033
    • Aili, M.1    Isaksson, E.L.2    Hallberg, B.3    Wolf-Watz, H.4    Rosqvist, R.5
  • 2
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type III secretion
    • Akeda, Y., and J. E. Galan. 2005. Chaperone release and unfolding of substrates in type III secretion. Nature 437:911-915.
    • (2005) Nature , vol.437 , pp. 911-915
    • Akeda, Y.1    Galan, J.E.2
  • 3
    • 79952126769 scopus 로고    scopus 로고
    • Translocation of surface-localized effectors in type III secretion
    • Akopyan, K., et al. 2011. Translocation of surface-localized effectors in type III secretion. Proc. Natl. Acad. Sci. U. S. A. 108:1639-1644.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 1639-1644
    • Akopyan, K.1
  • 4
    • 0036182095 scopus 로고    scopus 로고
    • YopD and LcrH regulate expression of Yersinia enterocolitica YopQ by a posttranscriptional mechanism and bind to yopQ RNA
    • Anderson, D. M., K. S. Ramamurthi, C. Tam, and O. Schneewind. 2002. YopD and LcrH regulate expression of Yersinia enterocolitica YopQ by a posttranscriptional mechanism and bind to yopQ RNA. J. Bacteriol. 184:1287-1295.
    • (2002) J. Bacteriol. , vol.184 , pp. 1287-1295
    • Anderson, D.M.1    Ramamurthi, K.S.2    Tam, C.3    Schneewind, O.4
  • 5
    • 0032959552 scopus 로고    scopus 로고
    • Yersinia pseudotuberculosis-induced calcium signaling in neutrophils is blocked by the virulence effector YopH
    • Andersson, K., K. E. Magnusson, M. Majeed, O. Stendahl, and M. Fallman. 1999. Yersinia pseudotuberculosis-induced calcium signaling in neutrophils is blocked by the virulence effector YopH. Infect. Immun. 67:2567-2574.
    • (1999) Infect. Immun. , vol.67 , pp. 2567-2574
    • Andersson, K.1    Magnusson, K.E.2    Majeed, M.3    Stendahl, O.4    Fallman, M.5
  • 6
    • 66349124179 scopus 로고    scopus 로고
    • Sequence-based prediction of type III secreted proteins
    • Arnold, R., et al. 2009. Sequence-based prediction of type III secreted proteins. PLoS Pathog. 5:e1000376.
    • (2009) PLoS Pathog. , vol.5
    • Arnold, R.1
  • 7
    • 19044376774 scopus 로고    scopus 로고
    • The Yersinia YopE and YopH type III effector proteins enhance bacterial proliferation following contact with eukaryotic cells
    • Bartra, S., P. Cherepanov, A. Forsberg, and K. Schesser. 2001. The Yersinia YopE and YopH type III effector proteins enhance bacterial proliferation following contact with eukaryotic cells. BMC Microbiol. 1:22.
    • (2001) BMC Microbiol. , vol.1 , pp. 22
    • Bartra, S.1    Cherepanov, P.2    Forsberg, A.3    Schesser, K.4
  • 8
    • 67649400614 scopus 로고    scopus 로고
    • Autoproteolysis of YscU of Yersinia pseudotuberculosis is important for regulation of expression and secretion of Yop proteins
    • Björnfot, A. C., M. Lavander, A. Forsberg, and H. Wolf-Watz. 2009. Autoproteolysis of YscU of Yersinia pseudotuberculosis is important for regulation of expression and secretion of Yop proteins. J. Bacteriol. 191:4259-4267.
    • (2009) J. Bacteriol. , vol.191 , pp. 4259-4267
    • Björnfot, A.C.1    Lavander, M.2    Forsberg, A.3    Wolf-Watz, H.4
  • 9
    • 55349145620 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion of YopR requires a structure in its mRNA
    • Blaylock, B., J. A. Sorg, and O. Schneewind. 2008. Yersinia enterocolitica type III secretion of YopR requires a structure in its mRNA. Mol. Microbiol. 70:1210-1222.
    • (2008) Mol. Microbiol. , vol.70 , pp. 1210-1222
    • Blaylock, B.1    Sorg, J.A.2    Schneewind, O.3
  • 10
    • 77953225894 scopus 로고    scopus 로고
    • Salmonella pathogenicity island 1 (SPI-1) type III secretion of SopD involves N- and C-terminal signals and direct binding to the InvC ATPase
    • Boonyom, R., M. H. Karavolos, D. M. Bulmer, and C. M. Khan. 2010. Salmonella pathogenicity island 1 (SPI-1) type III secretion of SopD involves N- and C-terminal signals and direct binding to the InvC ATPase. Microbiology 156:1805-1814.
