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Volumn 95, Issue 5, 2015, Pages 875-884

Yersinia enterocolitica type III secretion injectisomes form regularly spaced clusters, which incorporate new machines upon activation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CALCIUM ION; PROTEIN LCRV; PROTEIN YSCD; PROTEIN YSCF; PROTEIN YSCJ; PROTEIN YSCP; PROTEIN YSCQ; UNCLASSIFIED DRUG;

EID: 84924068913     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12908     Document Type: Article
Times cited : (26)

References (62)
  • 1
    • 4744364745 scopus 로고    scopus 로고
    • Type III secretion system effector proteins: double agents in bacterial disease and plant defense
    • Alfano, J.R., and Collmer, A. (2004) Type III secretion system effector proteins: double agents in bacterial disease and plant defense. Annu Rev Phytopathol 42: 385-414.
    • (2004) Annu Rev Phytopathol , vol.42 , pp. 385-414
    • Alfano, J.R.1    Collmer, A.2
  • 2
    • 0028883418 scopus 로고
    • Mutational analysis of the Yersinia enterocolitica virC operon: characterization of yscE, F, G, I, J, K required for Yop secretion and yscH encoding YopR
    • Allaoui, A., Schulte, R., and Cornelis, G.R. (1995) Mutational analysis of the Yersinia enterocolitica virC operon: characterization of yscE, F, G, I, J, K required for Yop secretion and yscH encoding YopR. Mol Microbiol 18: 343-355.
    • (1995) Mol Microbiol , vol.18 , pp. 343-355
    • Allaoui, A.1    Schulte, R.2    Cornelis, G.R.3
  • 3
    • 84876840449 scopus 로고    scopus 로고
    • A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly
    • Bergeron, J.R., Worrall, L.J., Sgourakis, N.G., DiMaio, F., Pfuetzner, R.A., Felise, H.B., etal. (2013) A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly. PLoS Pathog 9: e1003307.
    • (2013) PLoS Pathog , vol.9 , pp. e1003307
    • Bergeron, J.R.1    Worrall, L.J.2    Sgourakis, N.G.3    DiMaio, F.4    Pfuetzner, R.A.5    Felise, H.B.6
  • 4
    • 0037453098 scopus 로고    scopus 로고
    • Type III secretion systems and bacterial flagella: insights into their function from structural similarities
    • Blocker, A., Komoriya, K., and Aizawa, S. (2003) Type III secretion systems and bacterial flagella: insights into their function from structural similarities. Proc Natl Acad Sci USA 100: 3027-3030.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3027-3030
    • Blocker, A.1    Komoriya, K.2    Aizawa, S.3
  • 5
    • 3843152683 scopus 로고    scopus 로고
    • Role of the pilot protein YscW in the biogenesis of the YscC secretin in Yersinia enterocolitica
    • Burghout, P., Beckers, F., de Wit, E., van Boxtel, R., Cornelis, G.R., Tommassen, J., and Koster, M. (2004a) Role of the pilot protein YscW in the biogenesis of the YscC secretin in Yersinia enterocolitica. J Bacteriol 186: 5366-5375.
    • (2004) J Bacteriol , vol.186 , pp. 5366-5375
    • Burghout, P.1    Beckers, F.2    de Wit, E.3    van Boxtel, R.4    Cornelis, G.R.5    Tommassen, J.6    Koster, M.7
  • 6
    • 3042812521 scopus 로고    scopus 로고
    • Structure and electrophysiological properties of the YscC secretin from the type III secretion system of Yersinia enterocolitica
    • Burghout, P., van Boxtel, R., Van Gelder, P., Ringler, P., Muller, S.A., Tommassen, J., and Koster, M. (2004b) Structure and electrophysiological properties of the YscC secretin from the type III secretion system of Yersinia enterocolitica. J Bacteriol 186: 4645-4654.
