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Volumn 85, Issue 5, 2012, Pages 878-892

Assembly of the Yersinia injectisome: The missing pieces

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CHAPERONE; SECRETIN; UNCLASSIFIED DRUG; YSCC PROTEIN; YSCF PROTEIN; YSCI PROTEIN; YSCL PROTEIN; YSCN PROTEIN; YSCO PROTEIN; YSCP PROTEIN; YSCV PROTEIN; YSCX PROTEIN; YSCY PROTEIN;

EID: 84865561778     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2012.08146.x     Document Type: Article
Times cited : (53)

References (95)
  • 1
    • 16244407371 scopus 로고    scopus 로고
    • Characterization of a Type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica
    • Agrain, C., Callebaut, I., Journet, L., Sorg, I., Paroz, C., Mota, L.J., etal. (2005a) Characterization of a Type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica. Mol Microbiol 56: 54-67.
    • (2005) Mol Microbiol , vol.56 , pp. 54-67
    • Agrain, C.1    Callebaut, I.2    Journet, L.3    Sorg, I.4    Paroz, C.5    Mota, L.J.6
  • 2
    • 23844543359 scopus 로고    scopus 로고
    • Secretion of YscP from Yersinia enterocolitica is essential to control the length of the injectisome needle but not to change the type III secretion substrate specificity
    • Agrain, C., Sorg, I., Paroz, C., and Cornelis, G.R. (2005b) Secretion of YscP from Yersinia enterocolitica is essential to control the length of the injectisome needle but not to change the type III secretion substrate specificity. Mol Microbiol 57: 1415-1427.
    • (2005) Mol Microbiol , vol.57 , pp. 1415-1427
    • Agrain, C.1    Sorg, I.2    Paroz, C.3    Cornelis, G.R.4
  • 3
    • 0028124264 scopus 로고
    • YscU, a Yersinia enterocolitica inner membrane protein involved in Yop secretion
    • Allaoui, A., Woestyn, S., Sluiters, C., and Cornelis, G.R. (1994) YscU, a Yersinia enterocolitica inner membrane protein involved in Yop secretion. J Bacteriol 176: 4534-4542.
    • (1994) J Bacteriol , vol.176 , pp. 4534-4542
    • Allaoui, A.1    Woestyn, S.2    Sluiters, C.3    Cornelis, G.R.4
  • 4
    • 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
  • 5
    • 77954920256 scopus 로고    scopus 로고
    • FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion system
    • Bange, G., Kummerer, N., Engel, C., Bozkurt, G., Wild, K., and Sinning, I. (2010) FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion system. Proc Natl Acad Sci USA 107: 11295-11300.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 11295-11300
    • Bange, G.1    Kummerer, N.2    Engel, C.3    Bozkurt, G.4    Wild, K.5    Sinning, I.6
  • 6
    • 0034194180 scopus 로고    scopus 로고
    • From flagellum assembly to virulence: the extended family of type III export chaperones
    • Bennett, J.C., and Hughes, C. (2000) From flagellum assembly to virulence: the extended family of type III export chaperones. Trends Microbiol 8: 202-204.
    • (2000) Trends Microbiol , vol.8 , pp. 202-204
    • Bennett, J.C.1    Hughes, C.2
  • 7
    • 0033230438 scopus 로고    scopus 로고
    • The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes
    • Blocker, A., Gounon, P., Larquet, E., Niebuhr, K., Cabiaux, V., Parsot, C., etal. (1999) The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes. J Cell Biol 147: 683-693.
    • (1999) J Cell Biol , vol.147 , pp. 683-693
    • Blocker, A.1    Gounon, P.2    Larquet, E.3    Niebuhr, K.4    Cabiaux, V.5    Parsot, C.6
  • 8
    • 0029814613 scopus 로고    scopus 로고
    • Status of YopM and YopN in the Yersinia Yop virulon: YopM of Y.enterocolitica is internalized inside the cytosol of PU5-1.8 macrophages by the YopB, D, N delivery apparatus
    • Boland, A., Sory, M., Iriarte, M., Kerbourch, C., Wattiau, P., and Cornelis, G.R. (1996) Status of YopM and YopN in the Yersinia Yop virulon: YopM of Y.enterocolitica is internalized inside the cytosol of PU5-1.8 macrophages by the YopB, D, N delivery apparatus. EMBO J 15: 5191-5201.