    • (2010) Microbiology , vol.156 , pp. 1805-1814
    • Boonyom, R.1    Karavolos, M.H.2    Bulmer, D.M.3    Khan, C.M.4
  • 11
    • 58149302495 scopus 로고    scopus 로고
    • MxiC is secreted by and controls the substrate specificity of the Shigella flexneri type III secretion apparatus
    • Botteaux, A., M. P. Sory, L. Biskri, C. Parsot, and A. Allaoui. 2009. MxiC is secreted by and controls the substrate specificity of the Shigella flexneri type III secretion apparatus. Mol. Microbiol. 71:449-460.
    • (2009) Mol. Microbiol. , vol.71 , pp. 449-460
    • Botteaux, A.1    Sory, M.P.2    Biskri, L.3    Parsot, C.4    Allaoui, A.5
  • 12
    • 36749036576 scopus 로고    scopus 로고
    • Diminished LcrV secretion attenuates Yersinia pseudotuberculosis virulence
    • Bröms, J. E., M. S. Francis, and A. Forsberg. 2007. Diminished LcrV secretion attenuates Yersinia pseudotuberculosis virulence. J. Bacteriol. 189:8417-8429.
    • (2007) J. Bacteriol. , vol.189 , pp. 8417-8429
    • Bröms, J.E.1    Francis, M.S.2    Forsberg, A.3
  • 13
    • 0036838012 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion: yscM1 and yscM2 regulate yop gene expression by a posttranscriptional mechanism that targets the 5′ untranslated region of yop mRNA
    • Cambronne, E. D., and O. Schneewind. 2002. Yersinia enterocolitica type III secretion: yscM1 and yscM2 regulate yop gene expression by a posttranscriptional mechanism that targets the 5′ untranslated region of yop mRNA. J. Bacteriol. 184:5880-5893.
    • (2002) J. Bacteriol. , vol.184 , pp. 5880-5893
    • Cambronne, E.D.1    Schneewind, O.2
  • 14
    • 34547616133 scopus 로고    scopus 로고
    • Extracytoplasmic- stress-responsive pathways modulate type III secretion in Yersinia pseudotuberculosis
    • Carlsson, K. E., J. Liu, P. J. Edqvist, and M. S. Francis. 2007. Extracytoplasmic- stress-responsive pathways modulate type III secretion in Yersinia pseudotuberculosis. Infect. Immun. 75:3913-3924.
    • (2007) Infect. Immun. , vol.75 , pp. 3913-3924
    • Carlsson, K.E.1    Liu, J.2    Edqvist, P.J.3    Francis, M.S.4
  • 15
    • 77649251845 scopus 로고    scopus 로고
    • Structural and biochemical characterization of SrcA, a multi-cargo type III secretion chaperone in Salmonella required for pathogenic association with a host
    • Cooper, C. A., et al. 2010. Structural and biochemical characterization of SrcA, a multi-cargo type III secretion chaperone in Salmonella required for pathogenic association with a host. PLoS Pathog. 6:e1000751.
    • (2010) PLoS Pathog. , vol.6
    • Cooper, C.A.1
  • 16
    • 0345257863 scopus 로고    scopus 로고
    • How Yops find their way out of Yersinia
    • Cornelis, G. R. 2003. How Yops find their way out of Yersinia. Mol. Microbiol. 50:1091-1094.
    • (2003) Mol. Microbiol. , vol.50 , pp. 1091-1094
    • Cornelis, G.R.1
  • 17
    • 77955495219 scopus 로고    scopus 로고
    • YopD self-assembly and binding to LcrV facilitate type III secretion activity by Yersinia pseudotuberculosis
    • Costa, T. R., et al. 2010. YopD self-assembly and binding to LcrV facilitate type III secretion activity by Yersinia pseudotuberculosis. J. Biol. Chem. 285:25269-25284.
    • (2010) J. Biol. Chem. , vol.285 , pp. 25269-25284
    • Costa, T.R.1
  • 18
    • 20144387135 scopus 로고    scopus 로고
    • Regulation of type III secretion hierarchy of translocators and effectors in attaching and effacing bacterial pathogens
    • Deng, W., et al. 2005. Regulation of type III secretion hierarchy of translocators and effectors in attaching and effacing bacterial pathogens. Infect. Immun. 73:2135-2146.
    • (2005) Infect. Immun. , vol.73 , pp. 2135-2146
    • Deng, W.1
  • 19
    • 33846866251 scopus 로고    scopus 로고
    • Minimal YopB and YopD translocator secretion by Yersinia is sufficient for Yop-effector delivery into target cells
    • Edqvist, P. J., M. Aili, J. Liu, and M. S. Francis. 2007. Minimal YopB and YopD translocator secretion by Yersinia is sufficient for Yop-effector delivery into target cells. Microbes Infect. 9:224-233.
    • (2007) Microbes Infect. , vol.9 , pp. 224-233
    • Edqvist, P.J.1    Aili, M.2    Liu, J.3    Francis, M.S.4
  • 20
    • 33645093201 scopus 로고    scopus 로고
    • Tetratricopeptide repeats in the type-III-secretion chaperone, LcrH: their role in substrate binding and secretion
    • Edqvist, P. J., et al. 2006. Tetratricopeptide repeats in the type-III-secretion chaperone, LcrH: their role in substrate binding and secretion. Mol. Microbiol. 59:31-44.