    • (2004) J Bacteriol , vol.186 , pp. 4645-4654
    • Burghout, P.1    van Boxtel, R.2    Van Gelder, P.3    Ringler, P.4    Muller, S.A.5    Tommassen, J.6    Koster, M.7
  • 7
    • 84862556686 scopus 로고    scopus 로고
    • Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria
    • Buttner, D. (2012) Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria. Microbiol Mol Biol Rev 76: 262-310.
    • (2012) Microbiol Mol Biol Rev , vol.76 , pp. 262-310
    • Buttner, D.1
  • 8
    • 84875852406 scopus 로고    scopus 로고
    • Engineering the type III secretion system in non-replicating bacterial minicells for antigen delivery
    • Carleton, H.A., Lara-Tejero, M., Liu, X., and Galan, J.E. (2013) Engineering the type III secretion system in non-replicating bacterial minicells for antigen delivery. Nat Commun 4: 1590.
    • (2013) Nat Commun , vol.4 , pp. 1590
    • Carleton, H.A.1    Lara-Tejero, M.2    Liu, X.3    Galan, J.E.4
  • 9
    • 84860574289 scopus 로고    scopus 로고
    • Dynamo: a flexible, user-friendly development tool for subtomogram averaging of cryo-EM data in high-performance computing environments
    • Castano-Diez, D., Kudryashev, M., Arheit, M., and Stahlberg, H. (2012) Dynamo: a flexible, user-friendly development tool for subtomogram averaging of cryo-EM data in high-performance computing environments. J Struct Biol 178: 139-151.
    • (2012) J Struct Biol , vol.178 , pp. 139-151
    • Castano-Diez, D.1    Kudryashev, M.2    Arheit, M.3    Stahlberg, H.4
  • 10
  • 11
    • 0038608020 scopus 로고    scopus 로고
    • Helical structure of the needle of the type III secretion system of Shigella flexneri
    • Cordes, F.S., Komoriya, K., Larquet, E., Yang, S., Egelman, E.H., Blocker, A., and Lea, S.M. (2003) Helical structure of the needle of the type III secretion system of Shigella flexneri. J Biol Chem 278: 17103-17107.
    • (2003) J Biol Chem , vol.278 , pp. 17103-17107
    • Cordes, F.S.1    Komoriya, K.2    Larquet, E.3    Yang, S.4    Egelman, E.H.5    Blocker, A.6    Lea, S.M.7
  • 13
    • 33750110911 scopus 로고    scopus 로고
    • The type III secretion injectisome
    • Cornelis, G.R. (2006) The type III secretion injectisome. Nat Rev Microbiol 4: 811-825.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 811-825
    • Cornelis, G.R.1
  • 14
    • 0033764483 scopus 로고    scopus 로고
    • Assembly and function of type III secretory systems
    • Cornelis, G.R., and Van Gijsegem, F. (2000) Assembly and function of type III secretory systems. Annu Rev Microbiol 54: 735-774.
    • (2000) Annu Rev Microbiol , vol.54 , pp. 735-774
    • Cornelis, G.R.1    Van Gijsegem, F.2
  • 15
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells
    • Cornelis, G.R., and Wolf-Watz, H. (1997) The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol Microbiol 23: 861-867.
    • (1997) Mol Microbiol , vol.23 , pp. 861-867
    • Cornelis, G.R.1    Wolf-Watz, H.2
  • 16
    • 79960719451 scopus 로고    scopus 로고
    • Functional domains and motifs of bacterial type III effector proteins and their roles in infection
    • Dean, P. (2011) Functional domains and motifs of bacterial type III effector proteins and their roles in infection. FEMS Microbiol Rev 35: 1100-1125.