    • (1996) EMBO J , vol.15 , pp. 5191-5201
    • Boland, A.1    Sory, M.2    Iriarte, M.3    Kerbourch, C.4    Wattiau, P.5    Cornelis, G.R.6
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0016700103 scopus 로고
    • Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and phi80 transducing phages
    • Brickman, E., and Beckwith, J. (1975) Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and phi80 transducing phages. J Mol Biol 96: 307-316.
    • (1975) J Mol Biol , vol.96 , pp. 307-316
    • Brickman, E.1    Beckwith, J.2
  • 12
    • 27744513349 scopus 로고    scopus 로고
    • Mapping of a YscY binding domain within the LcrH chaperone that is required for regulation of Yersinia type III secretion
    • Broms, J.E., Edqvist, P.J., Carlsson, K.E., Forsberg, A., and Francis, M.S. (2005) Mapping of a YscY binding domain within the LcrH chaperone that is required for regulation of Yersinia type III secretion. J Bacteriol 187: 7738-7752.
    • (2005) J Bacteriol , vol.187 , pp. 7738-7752
    • Broms, J.E.1    Edqvist, P.J.2    Carlsson, K.E.3    Forsberg, A.4    Francis, M.S.5
  • 14
    • 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., etal. (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
  • 15
    • 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., etal. (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
  • 16
    • 0036837752 scopus 로고    scopus 로고
    • Evidence for a type III secretion system in Aeromonas salmonicida subsp. salmonicida
    • Burr, S.E., Stuber, K., Wahli, T., and Frey, J. (2002) Evidence for a type III secretion system in Aeromonas salmonicida subsp. salmonicida. J Bacteriol 184: 5966-5970.
    • (2002) J Bacteriol , vol.184 , pp. 5966-5970
    • Burr, S.E.1    Stuber, K.2    Wahli, T.3    Frey, J.4
  • 18
    • 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
  • 19
    • 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
  • 20
    • 0034065897 scopus 로고    scopus 로고
    • The Yersinia pestis YscY protein directly binds YscX, a secreted component of the type III secretion machinery
    • Day, J.B., and Plano, G.V. (2000) The Yersinia pestis YscY protein directly binds YscX, a secreted component of the type III secretion machinery. J Bacteriol 182: 1834-1843.
    • (2000) J Bacteriol , vol.182 , pp. 1834-1843
    • Day, J.B.1    Plano, G.V.2
  • 21
    • 0033793669 scopus 로고    scopus 로고
    • Yersinia pestis YscG protein is a Syc-like chaperone that directly binds yscE
    • Day, J.B., Guller, I., and Plano, G.V. (2000) Yersinia pestis YscG protein is a Syc-like chaperone that directly binds yscE. Infect Immun 68: 6466-6471.
    • (2000) Infect Immun , vol.68 , pp. 6466-6471
    • Day, J.B.1    Guller, I.2    Plano, G.V.3
  • 22
    • 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
  • 23
    • 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
  • 24
    • 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
  • 25
    • 62549099973 scopus 로고    scopus 로고
    • Selective binding of virulence type III export chaperones by FliJ escort orthologues InvI and YscO
    • Evans, L.D., and Hughes, C. (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
  • 26
    • 33751208041 scopus 로고    scopus 로고
    • An escort mechanism for cycling of export chaperones during flagellum assembly
    • Evans, L.D., Stafford, G., Ahmed, S., Fraser, G.M., and Hughes, C. (2006) An escort mechanism for cycling of export chaperones during flagellum assembly. Proc Natl Acad Sci USA 103: 17474-17479.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17474-17479
    • Evans, L.D.1    Stafford, G.2    Ahmed, S.3    Fraser, G.M.4    Hughes, C.5
  • 27
    • 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
  • 28
    • 0028178610 scopus 로고
    • 2+ response (LCR) secretion (ysc) locus lies within the lcrB region of the LCR plasmid in Yersinia pestis
    • 2+ response (LCR) secretion (ysc) locus lies within the lcrB region of the LCR plasmid in Yersinia pestis. J Bacteriol 176: 569-579.