    • (2006) Mol. Microbiol. , vol.59 , pp. 31-44
    • Edqvist, P.J.1
  • 22
    • 62549099973 scopus 로고    scopus 로고
    • Selective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO
    • Evans, L. D., and C. Hughes. 2009. Selective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO. FEMS Microbiol. Lett. 293:292-297.
    • (2009) FEMS Microbiol. Lett. , vol.293 , pp. 292-297
    • Evans, L.D.1    Hughes, C.2
  • 24
    • 0036436338 scopus 로고    scopus 로고
    • SycE allows secretion of YopE-DHFR hybrids by the Yersinia enterocolitica type III Ysc system
    • Feldman, M. F., S. Muller, E. Wuest, and G. R. Cornelis. 2002. SycE allows secretion of YopE-DHFR hybrids by the Yersinia enterocolitica type III Ysc system. Mol. Microbiol. 46:1183-1197.
    • (2002) Mol. Microbiol. , vol.46 , pp. 1183-1197
    • Feldman, M.F.1    Muller, S.2    Wuest, E.3    Cornelis, G.R.4
  • 25
    • 0025762461 scopus 로고
    • The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculosis
    • Forsberg, Å., A. M. Viitanen, M. Skurnik, and H. Wolf-Watz. 1991. The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculosis. Mol. Microbiol. 5:977-986.
    • (1991) Mol. Microbiol. , vol.5 , pp. 977-986
    • Forsberg, Å.1    Viitanen, A.M.2    Skurnik, M.3    Wolf-Watz, H.4
  • 26
    • 84855778073 scopus 로고    scopus 로고
    • Type III secretion chaperones: a molecular toolkit for all occasions
    • P. Durante and L. Colucci (ed.), Nova Science Publishers, Inc., Hauppauge, NY
    • Francis, M. S. 2010. Type III secretion chaperones: a molecular toolkit for all occasions, p. 79-147. In P. Durante and L. Colucci (ed.), Handbook of molecular chaperones: roles, structures and mechanisms. Nova Science Publishers, Inc., Hauppauge, NY.
    • (2010) Handbook of molecular chaperones: roles, structures and mechanisms , pp. 79-147
    • Francis, M.S.1
  • 27
    • 0033810428 scopus 로고    scopus 로고
    • A study of the YopD-LcrH interaction from Yersinia pseudotuberculosis reveals a role for hydrophobic residues within the amphipathic domain of YopD
    • Francis, M. S., M. Aili, M. L. Wiklund, and H. Wolf-Watz. 2000. A study of the YopD-LcrH interaction from Yersinia pseudotuberculosis reveals a role for hydrophobic residues within the amphipathic domain of YopD. Mol. Microbiol. 38:85-102.
    • (2000) Mol. Microbiol. , vol.38 , pp. 85-102
    • Francis, M.S.1    Aili, M.2    Wiklund, M.L.3    Wolf-Watz, H.4
  • 28
    • 0035170435 scopus 로고    scopus 로고
    • The type III secretion chaperone LcrH co-operates with YopD to establish a negative, regulatory loop for control of Yop synthesis in Yersinia pseudotuberculosis
    • Francis, M. S., S. A. Lloyd, and H. Wolf-Watz. 2001. The type III secretion chaperone LcrH co-operates with YopD to establish a negative, regulatory loop for control of Yop synthesis in Yersinia pseudotuberculosis. Mol. Microbiol. 42:1075-1093.
    • (2001) Mol. Microbiol. , vol.42 , pp. 1075-1093
    • Francis, M.S.1    Lloyd, S.A.2    Wolf-Watz, H.3
  • 29
    • 0031928329 scopus 로고    scopus 로고
    • YopD of Yersinia pseudotuberculosis is translocated into the cytosol of HeLa epithelial cells: evidence of a structural domain necessary for translocation
    • Francis, M. S., and H. Wolf-Watz. 1998. YopD of Yersinia pseudotuberculosis is translocated into the cytosol of HeLa epithelial cells: evidence of a structural domain necessary for translocation. Mol. Microbiol. 29:799-813.
    • (1998) Mol. Microbiol. , vol.29 , pp. 799-813
    • Francis, M.S.1    Wolf-Watz, H.2
  • 30
    • 77951722801 scopus 로고    scopus 로고
    • How the sequence of a gene can tune its translation
    • Fredrick, K., and M. Ibba. 2010. How the sequence of a gene can tune its translation. Cell 141:227-229.
    • (2010) Cell , vol.141 , pp. 227-229
    • Fredrick, K.1    Ibba, M.2
  • 31
    • 67649400561 scopus 로고    scopus 로고
    • Common themes in the design and function of bacterial effectors
    • Galán, J. E. 2009. Common themes in the design and function of bacterial effectors. Cell Host Microbe 5:571-579.