    • (2011) FEMS Microbiol Rev , vol.35 , pp. 1100-1125
    • Dean, P.1
  • 17
    • 33747613328 scopus 로고    scopus 로고
    • Molecular model of a type III secretion system needle: implications for host-cell sensing
    • Deane, J.E., Roversi, P., Cordes, F.S., Johnson, S., Kenjale, R., Daniell, S., etal. (2006) Molecular model of a type III secretion system needle: implications for host-cell sensing. Proc Natl Acad Sci USA 103: 12529-12533.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 12529-12533
    • Deane, J.E.1    Roversi, P.2    Cordes, F.S.3    Johnson, S.4    Kenjale, R.5    Daniell, S.6
  • 18
    • 84904040058 scopus 로고    scopus 로고
    • Assembly of the bacterial type III secretion machinery
    • Diepold, A., and Wagner, S. (2014) Assembly of the bacterial type III secretion machinery. FEMS Microbiol Rev 38: 802-822.
    • (2014) FEMS Microbiol Rev , vol.38 , pp. 802-822
    • Diepold, A.1    Wagner, S.2
  • 19
    • 77953123027 scopus 로고    scopus 로고
    • Deciphering the assembly of the Yersinia type III secretion injectisome
    • Diepold, A., Amstutz, M., Abel, S., Sorg, I., Jenal, U., and Cornelis, G.R. (2010) Deciphering the assembly of the Yersinia type III secretion injectisome. EMBO J 29: 1928-1940.
    • (2010) EMBO J , vol.29 , pp. 1928-1940
    • Diepold, A.1    Amstutz, M.2    Abel, S.3    Sorg, I.4    Jenal, U.5    Cornelis, G.R.6
  • 20
    • 80053983313 scopus 로고    scopus 로고
    • The assembly of the export apparatus (YscR,S,T,U,V) of the Yersinia type III secretion apparatus occurs independently of other structural components and involves the formation of an YscV oligomer
    • Diepold, A., Wiesand, U., and Cornelis, G.R. (2011) The assembly of the export apparatus (YscR, S, T, U, V) of the Yersinia type III secretion apparatus occurs independently of other structural components and involves the formation of an YscV oligomer. Mol Microbiol 82: 502-514.
    • (2011) Mol Microbiol , vol.82 , pp. 502-514
    • Diepold, A.1    Wiesand, U.2    Cornelis, G.R.3
  • 21
    • 84922260211 scopus 로고    scopus 로고
    • Composition, Formation, and Regulation of the Cytosolic C-ring, a Dynamic Component of the Type III Secretion Injectisome
    • Diepold, A., Kudryashev, M., Delalez, N.J., Berry, R.M., and Armitage, J.P. (2015) Composition, Formation, and Regulation of the Cytosolic C-ring, a Dynamic Component of the Type III Secretion Injectisome. PLoS biology 13 (1), e1002039-e1002039.
    • (2015) PLoS biology , vol.13 , Issue.1 , pp. e1002039-e1002039
    • Diepold, A.1    Kudryashev, M.2    Delalez, N.J.3    Berry, R.M.4    Armitage, J.P.5
  • 22
    • 79952468635 scopus 로고    scopus 로고
    • Bacterial nanomachines: the flagellum and type III injectisome
    • Erhardt, M., Namba, K., and Hughes, K.T. (2010) Bacterial nanomachines: the flagellum and type III injectisome. Cold Spring Harb Perspect Biol 2: a000299.
    • (2010) Cold Spring Harb Perspect Biol , vol.2 , pp. a000299
    • Erhardt, M.1    Namba, K.2    Hughes, K.T.3
  • 23
    • 23744437504 scopus 로고    scopus 로고
    • Selection and characterization of Yersinia pestis YopN mutants that constitutively block Yop secretion
    • Ferracci, F., Schubot, F.D., Waugh, D.S., and Plano, G.V. (2005) Selection and characterization of Yersinia pestis YopN mutants that constitutively block Yop secretion. Mol Microbiol 57: 970-987.