    • (1994) J Bacteriol , vol.176 , pp. 569-579
    • Fields, K.A.1    Plano, G.V.2    Straley, S.C.3
  • 29
    • 0025762461 scopus 로고
    • The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculosis
    • Forsberg, A., Viitanen, A.M., Skurnik, M., and Wolf-Watz, H. (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, A.1    Viitanen, A.M.2    Skurnik, M.3    Wolf-Watz, H.4
  • 30
    • 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., Lloyd, S.A., and Wolf-Watz, H. (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
  • 31
    • 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
  • 32
    • 79952359941 scopus 로고    scopus 로고
    • Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases
    • Ibuki, T., Imada, K., Minamino, T., Kato, T., Miyata, T., and Namba, K. (2011) Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases. Nat Struct Mol Biol 18: 277-282.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 277-282
    • Ibuki, T.1    Imada, K.2    Minamino, T.3    Kato, T.4    Miyata, T.5    Namba, K.6
  • 33
    • 33846314672 scopus 로고    scopus 로고
    • Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits
    • Imada, K., Minamino, T., Tahara, A., and Namba, K. (2007) Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits. Proc Natl Acad Sci USA 104: 485-490.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 485-490
    • Imada, K.1    Minamino, T.2    Tahara, A.3    Namba, K.4
  • 34
    • 0032929404 scopus 로고    scopus 로고
    • Identification of SycN, YscX, and YscY, three new elements of the Yersinia yop virulon
    • Iriarte, M., and Cornelis, G.R. (1999) Identification of SycN, YscX, and YscY, three new elements of the Yersinia yop virulon. J Bacteriol 181: 675-680.
    • (1999) J Bacteriol , vol.181 , pp. 675-680
    • Iriarte, M.1    Cornelis, G.R.2
  • 35
    • 77954407664 scopus 로고    scopus 로고
    • Structural basis of chaperone recognition of type III secretion system minor translocator proteins
    • Job, V., Mattei, P.J., Lemaire, D., Attree, I., and Dessen, A. (2010) Structural basis of chaperone recognition of type III secretion system minor translocator proteins. J Biol Chem 285: 23224-23232.
    • (2010) J Biol Chem , vol.285 , pp. 23224-23232
    • Job, V.1    Mattei, P.J.2    Lemaire, D.3    Attree, I.4    Dessen, A.5
  • 36
    • 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., Delor, I., and Cornelis, G.R. (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
  • 37
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A., Nesvizhskii, A.I., Kolker, E., and Aebersold, R. (2002) Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 74: 5383-5392.
    • (2002) Anal Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 38
    • 0034718542 scopus 로고    scopus 로고
    • Contribution of Salmonella typhimurium type III secretion components to needle complex formation
    • Kimbrough, T.G., and Miller, S.I. (2000) Contribution of Salmonella typhimurium type III secretion components to needle complex formation. Proc Natl Acad Sci USA 97: 11008-11013.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11008-11013
    • Kimbrough, T.G.1    Miller, S.I.2
  • 39
    • 0036165971 scopus 로고    scopus 로고
    • Assembly of the type III secretion needle complex of Salmonella typhimurium
    • Kimbrough, T.G., and Miller, S.I. (2002) Assembly of the type III secretion needle complex of Salmonella typhimurium. Microbes Infect 4: 75-82.
    • (2002) Microbes Infect , vol.4 , pp. 75-82
    • Kimbrough, T.G.1    Miller, S.I.2
  • 40
    • 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
  • 41
    • 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
  • 42
    • 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
  • 43
    • 79952280754 scopus 로고    scopus 로고
    • A sorting platform determines the order of protein secretion in bacterial type III systems
    • Lara-Tejero, M., Kato, J., Wagner, S., Liu, X., and Galan, J.E. (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
  • 44
    • 0016219080 scopus 로고
    • Chemomechanical coupling without ATP: the source of energy for motility and chemotaxis in bacteria
    • Larsen, S.H., Adler, J., Gargus, J.J., and Hogg, R.W. (1974) Chemomechanical coupling without ATP: the source of energy for motility and chemotaxis in bacteria. Proc Natl Acad Sci USA 71: 1239-1243.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 1239-1243
    • Larsen, S.H.1    Adler, J.2    Gargus, J.J.3    Hogg, R.W.4
  • 45
    • 79955733488 scopus 로고    scopus 로고
    • Assembly and stability of flagellar motor in Escherichia coli
    • Li, H., and Sourjik, V. (2011) Assembly and stability of flagellar motor in Escherichia coli. Mol Microbiol 80: 886-899.