    • (2009) Cell Host Microbe , vol.5 , pp. 571-579
    • Galán, J.E.1
  • 32
    • 38849131977 scopus 로고    scopus 로고
    • Energizing type III secretion machines: what is the fuel?
    • Galán, J. E. 2008. Energizing type III secretion machines: what is the fuel? Nat. Struct. Mol. Biol. 15:127-128.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 127-128
    • Galán, J.E.1
  • 33
    • 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
  • 34
    • 22244476683 scopus 로고    scopus 로고
    • Protective anti-V antibodies inhibit Pseudomonas and Yersinia translocon assembly within host membranes
    • Goure, J., P. Broz, O. Attree, G. R. Cornelis, and I. Attree. 2005. Protective anti-V antibodies inhibit Pseudomonas and Yersinia translocon assembly within host membranes. J. Infect. Dis. 192:218-225.
    • (2005) J. Infect. Dis. , vol.192 , pp. 218-225
    • Goure, J.1    Broz, P.2    Attree, O.3    Cornelis, G.R.4    Attree, I.5
  • 35
    • 0037369772 scopus 로고    scopus 로고
    • Structural characterization of the N terminus of IpaC from Shigella flexneri
    • Harrington, A. T., et al. 2003. Structural characterization of the N terminus of IpaC from Shigella flexneri. Infect. Immun. 71:1255-1264.
    • (2003) Infect. Immun. , vol.71 , pp. 1255-1264
    • Harrington, A.T.1
  • 36
    • 0027930194 scopus 로고
    • Essential role of YopD in inhibition of the respiratory burst of macrophages by Yersinia enterocolitica
    • Hartland, E. L., S. P. Green, W. A. Phillips, and R. M. Robins-Browne. 1994. Essential role of YopD in inhibition of the respiratory burst of macrophages by Yersinia enterocolitica. Infect. Immun. 62:4445-4453.
    • (1994) Infect. Immun. , vol.62 , pp. 4445-4453
    • Hartland, E.L.1    Green, S.P.2    Phillips, W.A.3    Robins-Browne, R.M.4
  • 37
    • 77952710839 scopus 로고    scopus 로고
    • Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners
    • Imada, K., T. Minamino, M. Kinoshita, Y. Furukawa, and K. Namba. 2010. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners. Proc. Natl. Acad. Sci. U. S. A. 107:8812-8817.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 8812-8817
    • Imada, K.1    Minamino, T.2    Kinoshita, M.3    Furukawa, Y.4    Namba, K.5
  • 38
    • 33846314672 scopus 로고    scopus 로고
    • Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits
    • Imada, K., T. Minamino, A. Tahara, and K. Namba. 2007. Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits. Proc. Natl. Acad. Sci. U. S. A. 104:485-490.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 485-490
    • Imada, K.1    Minamino, T.2    Tahara, A.3    Namba, K.4
  • 39
    • 0032055051 scopus 로고    scopus 로고
    • TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors
    • Iriarte, M., et al. 1998. TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors. EMBO J. 17:1907-1918.
    • (1998) EMBO J. , vol.17 , pp. 1907-1918
    • Iriarte, M.1
  • 40
    • 0034682740 scopus 로고    scopus 로고
    • Translation/secretion coupling by type III secretion systems
    • Karlinsey, J. E., J. Lonner, K. L. Brown, and K. T. Hughes. 2000. Translation/secretion coupling by type III secretion systems. Cell 102:487-497.
    • (2000) Cell , vol.102 , pp. 487-497
    • Karlinsey, J.E.1    Lonner, J.2    Brown, K.L.3    Hughes, K.T.4
  • 41
    • 34948840439 scopus 로고    scopus 로고
    • Analysis of functional domains present in the N-terminus of the SipB protein
    • Kim, B. H., H. G. Kim, J. S. Kim, J. I. Jang, and Y. K. Park. 2007. Analysis of functional domains present in the N-terminus of the SipB protein. Microbiology 153:2998-3008.
    • (2007) Microbiology , vol.153 , pp. 2998-3008
    • Kim, B.H.1    Kim, H.G.2    Kim, J.S.3    Jang, J.I.4    Park, Y.K.5
  • 42
    • 27144555357 scopus 로고    scopus 로고
    • Regulation of translation via mRNA structure in prokaryotes and eukaryotes
    • Kozak, M. 2005. Regulation of translation via mRNA structure in prokaryotes and eukaryotes. Gene 361:13-37.
    • (2005) Gene , vol.361 , pp. 13-37
    • Kozak, M.1
  • 43
    • 0036719968 scopus 로고    scopus 로고
    • Salmonella type III secretion-associated protein InvE controls translocation of effector proteins into host cells
    • Kubori, T., and J. E. Galán. 2002. Salmonella type III secretion-associated protein InvE controls translocation of effector proteins into host cells. J. Bacteriol. 184:4699-4708.