    • (2005) Mol Microbiol , vol.57 , pp. 970-987
    • Ferracci, F.1    Schubot, F.D.2    Waugh, D.S.3    Plano, G.V.4
  • 24
    • 0023673829 scopus 로고
    • The virulence protein Yop5 of Yersinia pseudotuberculosis is regulated at transcriptional level by plasmid-plB1-encoded trans-acting elements controlled by temperature and calcium
    • Forsberg, A., and Wolf-Watz, H. (1988) The virulence protein Yop5 of Yersinia pseudotuberculosis is regulated at transcriptional level by plasmid-plB1-encoded trans-acting elements controlled by temperature and calcium. Mol Microbiol 2: 121-133.
    • (1988) Mol Microbiol , vol.2 , pp. 121-133
    • Forsberg, A.1    Wolf-Watz, H.2
  • 25
    • 0033591446 scopus 로고    scopus 로고
    • Type III secretion machines: bacterial devices for protein delivery into host cells
    • Galan, J.E., and Collmer, A. (1999) Type III secretion machines: bacterial devices for protein delivery into host cells. Science 284: 1322-1328.
    • (1999) Science , vol.284 , pp. 1322-1328
    • Galan, J.E.1    Collmer, A.2
  • 26
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • Galan, J.E., and Wolf-Watz, H. (2006) Protein delivery into eukaryotic cells by type III secretion machines. Nature 444: 567-573.
    • (2006) Nature , vol.444 , pp. 567-573
    • Galan, J.E.1    Wolf-Watz, H.2
  • 27
    • 33750097480 scopus 로고    scopus 로고
    • Subterfuge and manipulation: type III effector proteins of phytopathogenic bacteria
    • Grant, S.R., Fisher, E.J., Chang, J.H., Mole, B.M., and Dangl, J.L. (2006) Subterfuge and manipulation: type III effector proteins of phytopathogenic bacteria. Annu Rev Microbiol 60: 425-429.
    • (2006) Annu Rev Microbiol , vol.60 , pp. 425-429
    • Grant, S.R.1    Fisher, E.J.2    Chang, J.H.3    Mole, B.M.4    Dangl, J.L.5
  • 28
    • 78149443620 scopus 로고    scopus 로고
    • Bacterial contact-dependent delivery systems
    • Hayes, C.S., Aoki, S.K., and Low, D.A. (2010) Bacterial contact-dependent delivery systems. Annu Rev Genet 44: 71-90.
    • (2010) Annu Rev Genet , vol.44 , pp. 71-90
    • Hayes, C.S.1    Aoki, S.K.2    Low, D.A.3
  • 29
    • 77956909246 scopus 로고    scopus 로고
    • Fluorescence microscopy beyond the diffraction limit
    • Heilemann, M. (2010) Fluorescence microscopy beyond the diffraction limit. J Biotechnol 149: 243-251.
    • (2010) J Biotechnol , vol.149 , pp. 243-251
    • Heilemann, M.1
  • 30
    • 41649116701 scopus 로고    scopus 로고
    • Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure
    • Hoffmann, C., Leis, A., Niederweis, M., Plitzko, J.M., and Engelhardt, H. (2008) Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure. Proc Natl Acad Sci USA 105: 3963-3967.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3963-3967
    • Hoffmann, C.1    Leis, A.2    Niederweis, M.3    Plitzko, J.M.4    Engelhardt, H.5
  • 31
    • 0034669051 scopus 로고    scopus 로고
    • Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins
    • Hoiczyk, E., Roggenkamp, A., Reichenbecher, M., Lupas, A., and Heesemann, J. (2000) Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins. EMBO J 19: 5989-5999.
    • (2000) EMBO J , vol.19 , pp. 5989-5999
    • Hoiczyk, E.1    Roggenkamp, A.2    Reichenbecher, M.3    Lupas, A.4    Heesemann, J.5
  • 32
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • Hueck, C.J. (1998) Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol Mol Biol Rev 62: 379-433.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 33
    • 84889777894 scopus 로고    scopus 로고
    • Common and distinct structural features of Salmonella injectisome and flagellar basal body
    • Kawamoto, A., Morimoto, Y.V., Miyata, T., Minamino, T., Hughes, K.T., Kato, T., and Namba, K. (2013) Common and distinct structural features of Salmonella injectisome and flagellar basal body. Sci Rep 3: 3369.