    • (2011) Mol Microbiol , vol.80 , pp. 886-899
    • Li, H.1    Sourjik, V.2
  • 46
    • 77953161216 scopus 로고    scopus 로고
    • A conserved domain in type III secretion links the cytoplasmic domain of InvA to elements of the basal body
    • Lilic, M., Quezada, C.M., and Stebbins, C.E. (2010) A conserved domain in type III secretion links the cytoplasmic domain of InvA to elements of the basal body. Acta Crystallogr D Biol Crystallogr 66: 709-713.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 709-713
    • Lilic, M.1    Quezada, C.M.2    Stebbins, C.E.3
  • 47
    • 67649861394 scopus 로고    scopus 로고
    • IpaB-IpgC interaction defines binding motif for type III secretion translocator
    • Lunelli, M., Lokareddy, R.K., Zychlinsky, A., and Kolbe, M. (2009) IpaB-IpgC interaction defines binding motif for type III secretion translocator. Proc Natl Acad Sci USA 106: 9661-9666.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9661-9666
    • Lunelli, M.1    Lokareddy, R.K.2    Zychlinsky, A.3    Kolbe, M.4
  • 48
    • 0037333881 scopus 로고    scopus 로고
    • Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V.cholerae
    • Makino, K., Oshima, K., Kurokawa, K., Yokoyama, K., Uda, T., Tagomori, K., etal. (2003) Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V.cholerae. Lancet 361: 743-749.
    • (2003) Lancet , vol.361 , pp. 743-749
    • Makino, K.1    Oshima, K.2    Kurokawa, K.3    Yokoyama, K.4    Uda, T.5    Tagomori, K.6
  • 49
    • 80051555789 scopus 로고    scopus 로고
    • The genome and surface proteome of Capnocytophaga canimorsus reveal a key role of glycan foraging systems in host glycoproteins deglycosylation
    • Manfredi, P., Renzi, F., Mally, M., Sauteur, L., Schmaler, M., Moes, S., etal. (2011) The genome and surface proteome of Capnocytophaga canimorsus reveal a key role of glycan foraging systems in host glycoproteins deglycosylation. Mol Microbiol 81: 1050-1060.
    • (2011) Mol Microbiol , vol.81 , pp. 1050-1060
    • Manfredi, P.1    Renzi, F.2    Mally, M.3    Sauteur, L.4    Schmaler, M.5    Moes, S.6
  • 50
    • 37049184497 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil, C., and Beckwith, J. (1986) A genetic approach to analyzing membrane protein topology. Science 233: 1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 51
    • 8344258355 scopus 로고    scopus 로고
    • Structural insights into the assembly of the type III secretion needle complex
    • Marlovits, T.C., Kubori, T., Sukhan, A., Thomas, D.R., Galan, J.E., and Unger, V.M. (2004) Structural insights into the assembly of the type III secretion needle complex. Science 306: 1040-1042.
    • (2004) Science , vol.306 , pp. 1040-1042
    • Marlovits, T.C.1    Kubori, T.2    Sukhan, A.3    Thomas, D.R.4    Galan, J.E.5    Unger, V.M.6
  • 52
    • 0020582636 scopus 로고
    • In vitro construction and characterization of phoA-lacZ gene fusions in Escherichia coli
    • Michaelis, S., Guarente, L., and Beckwith, J. (1983) In vitro construction and characterization of phoA-lacZ gene fusions in Escherichia coli. J Bacteriol 154: 356-365.
    • (1983) J Bacteriol , vol.154 , pp. 356-365
    • Michaelis, S.1    Guarente, L.2    Beckwith, J.3
  • 53
    • 0033158524 scopus 로고    scopus 로고
    • Substrate specificity switching of the flagellum-specific export apparatus during flagellar morphogenesis in Salmonella typhimurium
    • Minamino, T., Doi, H., and Kutsukake, K. (1999) Substrate specificity switching of the flagellum-specific export apparatus during flagellar morphogenesis in Salmonella typhimurium. Biosci Biotechnol Biochem 63: 1301-1303.