    • (2002) J. Bacteriol. , vol.184 , pp. 4699-4708
    • Kubori, T.1    Galán, J.E.2
  • 44
    • 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 331:1188-1189.
    • (2011) Science , vol.331 , pp. 1188-1189
    • Lara-Tejero, M.1    Kato, J.2    Wagner, S.3    Liu, X.4    Galan, J.E.5
  • 45
    • 0036334915 scopus 로고    scopus 로고
    • Proteolytic cleavage of the FlhB homologue YscU of Yersinia pseudotuberculosis is essential for bacterial survival but not for type III secretion
    • Lavander, M., et al. 2002. Proteolytic cleavage of the FlhB homologue YscU of Yersinia pseudotuberculosis is essential for bacterial survival but not for type III secretion. J. Bacteriol. 184:4500-4509.
    • (2002) J. Bacteriol. , vol.184 , pp. 4500-4509
    • Lavander, M.1
  • 46
    • 0035423161 scopus 로고    scopus 로고
    • Targeting exported substrates to the Yersinia TTSS: different functions for different signals?
    • Lloyd, S. A., Å. Forsberg, H. Wolf-Watz, and M. S. Francis. 2001. Targeting exported substrates to the Yersinia TTSS: different functions for different signals? Trends Microbiol. 9:367-371.
    • (2001) Trends Microbiol. , vol.9 , pp. 367-371
    • Lloyd, S.A.1    Forsberg, Å.2    Wolf-Watz, H.3    Francis, M.S.4
  • 47
    • 0036197569 scopus 로고    scopus 로고
    • Molecular characterization of type III secretion signals via analysis of synthetic N-terminal amino acid sequences
    • Lloyd, S. A., M. Sjöström, S. Andersson, and H. Wolf-Watz. 2002. Molecular characterization of type III secretion signals via analysis of synthetic N-terminal amino acid sequences. Mol. Microbiol. 43:51-59.
    • (2002) Mol. Microbiol. , vol.43 , pp. 51-59
    • Lloyd, S.A.1    Sjöström, M.2    Andersson, S.3    Wolf-Watz, H.4
  • 48
    • 67650151451 scopus 로고    scopus 로고
    • Prediction of type III secretion signals in genomes of gram-negative bacteria
    • Löwer, M., and G. Schneider. 2009. Prediction of type III secretion signals in genomes of gram-negative bacteria. PLoS One 4:e5917.
    • (2009) PLoS One , vol.4
    • Löwer, M.1    Schneider, G.2
  • 49
    • 78449271872 scopus 로고    scopus 로고
    • The Shigella T3SS needle transmits a signal for MxiC release, which controls secretion of effectors
    • Martinez-Argudo, I., and A. J. Blocker. 2010. The Shigella T3SS needle transmits a signal for MxiC release, which controls secretion of effectors. Mol. Microbiol. 78:1365-1378.
    • (2010) Mol. Microbiol. , vol.78 , pp. 1365-1378
    • Martinez-Argudo, I.1    Blocker, A.J.2
  • 50
    • 70350455913 scopus 로고    scopus 로고
    • Functional characterization of SsaE, a novel chaperone protein of the type III secretion system encoded by Salmonella pathogenicity island 2
    • Miki, T., Y. Shibagaki, H. Danbara, and N. Okada. 2009. Functional characterization of SsaE, a novel chaperone protein of the type III secretion system encoded by Salmonella pathogenicity island 2. J. Bacteriol. 191:6843-6854.
    • (2009) J. Bacteriol. , vol.191 , pp. 6843-6854
    • Miki, T.1    Shibagaki, Y.2    Danbara, H.3    Okada, N.4
  • 51
    • 38849122594 scopus 로고    scopus 로고
    • Real-time analysis of effector translocation by the type III secretion system of enteropathogenic Escherichia coli
    • Mills, E., K. Baruch, X. Charpentier, S. Kobi, and I. Rosenshine. 2008. Real-time analysis of effector translocation by the type III secretion system of enteropathogenic Escherichia coli. Cell Host Microbe 3:104-113.
    • (2008) Cell Host Microbe , vol.3 , pp. 104-113
    • Mills, E.1    Baruch, K.2    Charpentier, X.3    Kobi, S.4    Rosenshine, I.5
  • 52
    • 0029913592 scopus 로고    scopus 로고
    • Flagellin A is essential for the virulence of Vibrio anguillarum
    • Milton, D. L., R. O'Toole, P. Horstedt, and H. Wolf-Watz. 1996. Flagellin A is essential for the virulence of Vibrio anguillarum. J. Bacteriol. 178:1310-1319.
    • (1996) J. Bacteriol. , vol.178 , pp. 1310-1319
    • Milton, D.L.1    O'Toole, R.2    Horstedt, P.3    Wolf-Watz, H.4
  • 53
    • 43449122166 scopus 로고    scopus 로고
    • The type III secretion system tip complex and translocon
    • Mueller, C. A., P. Broz, and G. R. Cornelis. 2008. The type III secretion system tip complex and translocon. Mol. Microbiol. 68:1085-1095.