    • (2013) Sci Rep , vol.3 , pp. 3369
    • Kawamoto, A.1    Morimoto, Y.V.2    Miyata, T.3    Minamino, T.4    Hughes, K.T.5    Kato, T.6    Namba, K.7
  • 34
    • 0344393521 scopus 로고    scopus 로고
    • Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria
    • Koraimann, G. (2003) Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria. Cell Mol Life Sci 60: 2371-2388.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 2371-2388
    • Koraimann, G.1
  • 35
    • 0030716279 scopus 로고    scopus 로고
    • The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex
    • Koster, M., Bitter, W., de Cock, H., Allaoui, A., Cornelis, G.R., and Tommassen, J. (1997) The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex. Mol Microbiol 26: 789-797.
    • (1997) Mol Microbiol , vol.26 , pp. 789-797
    • Koster, M.1    Bitter, W.2    de Cock, H.3    Allaoui, A.4    Cornelis, G.R.5    Tommassen, J.6
  • 36
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer, J.R., Mastronarde, D.N., and McIntosh, J.R. (1996) Computer visualization of three-dimensional image data using IMOD. J Struct Biol 116: 71-76.
    • (1996) J Struct Biol , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 37
    • 0032562678 scopus 로고    scopus 로고
    • Supramolecular structure of the Salmonella typhimurium type III protein secretion system
    • Kubori, T., Matsushima, Y., Nakamura, D., Uralil, J., Lara-Tejero, M., Sukhan, A., etal. (1998) Supramolecular structure of the Salmonella typhimurium type III protein secretion system. Science 280: 602-605.
    • (1998) Science , vol.280 , pp. 602-605
    • Kubori, T.1    Matsushima, Y.2    Nakamura, D.3    Uralil, J.4    Lara-Tejero, M.5    Sukhan, A.6
  • 38
    • 0034730179 scopus 로고    scopus 로고
    • Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system
    • Kubori, T., Sukhan, A., Aizawa, S.I., and Galan, J.E. (2000) Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system. Proc Natl Acad Sci USA 97: 10225-10230.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10225-10230
    • Kubori, T.1    Sukhan, A.2    Aizawa, S.I.3    Galan, J.E.4
  • 39
    • 84860590097 scopus 로고    scopus 로고
    • Assessing the benefits of focal pair cryo-electron tomography
    • Kudryashev, M., Stahlberg, H., and Castano-Diez, D. (2012) Assessing the benefits of focal pair cryo-electron tomography. J Struct Biol 178: 88-97.
    • (2012) J Struct Biol , vol.178 , pp. 88-97
    • Kudryashev, M.1    Stahlberg, H.2    Castano-Diez, D.3
  • 41
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: from cells to molecules
    • Lucic, V., Forster, F., and Baumeister, W. (2005) Structural studies by electron tomography: from cells to molecules. Annu Rev Biochem 74: 833-865.
    • (2005) Annu Rev Biochem , vol.74 , pp. 833-865
    • Lucic, V.1    Forster, F.2    Baumeister, W.3
  • 42
    • 8844249277 scopus 로고    scopus 로고
    • Type III flagellar protein export and flagellar assembly
    • Macnab, R.M. (2004) Type III flagellar protein export and flagellar assembly. Biochim Biophys Acta 1694: 207-217.
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 207-217
    • Macnab, R.M.1
  • 44
    • 84879425130 scopus 로고    scopus 로고
    • Yersinia infection tools - characterization of structure and function of adhesins
    • Mikula, K.M., Kolodziejczyk, R., and Goldman, A. (2012) Yersinia infection tools - characterization of structure and function of adhesins. Front Cell Infect Microbiol 2: 169.