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 1301-1303
    • Minamino, T.1    Doi, H.2    Kutsukake, K.3
  • 54
    • 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
  • 55
    • 77954239967 scopus 로고    scopus 로고
    • Structure of the cytoplasmic domain of the flagellar secretion apparatus component FlhA from Helicobacter pylori
    • Moore, S.A., and Jia, Y. (2010) Structure of the cytoplasmic domain of the flagellar secretion apparatus component FlhA from Helicobacter pylori. J Biol Chem 285: 21060-21069.
    • (2010) J Biol Chem , vol.285 , pp. 21060-21069
    • Moore, S.A.1    Jia, Y.2
  • 56
    • 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
  • 58
    • 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
  • 59
    • 33745219453 scopus 로고    scopus 로고
    • Double hexameric ring assembly of the type III protein translocase ATPase HrcN
    • Muller, S.A., Pozidis, C., Stone, R., Meesters, C., Chami, M., Engel, A., etal. (2006) Double hexameric ring assembly of the type III protein translocase ATPase HrcN. Mol Microbiol 61: 119-125.
    • (2006) Mol Microbiol , vol.61 , pp. 119-125
    • Muller, S.A.1    Pozidis, C.2    Stone, R.3    Meesters, C.4    Chami, M.5    Engel, A.6
  • 60
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii, A.I., Keller, A., Kolker, E., and Aebersold, R. (2003) A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 75: 4646-4658.
    • (2003) Anal Chem , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 61
    • 33645985137 scopus 로고    scopus 로고
    • Assembly of the type III secretion apparatus of enteropathogenic Escherichia coli
    • Ogino, T., Ohno, R., Sekiya, K., Kuwae, A., Matsuzawa, T., Nonaka, T., etal. (2006) Assembly of the type III secretion apparatus of enteropathogenic Escherichia coli. J Bacteriol 188: 2801-2811.
    • (2006) J Bacteriol , vol.188 , pp. 2801-2811
    • Ogino, T.1    Ohno, R.2    Sekiya, K.3    Kuwae, A.4    Matsuzawa, T.5    Nonaka, T.6
  • 62
    • 0036032109 scopus 로고    scopus 로고
    • Chaperones of the type III secretion pathway: jacks of all trades
    • Page, A.L., and Parsot, C. (2002) Chaperones of the type III secretion pathway: jacks of all trades. Mol Microbiol 46: 1-11.
    • (2002) Mol Microbiol , vol.46 , pp. 1-11
    • Page, A.L.1    Parsot, C.2
  • 63
    • 0038546513 scopus 로고    scopus 로고
    • Tetratricopeptide-like repeats in type-III-secretion chaperones and regulators
    • Pallen, M.J., Francis, M.S., and Futterer, K. (2003) Tetratricopeptide-like repeats in type-III-secretion chaperones and regulators. FEMS Microbiol Lett 223: 53-60.
    • (2003) FEMS Microbiol Lett , vol.223 , pp. 53-60
    • Pallen, M.J.1    Francis, M.S.2    Futterer, K.3
  • 64
    • 0031830239 scopus 로고    scopus 로고
    • YscO of Yersinia pestis is a mobile core component of the Yop secretion system
    • Payne, P.L., and Straley, S.C. (1998) YscO of Yersinia pestis is a mobile core component of the Yop secretion system. J Bacteriol 180: 3882-3890.
    • (1998) J Bacteriol , vol.180 , pp. 3882-3890
    • Payne, P.L.1    Straley, S.C.2
  • 66
    • 0025840282 scopus 로고
    • LcrD, a membrane-bound regulator of the Yersinia pestis low-calcium response
    • Plano, G.V., Barve, S.S., and Straley, S.C. (1991) LcrD, a membrane-bound regulator of the Yersinia pestis low-calcium response. J Bacteriol 173: 7293-7303.