    • (2008) Mol. Microbiol. , vol.68 , pp. 1085-1095
    • Mueller, C.A.1    Broz, P.2    Cornelis, G.R.3
  • 54
    • 77954362751 scopus 로고    scopus 로고
    • N-terminal type III secretion signal of enteropathogenic Escherichia coli translocator proteins
    • Munera, D., V. F. Crepin, O. Marches, and G. Frankel. 2010. N-terminal type III secretion signal of enteropathogenic Escherichia coli translocator proteins. J. Bacteriol. 192:3534-3539.
    • (2010) J. Bacteriol. , vol.192 , pp. 3534-3539
    • Munera, D.1    Crepin, V.F.2    Marches, O.3    Frankel, G.4
  • 55
    • 0032835828 scopus 로고    scopus 로고
    • Insertion of a Yop translocation pore into the macrophage plasma membrane by Yersinia enterocolitica: requirement for translocators YopB and YopD, but not LcrG
    • Neyt, C., and G. R. Cornelis. 1999. Insertion of a Yop translocation pore into the macrophage plasma membrane by Yersinia enterocolitica: requirement for translocators YopB and YopD, but not LcrG. Mol. Microbiol. 33:971-981.
    • (1999) Mol. Microbiol. , vol.33 , pp. 971-981
    • Neyt, C.1    Cornelis, G.R.2
  • 56
    • 3042661989 scopus 로고    scopus 로고
    • SepL, a protein required for enteropathogenic Escherichia coli type III translocation, interacts with secretion component SepD
    • O'Connell, C. B., et al. 2004. SepL, a protein required for enteropathogenic Escherichia coli type III translocation, interacts with secretion component SepD. Mol. Microbiol. 52:1613-1625.
    • (2004) Mol. Microbiol. , vol.52 , pp. 1613-1625
    • O'Connell, C.B.1
  • 57
    • 3042519348 scopus 로고    scopus 로고
    • The YopD translocator of Yersinia pseudotuberculosis is a multifunctional protein comprised of discrete domains
    • Olsson, J., et al. 2004. The YopD translocator of Yersinia pseudotuberculosis is a multifunctional protein comprised of discrete domains. J. Bacteriol. 186:4110-4123.
    • (2004) J. Bacteriol. , vol.186 , pp. 4110-4123
    • Olsson, J.1
  • 58
    • 15944409588 scopus 로고    scopus 로고
    • Bioinformatics, genomics and evolution of non-flagellar type-III secretion systems: a Darwinian perpective
    • Pallen, M. J., S. A. Beatson, and C. M. Bailey. 2005. Bioinformatics, genomics and evolution of non-flagellar type-III secretion systems: a Darwinian perpective. FEMS Microbiol. Rev. 29:201-229.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 201-229
    • Pallen, M.J.1    Beatson, S.A.2    Bailey, C.M.3
  • 59
    • 11844279779 scopus 로고    scopus 로고
    • A synonymous mutation in Yersinia enterocolitica yopE affects the function of the YopE type III secretion signal
    • Ramamurthi, K. S., and O. Schneewind. 2005. A synonymous mutation in Yersinia enterocolitica yopE affects the function of the YopE type III secretion signal. J. Bacteriol. 187:707-715.
    • (2005) J. Bacteriol. , vol.187 , pp. 707-715
    • Ramamurthi, K.S.1    Schneewind, O.2
  • 60
    • 0344826585 scopus 로고    scopus 로고
    • Yersinia yopQ mRNA encodes a bipartite type III secretion signal in the first 15 codons
    • Ramamurthi, K. S., and O. Schneewind. 2003. Yersinia yopQ mRNA encodes a bipartite type III secretion signal in the first 15 codons. Mol. Microbiol. 50:1189-1198.
    • (2003) Mol. Microbiol. , vol.50 , pp. 1189-1198
    • Ramamurthi, K.S.1    Schneewind, O.2
  • 61
    • 44249119642 scopus 로고    scopus 로고
    • YscU cleavage and the assembly of Yersinia type III secretion machine complexes
    • Riordan, K. E., and O. Schneewind. 2008. YscU cleavage and the assembly of Yersinia type III secretion machine complexes. Mol. Microbiol. 68:1485-1501.
    • (2008) Mol. Microbiol. , vol.68 , pp. 1485-1501
    • Riordan, K.E.1    Schneewind, O.2
  • 62
    • 0025788249 scopus 로고
    • Intracellular targeting of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption
    • Rosqvist, R., Å. Forsberg, and H. Wolf-Watz. 1991. Intracellular targeting of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption. Infect. Immun. 59:4562-4569.
    • (1991) Infect. Immun. , vol.59 , pp. 4562-4569
    • Rosqvist, R.1    Forsberg, Å.2    Wolf-Watz, H.3
  • 63
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist, R., K. E. Magnusson, and H. Wolf-Watz. 1994. Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J. 13:964-972.