    • (2012) Front Cell Infect Microbiol , vol.2 , pp. 169
    • Mikula, K.M.1    Kolodziejczyk, R.2    Goldman, A.3
  • 45
    • 38549158887 scopus 로고    scopus 로고
    • Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export
    • Minamino, T., and Namba, K. (2008) Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export. Nature 451: 485-488.
    • (2008) Nature , vol.451 , pp. 485-488
    • Minamino, T.1    Namba, K.2
  • 46
    • 84855824363 scopus 로고    scopus 로고
    • Translocators YopB and YopD from Yersinia enterocolitica form a multimeric integral membrane complex in eukaryotic cell membranes
    • Montagner, C., Arquint, C., and Cornelis, G.R. (2011) Translocators YopB and YopD from Yersinia enterocolitica form a multimeric integral membrane complex in eukaryotic cell membranes. J Bacteriol 193: 6923-6928.
    • (2011) J Bacteriol , vol.193 , pp. 6923-6928
    • Montagner, C.1    Arquint, C.2    Cornelis, G.R.3
  • 47
    • 21344453525 scopus 로고    scopus 로고
    • The bacterial injection kit: type III secretion systems
    • Mota, L.J., and Cornelis, G.R. (2005) The bacterial injection kit: type III secretion systems. Ann Med 37: 234-249.
    • (2005) Ann Med , vol.37 , pp. 234-249
    • Mota, L.J.1    Cornelis, G.R.2
  • 49
    • 27344457144 scopus 로고    scopus 로고
    • The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles
    • Mueller, C.A., Broz, P., Muller, S.A., Ringler, P., Erne-Brand, F., Sorg, I., etal. (2005) The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles. Science 310: 674-676.
    • (2005) Science , vol.310 , pp. 674-676
    • Mueller, C.A.1    Broz, P.2    Muller, S.A.3    Ringler, P.4    Erne-Brand, F.5    Sorg, I.6
  • 50
    • 39849105856 scopus 로고    scopus 로고
    • Novel ultrastructures of Treponema primitia and their implications for motility
    • Murphy, G.E., Matson, E.G., Leadbetter, J.R., Berg, H.C., and Jensen, G.J. (2008) Novel ultrastructures of Treponema primitia and their implications for motility. Mol Microbiol 67: 1184-1195.
    • (2008) Mol Microbiol , vol.67 , pp. 1184-1195
    • Murphy, G.E.1    Matson, E.G.2    Leadbetter, J.R.3    Berg, H.C.4    Jensen, G.J.5
  • 51
    • 84908060953 scopus 로고    scopus 로고
    • Pathogen-host reorganization during Chlamydia invasion revealed by cryo-electron tomography
    • Nans, A., Saibil, H.R., and Hayward, R.D. (2014) Pathogen-host reorganization during Chlamydia invasion revealed by cryo-electron tomography. Cell Microbiol 16: 1457-1472.
    • (2014) Cell Microbiol , vol.16 , pp. 1457-1472
    • Nans, A.1    Saibil, H.R.2    Hayward, R.D.3
  • 52
    • 33645519210 scopus 로고    scopus 로고
    • Evolutionary links between FliH/YscL-like proteins from bacterial type III secretion systems and second-stalk components of the FoF1 and vacuolar ATPases
    • Pallen, M.J., Bailey, C.M., and Beatson, S.A. (2006) Evolutionary links between FliH/YscL-like proteins from bacterial type III secretion systems and second-stalk components of the FoF1 and vacuolar ATPases. Protein Sci 15: 935-941.
    • (2006) Protein Sci , vol.15 , pp. 935-941
    • Pallen, M.J.1    Bailey, C.M.2    Beatson, S.A.3
  • 53
    • 84892990958 scopus 로고    scopus 로고
    • Architecture and host interface of environmental chlamydiae revealed by electron cryotomography
    • Pilhofer, M., Aistleitner, K., Ladinsky, M.S., Konig, L., Horn, M., and Jensen, G.J. (2014) Architecture and host interface of environmental chlamydiae revealed by electron cryotomography. Environ Microbiol 16: 417-429.