    • (1991) J Bacteriol , vol.173 , pp. 7293-7303
    • Plano, G.V.1    Barve, S.S.2    Straley, S.C.3
  • 67
    • 77954394940 scopus 로고    scopus 로고
    • Cochaperone interactions in export of the type III needle component PscF of Pseudomonas aeruginosa
    • Ple, S., Job, V., Dessen, A., and Attree, I. (2010) Cochaperone interactions in export of the type III needle component PscF of Pseudomonas aeruginosa. J Bacteriol 192: 3801-3808.
    • (2010) J Bacteriol , vol.192 , pp. 3801-3808
    • Ple, S.1    Job, V.2    Dessen, A.3    Attree, I.4
  • 68
    • 0038507200 scopus 로고    scopus 로고
    • Type III protein translocase: HrcN is a peripheral ATPase that is activated by oligomerization
    • Pozidis, C., Chalkiadaki, A., Gomez-Serrano, A., Stahlberg, H., Brown, I., Tampakaki, A., etal. (2003) Type III protein translocase: HrcN is a peripheral ATPase that is activated by oligomerization. J Biol Chem 278: 25816-25824.
    • (2003) J Biol Chem , vol.278 , pp. 25816-25824
    • Pozidis, C.1    Chalkiadaki, A.2    Gomez-Serrano, A.3    Stahlberg, H.4    Brown, I.5    Tampakaki, A.6
  • 69
    • 27744509836 scopus 로고    scopus 로고
    • The PscE-PscF-PscG complex controls type III secretion needle biogenesis in Pseudomonas aeruginosa
    • Quinaud, M., Chabert, J., Faudry, E., Neumann, E., Lemaire, D., Pastor, A., etal. (2005) The PscE-PscF-PscG complex controls type III secretion needle biogenesis in Pseudomonas aeruginosa. J Biol Chem 280: 36293-36300.
    • (2005) J Biol Chem , vol.280 , pp. 36293-36300
    • Quinaud, M.1    Chabert, J.2    Faudry, E.3    Neumann, E.4    Lemaire, D.5    Pastor, A.6
  • 70
    • 34249942920 scopus 로고    scopus 로고
    • Structure of the heterotrimeric complex that regulates type III secretion needle formation
    • Quinaud, M., Ple, S., Job, V., Contreras-Martel, C., Simorre, J., Attree, I., etal. (2007) Structure of the heterotrimeric complex that regulates type III secretion needle formation. Proc Natl Acad Sci USA 104: 7803-7808.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7803-7808
    • Quinaud, M.1    Ple, S.2    Job, V.3    Contreras-Martel, C.4    Simorre, J.5    Attree, I.6
  • 71
    • 84856247471 scopus 로고    scopus 로고
    • EscI: a crucial component of the type III secretion system forms the inner rod structure in enteropathogenic Escherichia coli
    • Sal-Man, N., Deng, W., and Finlay, B.B. (2012) EscI: a crucial component of the type III secretion system forms the inner rod structure in enteropathogenic Escherichia coli. Biochem J 442: 119-125.
    • (2012) Biochem J , vol.442 , pp. 119-125
    • Sal-Man, N.1    Deng, W.2    Finlay, B.B.3
  • 72
    • 0024465189 scopus 로고
    • Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase
    • San Millan, J.L., Boyd, D., Dalbey, R., Wickner, W., and Beckwith, J. (1989) Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase. J Bacteriol 171: 5536-5541.
    • (1989) J Bacteriol , vol.171 , pp. 5536-5541
    • San Millan, J.L.1    Boyd, D.2    Dalbey, R.3    Wickner, W.4    Beckwith, J.5
  • 73
    • 33845869544 scopus 로고    scopus 로고
    • Structural organization of the needle complex of the type III secretion apparatus of Shigella flexneri
    • Sani, M., Allaoui, A., Fusetti, F., Oostergetel, G.T., Keegstra, W., and Boekema, E.J. (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    Allaoui, A.2    Fusetti, F.3    Oostergetel, G.T.4    Keegstra, W.5    Boekema, E.J.6
  • 74
    • 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
  • 75
    • 77954067915 scopus 로고    scopus 로고
    • Topology and organization of the Salmonella typhimurium type III secretion needle complex components
    • Schraidt, O., Lefebre, M.D., Brunner, M.J., Schmied, W.H., Schmidt, A., Radics, J., etal. (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    Lefebre, M.D.2    Brunner, M.J.3    Schmied, W.H.4    Schmidt, A.5    Radics, J.6
  • 76
    • 13444303937 scopus 로고    scopus 로고
    • Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis
    • Schubot, F.D., Jackson, M.W., Penrose, K.J., Cherry, S., Tropea, J.E., Plano, G.V., etal. (2005) Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis. J Mol Biol 346: 1147-1161.