    • (1994) EMBO J. , vol.13 , pp. 964-972
    • Rosqvist, R.1    Magnusson, K.E.2    Wolf-Watz, H.3
  • 64
    • 66349123567 scopus 로고    scopus 로고
    • Accurate prediction of secreted substrates and identification of a conserved putative secretion signal for type III secretion systems
    • Samudrala, R., F. Heffron, and J. E. McDermott. 2009. Accurate prediction of secreted substrates and identification of a conserved putative secretion signal for type III secretion systems. PLoS Pathog. 5:e1000375.
    • (2009) PLoS Pathog. , vol.5
    • Samudrala, R.1    Heffron, F.2    McDermott, J.E.3
  • 65
    • 0021027842 scopus 로고
    • A broad host range mobilisation system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilisation system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria. Nat. Biotechnol 1:784-791.
    • (1983) Nat. Biotechnol , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 66
    • 0029031698 scopus 로고
    • Differential effects of deletions in lcrV on secretion of V antigen, regulation of the low-Ca2+ response, and virulence of Yersinia pestis
    • Skrzypek, E., and S. C. Straley. 1995. Differential effects of deletions in lcrV on secretion of V antigen, regulation of the low-Ca2+ response, and virulence of Yersinia pestis. J. Bacteriol. 177:2530-2542.
    • (1995) J. Bacteriol. , vol.177 , pp. 2530-2542
    • Skrzypek, E.1    Straley, S.C.2
  • 67
    • 34250840609 scopus 로고    scopus 로고
    • YscU recognizes translocators as export substrates of the Yersinia injectisome
    • Sorg, I., et al. 2007. YscU recognizes translocators as export substrates of the Yersinia injectisome. EMBO J. 26:3015-3024.
    • (2007) EMBO J. , vol.26 , pp. 3015-3024
    • Sorg, I.1
  • 68
    • 33750809905 scopus 로고    scopus 로고
    • Secretion signal recognition by YscN, the Yersinia type III secretion ATPase
    • Sorg, J. A., B. Blaylock, and O. Schneewind. 2006. Secretion signal recognition by YscN, the Yersinia type III secretion ATPase. Proc. Natl. Acad. Sci. U. S. A. 103:16490-16495.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 16490-16495
    • Sorg, J.A.1    Blaylock, B.2    Schneewind, O.3
  • 69
    • 23844485234 scopus 로고    scopus 로고
    • Substrate recognition of type III secretion machines-testing the RNA signal hypothesis
    • Sorg, J. A., N. C. Miller, and O. Schneewind. 2005. Substrate recognition of type III secretion machines-testing the RNA signal hypothesis. Cell Microbiol. 7:1217-1225.
    • (2005) Cell Microbiol. , vol.7 , pp. 1217-1225
    • Sorg, J.A.1    Miller, N.C.2    Schneewind, O.3
  • 70
    • 35748929649 scopus 로고    scopus 로고
    • Sorting of early and late flagellar subunits after docking at the membrane ATPase of the type III export pathway
    • Stafford, G. P., et al. 2007. Sorting of early and late flagellar subunits after docking at the membrane ATPase of the type III export pathway. J. Mol. Biol. 374:877-882.
    • (2007) J. Mol. Biol. , vol.374 , pp. 877-882
    • Stafford, G.P.1
  • 71
    • 0037347101 scopus 로고    scopus 로고
    • TyeA of Yersinia pseudotuberculosis is involved in regulation of Yop expression and is required for polarized translocation of Yop effectors
    • Sundberg, L., and A. Forsberg. 2003. TyeA of Yersinia pseudotuberculosis is involved in regulation of Yop expression and is required for polarized translocation of Yop effectors. Cell Microbiol. 5:187-202.
    • (2003) Cell Microbiol. , vol.5 , pp. 187-202
    • Sundberg, L.1    Forsberg, A.2
  • 72
    • 0033485823 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion-translocation system: channel formation by secreted Yops
    • Tardy, F., et al. 1999. Yersinia enterocolitica type III secretion-translocation system: channel formation by secreted Yops. EMBO J. 18:6793-6799.
    • (1999) EMBO J. , vol.18 , pp. 6793-6799
    • Tardy, F.1
  • 73
    • 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
  • 74
    • 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
  • 75
    • 79951817476 scopus 로고    scopus 로고
    • The RACK1 signaling scaffold protein selectively interacts with Yersinia pseudotuberculosis virulence function
    • Thorslund, S. E., et al. 2011. The RACK1 signaling scaffold protein selectively interacts with Yersinia pseudotuberculosis virulence function. PLoS One 6:e16784.
    • (2011) PLoS One , vol.6
    • Thorslund, S.E.1
  • 76
    • 26844521751 scopus 로고    scopus 로고
    • Type III secretion: more systems than you think
    • Troisfontaines, P., and G. R. Cornelis. 2005. Type III secretion: more systems than you think. Physiology (Bethesda) 20:326-339.