    • (2014) Environ Microbiol , vol.16 , pp. 417-429
    • Pilhofer, M.1    Aistleitner, K.2    Ladinsky, M.S.3    Konig, L.4    Horn, M.5    Jensen, G.J.6
  • 54
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist, R., Magnusson, K.E., and Wolf-Watz, H. (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
  • 56
    • 79952262440 scopus 로고    scopus 로고
    • Three-dimensional model of Salmonella's needle complex at subnanometer resolution
    • Schraidt, O., and Marlovits, T.C. (2011) Three-dimensional model of Salmonella's needle complex at subnanometer resolution. Science 331: 1192-1195.
    • (2011) Science , vol.331 , pp. 1192-1195
    • Schraidt, O.1    Marlovits, T.C.2
  • 57
    • 0028105015 scopus 로고
    • Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells
    • Sory, M.P., and Cornelis, G.R. (1994) Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells. Mol Microbiol 14: 583-594.
    • (1994) Mol Microbiol , vol.14 , pp. 583-594
    • Sory, M.P.1    Cornelis, G.R.2
  • 58
    • 0029608720 scopus 로고
    • Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach
    • Sory, M.P., Boland, A., Lambermont, I., and Cornelis, G.R. (1995) Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach. Proc Natl Acad Sci U S A 92: 11998-12002.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 11998-12002
    • Sory, M.P.1    Boland, A.2    Lambermont, I.3    Cornelis, G.R.4
  • 59
    • 0030698085 scopus 로고    scopus 로고
    • YscM1 and YscM2, two Yersinia enterocolitica proteins causing downregulation of yop transcription
    • Stainier, I., Iriarte, M., and Cornelis, G.R. (1997) YscM1 and YscM2, two Yersinia enterocolitica proteins causing downregulation of yop transcription. Mol Microbiol 26: 833-843.
    • (1997) Mol Microbiol , vol.26 , pp. 833-843
    • Stainier, I.1    Iriarte, M.2    Cornelis, G.R.3
  • 60
    • 33947249049 scopus 로고    scopus 로고
    • The type III secretion system needle tip complex mediates host cell sensing and translocon insertion
    • Veenendaal, A.K., Hodgkinson, J.L., Schwarzer, L., Stabat, D., Zenk, S.F., and Blocker, A.J. (2007) The type III secretion system needle tip complex mediates host cell sensing and translocon insertion. Mol Microbiol 63: 1719-1730.
    • (2007) Mol Microbiol , vol.63 , pp. 1719-1730
    • Veenendaal, A.K.1    Hodgkinson, J.L.2    Schwarzer, L.3    Stabat, D.4    Zenk, S.F.5    Blocker, A.J.6
  • 61
    • 0031746607 scopus 로고    scopus 로고
    • Symbiotic implications of type III protein secretion machinery in Rhizobium
    • Viprey, V., Del Greco, A., Golinowski, W., Broughton, W.J., and Perret, X. (1998) Symbiotic implications of type III protein secretion machinery in Rhizobium. Mol Microbiol 28: 1381-1389.
    • (1998) Mol Microbiol , vol.28 , pp. 1381-1389
    • Viprey, V.1    Del Greco, A.2    Golinowski, W.3    Broughton, W.J.4    Perret, X.5
  • 62
    • 0022270769 scopus 로고
    • Isolation and characterization of Ca2+-blind mutants of Yersinia pestis
    • Yother, J., and Goguen, J.D. (1985) Isolation and characterization of Ca2+-blind mutants of Yersinia pestis. J Bacteriol 164: 704-711.
    • (1985) J Bacteriol , vol.164 , pp. 704-711
    • Yother, J.1    Goguen, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.