    • (2005) J Mol Biol , vol.346 , pp. 1147-1161
    • Schubot, F.D.1    Jackson, M.W.2    Penrose, K.J.3    Cherry, S.4    Tropea, J.E.5    Plano, G.V.6
  • 77
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Soding, J. (2005) Protein homology detection by HMM-HMM comparison. Bioinformatics 21: 951-960.
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Soding, J.1
  • 78
    • 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 USA 92: 11998-12002.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11998-12002
    • Sory, M.P.1    Boland, A.2    Lambermont, I.3    Cornelis, G.R.4
  • 79
    • 66149092022 scopus 로고    scopus 로고
    • A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system
    • Spreter, T., Yip, C.K., Sanowar, S., Andre, I., Kimbrough, T.G., Vuckovic, M., etal. (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    Yip, C.K.2    Sanowar, S.3    Andre, I.4    Kimbrough, T.G.5    Vuckovic, M.6
  • 80
    • 0035145235 scopus 로고    scopus 로고
    • Genetic analysis of assembly of the Salmonella enterica serovar Typhimurium type III secretion-associated needle complex
    • Sukhan, A., Kubori, T., Wilson, J., and Galan, J.E. (2001) Genetic analysis of assembly of the Salmonella enterica serovar Typhimurium type III secretion-associated needle complex. J Bacteriol 183: 1159-1167.
    • (2001) J Bacteriol , vol.183 , pp. 1159-1167
    • Sukhan, A.1    Kubori, T.2    Wilson, J.3    Galan, J.E.4
  • 81
    • 0038190990 scopus 로고    scopus 로고
    • Synthesis and localization of the Salmonella SPI-1 type III secretion needle complex proteins PrgI and PrgJ
    • Sukhan, A., Kubori, T., and Galan, J.E. (2003) Synthesis and localization of the Salmonella SPI-1 type III secretion needle complex proteins PrgI and PrgJ. J Bacteriol 185: 3480-3483.
    • (2003) J Bacteriol , vol.185 , pp. 3480-3483
    • Sukhan, A.1    Kubori, T.2    Galan, J.E.3
  • 82
    • 40649128950 scopus 로고    scopus 로고
    • Structural characterization of the Yersinia pestis type III secretion system needle protein YscF in complex with its heterodimeric chaperone YscE/YscG
    • Sun, P., Tropea, J.E., Austin, B., Cherry, S., and Waugh, D.S. (2008) Structural characterization of the Yersinia pestis type III secretion system needle protein YscF in complex with its heterodimeric chaperone YscE/YscG. J Mol Biol 377: 819-830.
    • (2008) J Mol Biol , vol.377 , pp. 819-830
    • Sun, P.1    Tropea, J.E.2    Austin, B.3    Cherry, S.4    Waugh, D.S.5
  • 83
    • 26844521751 scopus 로고    scopus 로고
    • Type III secretion: more systems than you think
    • Troisfontaines, P., and Cornelis, G.R. (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
  • 84
    • 0028951802 scopus 로고
    • The hrp gene locus of Pseudomonas solanacearum, which controls the production of a type III secretion system, encodes eight proteins related to components of the bacterial flagellar biogenesis complex
    • Van Gijsegem, F., Gough, C., Zischek, C., Niqueux, E., Arlat, M., Genin, S., etal. (1995) The hrp gene locus of Pseudomonas solanacearum, which controls the production of a type III secretion system, encodes eight proteins related to components of the bacterial flagellar biogenesis complex. Mol Microbiol 15: 1095-1114.
    • (1995) Mol Microbiol , vol.15 , pp. 1095-1114
    • Van Gijsegem, F.1    Gough, C.2    Zischek, C.3    Niqueux, E.4    Arlat, M.5    Genin, S.6
  • 87
    • 0027499076 scopus 로고
    • SycE, a chaperone-like protein of Yersinia enterocolitica involved in the secretion of YopE
    • Wattiau, P., and Cornelis, G.R. (1993) SycE, a chaperone-like protein of Yersinia enterocolitica involved in the secretion of YopE. Mol Microbiol 8: 123-131.