    • (2005) Physiology (Bethesda) , vol.20 , pp. 326-339
    • Troisfontaines, P.1    Cornelis, G.R.2
  • 77
    • 4544339989 scopus 로고    scopus 로고
    • Contribution of the major secreted Yops of Yersinia enterocolitica O:8 to pathogenicity in the mouse infection model
    • Trülzsch, K., T. Sporleder, E. I. Igwe, H. Rüssmann, and J. Heesemann. 2004. Contribution of the major secreted Yops of Yersinia enterocolitica O:8 to pathogenicity in the mouse infection model. Infect. Immun. 72:5227-5234.
    • (2004) Infect. Immun. , vol.72 , pp. 5227-5234
    • Trülzsch, K.1    Sporleder, T.2    Igwe, E.I.3    Rüssmann, H.4    Heesemann, J.5
  • 78
    • 44949102310 scopus 로고    scopus 로고
    • Quantification of real-time Salmonella effector type III secretion kinetics reveals differential secretion rates for SopE2 and SptP
    • Van Engelenburg, S. B., and A. E. Palmer. 2008. Quantification of real-time Salmonella effector type III secretion kinetics reveals differential secretion rates for SopE2 and SptP. Chem. Biol. 15:619-628.
    • (2008) Chem. Biol. , vol.15 , pp. 619-628
    • Van Engelenburg, S.B.1    Palmer, A.E.2
  • 80
    • 34548561946 scopus 로고    scopus 로고
    • Induction of the Yersinia type 3 secretion system as an all-or-none phenomenon
    • Wiley, D. J., R. Rosqvist, and K. Schesser. 2007. Induction of the Yersinia type 3 secretion system as an all-or-none phenomenon. J. Mol. Biol. 373:27-37.
    • (2007) J. Mol. Biol. , vol.373 , pp. 27-37
    • Wiley, D.J.1    Rosqvist, R.2    Schesser, K.3
  • 81
    • 0031936516 scopus 로고    scopus 로고
    • YopD of Yersinia pestis plays a role in negative regulation of the low-calcium response in addition to its role in translocation of Yops
    • Williams, A. W., and S. C. Straley. 1998. YopD of Yersinia pestis plays a role in negative regulation of the low-calcium response in addition to its role in translocation of Yops. J. Bacteriol. 180:350-358.
    • (1998) J. Bacteriol. , vol.180 , pp. 350-358
    • Williams, A.W.1    Straley, S.C.2
  • 82
    • 48249085360 scopus 로고    scopus 로고
    • Hierarchical effector protein transport by the Salmonella Typhimurium SPI-1 type III secretion system
    • Winnen, B., et al. 2008. Hierarchical effector protein transport by the Salmonella Typhimurium SPI-1 type III secretion system. PLoS One 3:e2178.
    • (2008) PLoS One , vol.3
    • Winnen, B.1
  • 83
    • 0029944323 scopus 로고    scopus 로고
    • The cytosolic SycE and SycH chaperones of Yersinia protect the region of YopE and YopH involved in translocation across eukaryotic cell membranes
    • Woestyn, S., M. P. Sory, A. Boland, O. Lequenne, and G. R. Cornelis. 1996. The cytosolic SycE and SycH chaperones of Yersinia protect the region of YopE and YopH involved in translocation across eukaryotic cell membranes. Mol. Microbiol. 20:1261-1271.
    • (1996) Mol. Microbiol. , vol.20 , pp. 1261-1271
    • Woestyn, S.1    Sory, M.P.2    Boland, A.3    Lequenne, O.4    Cornelis, G.R.5
  • 84
    • 75149124497 scopus 로고    scopus 로고
    • Computational prediction of type III secreted proteins from gram-negative bacteria
    • Yang, Y., J. Zhao, R. L. Morgan, W. Ma, and T. Jiang. 2010. Computational prediction of type III secreted proteins from gram-negative bacteria. BMC Bioinformatics 11(Suppl. 1):S47.
    • (2010) BMC Bioinformatics , vol.11 , Issue.SUPPL. 1
    • Yang, Y.1    Zhao, J.2    Morgan, R.L.3    Ma, W.4    Jiang, T.5
  • 85
    • 7644233076 scopus 로고    scopus 로고
    • SsaM and SpiC interact and regulate secretion of Salmonella pathogenicity island 2 type III secretion system effectors and translocators
    • Yu, X. J., M. Liu, and D. W. Holden. 2004. SsaM and SpiC interact and regulate secretion of Salmonella pathogenicity island 2 type III secretion system effectors and translocators. Mol. Microbiol. 54:604-619.
    • (2004) Mol. Microbiol. , vol.54 , pp. 604-619
    • Yu, X.J.1    Liu, M.2    Holden, D.W.3
  • 87
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker, M. 2003. Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res. 31:3406-3415.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3406-3415
    • Zuker, M.1


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