    • (1993) Mol Microbiol , vol.8 , pp. 123-131
    • Wattiau, P.1    Cornelis, G.R.2
  • 89
    • 0029886432 scopus 로고    scopus 로고
    • Customized secretion chaperones in pathogenic bacteria
    • Wattiau, P., Woestyn, S., and Cornelis, G.R. (1996) Customized secretion chaperones in pathogenic bacteria. Mol Microbiol 20: 255-262.
    • (1996) Mol Microbiol , vol.20 , pp. 255-262
    • Wattiau, P.1    Woestyn, S.2    Cornelis, G.R.3
  • 90
    • 20044379025 scopus 로고    scopus 로고
    • Optimization of virulence functions through glucosylation of Shigella LPS
    • West, N.P., Sansonetti, P., Mounier, J., Exley, R.M., Parsot, C., Guadagnini, S., etal. (2005) Optimization of virulence functions through glucosylation of Shigella LPS. Science 307: 1313-1317.
    • (2005) Science , vol.307 , pp. 1313-1317
    • West, N.P.1    Sansonetti, P.2    Mounier, J.3    Exley, R.M.4    Parsot, C.5    Guadagnini, S.6
  • 91
    • 0028292926 scopus 로고
    • YscN, the putative energizer of the Yersinia Yop secretion machinery
    • Woestyn, S., Allaoui, A., Wattiau, P., and Cornelis, G.R. (1994) YscN, the putative energizer of the Yersinia Yop secretion machinery. J Bacteriol 176: 1561-1569.
    • (1994) J Bacteriol , vol.176 , pp. 1561-1569
    • Woestyn, S.1    Allaoui, A.2    Wattiau, P.3    Cornelis, G.R.4
  • 92
    • 44949221276 scopus 로고    scopus 로고
    • YscP and YscU switch the substrate specificity of the Yersinia type III secretion system by regulating export of the inner rod protein YscI
    • Wood, S.E., Jin, J., and Lloyd, S.A. (2008) YscP and YscU switch the substrate specificity of the Yersinia type III secretion system by regulating export of the inner rod protein YscI. J Bacteriol 190: 4252-4262.
    • (2008) J Bacteriol , vol.190 , pp. 4252-4262
    • Wood, S.E.1    Jin, J.2    Lloyd, S.A.3
  • 93
    • 77954224937 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal domain of the Salmonella type III secretion system export apparatus protein InvA
    • Worrall, L.J., Vuckovic, M., and Strynadka, N.C. (2010) Crystal structure of the C-terminal domain of the Salmonella type III secretion system export apparatus protein InvA. Protein Sci 19: 1091-1096.
    • (2010) Protein Sci , vol.19 , pp. 1091-1096
    • Worrall, L.J.1    Vuckovic, M.2    Strynadka, N.C.3
  • 94
    • 34147161055 scopus 로고    scopus 로고
    • Regulatory role of PopN and its interacting partners in type III secretion of Pseudomonas aeruginosa
    • Yang, H., Shan, Z., Kim, J., Wu, W., Lian, W., Zeng, L., etal. (2007) Regulatory role of PopN and its interacting partners in type III secretion of Pseudomonas aeruginosa. J Bacteriol 189: 2599-2609.
    • (2007) J Bacteriol , vol.189 , pp. 2599-2609
    • Yang, H.1    Shan, Z.2    Kim, J.3    Wu, W.4    Lian, W.5    Zeng, L.6
  • 95
    • 33846941536 scopus 로고    scopus 로고
    • Structural analysis of a prototypical ATPase from the type III secretion system
    • Zarivach, R., Vuckovic, M., Deng, W., Finlay, B.B., and Strynadka, N.C. (2007) Structural analysis of a prototypical ATPase from the type III secretion system. Nat Struct Mol Biol 14: 131-137.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 131-137
    • Zarivach, R.1    Vuckovic, M.2    Deng, W.3    Finlay, B.B.4    Strynadka, N.C.5


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