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Volumn 391, Issue 7, 2010, Pages 745-751

The type III secretion injectisome, a complex nanomachine for intracellular 'toxin' delivery

Author keywords

microbial pathogenesis; protein secretion; virulence; Yersinia

Indexed keywords

PEPTIDOGLYCAN; PROTEIN SUBUNIT;

EID: 77954597457     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2010.079     Document Type: Short Survey
Times cited : (103)

References (91)
  • 1
    • 16244407371 scopus 로고    scopus 로고
    • Characterization of a type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia ente-rocolitica
    • Agrain, C, Callebaut, I., Journet, L., Sorg, I., Paroz, C, Mota, L.J., et al. (2005a). Characterization of a type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia ente-rocolitica. 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
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type III secretion
    • Akeda, Y. and Galan, J.E. (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
  • 4
    • 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
  • 5
    • 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
  • 6
    • 33646543996 scopus 로고    scopus 로고
    • Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator, YscL
    • DOI 10.1128/JB.188.10.3525-3534.2006
    • Blaylock, B., Riordan, K.E., Missiakas, D.M., and Schneewind, O. (2006). Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator, YscL. J. Bacteriol. 188, 3525-3534. (Pubitemid 43726217)
    • (2006) Journal of Bacteriology , vol.188 , Issue.10 , pp. 3525-3534
    • Blaylock, B.1    Riordan, K.E.2    Missiakas, D.M.3    Schneewind, O.4
  • 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., Par-sot, C., et al. (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    Par-Sot, C.6
  • 8
    • 0035133489 scopus 로고    scopus 로고
    • Structure and composition of the Shigella flex-neri 'needle complex', a part of its type III secreton
    • Blocker, A., Jouihri, N., Larquet, E., Gounon, P., Ebel, F., Parsot, C., et al. (2001). Structure and composition of the Shigella flex-neri 'needle complex', a part of its type III secreton. Mol. Microbiol. 39, 652-663.
    • (2001) Mol. Microbiol. , vol.39 , pp. 652-663
    • Blocker, A.1    Jouihri, N.2    Larquet, E.3    Gounon, P.4    Ebel, F.5    Parsot, C.6
  • 10
    • 34547908488 scopus 로고    scopus 로고
    • Function and molecular architecture of the Yer-sinia injectisome tip complex
    • Broz, P., Mueller, C.A., Muller, S.A., Philippsen, A., Sorg, I., Engel, A., et al. (2007). Function and molecular architecture of the Yer-sinia injectisome tip complex. Mol. Microbiol. 65, 1311-1320.
    • (2007) Mol. Microbiol. , vol.65 , pp. 1311-1320
    • Broz, P.1    Mueller, C.A.2    Muller, S.A.3    Philippsen, A.4    Sorg, I.5    Engel, A.6
  • 11
    • 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., et al. (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
  • 12
    • 3042812521 scopus 로고    scopus 로고
    • Structure and electrophysio-logical 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., et al. (2004b). Structure and electrophysio-logical properties of the YscC secretin from the type III secretion system of Yersinia enterocolitica. J. Bacteriol. 186, 46454654.
    • (2004) J. Bacteriol. , vol.186 , pp. 46454654
    • Burghout, P.1    Van Boxtel, R.2    Van Gelder, P.3    Ringler, P.4    Muller, S.A.5    Tommassen, J.6
  • 13
    • 1442283765 scopus 로고    scopus 로고
    • Association of Type III secretion genes with virulence of Aeromonas salmonicida subsp. salmonicida
    • Burr, S.E., Wahli, T., Segner, H., Pugovkin, D., and Frey, J. (2003). Association of type III secretion genes with virulence of Aero-monas salmonicida subsp. salmonicida. Dis. Aquat. Organ. 57, 167-171. (Pubitemid 38345271)
    • (2003) Diseases of Aquatic Organisms , vol.57 , Issue.1-2 , pp. 167-171
    • Burr, S.E.1    Wahli, T.2    Segner, H.3    Pugovkin, D.4    Frey, J.5
  • 15
    • 0038460046 scopus 로고    scopus 로고
    • Lig- omerization and activation of the FliI ATPase central to bacterial flagellum assembly
    • Claret, L., Calder, S.R., Higgins, M., and Hughes, C. (2003). Olig- omerization and activation of the FliI ATPase central to bacterial flagellum assembly. Mol. Microbiol. 48, 1349-1355.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1349-1355
    • Claret, L.1    Calder, S.R.2    Higgins, M.3    Hughes, C.4
  • 16
    • 4544346057 scopus 로고    scopus 로고
    • Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 A resolution
    • Collins, R.F., Frye, S.A., Kitmitto, A., Ford, R.C., Tonjum, T., and Derrick, J.P. (2004). Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 A resolution. J. Biol. Chem. 279, 39750-39756.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39750-39756
    • Collins, R.F.1    Frye, S.A.2    Kitmitto, A.3    Ford, R.C.4    Tonjum, T.5    Derrick, J.P.6
  • 17
    • 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., et al. (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
  • 18
    • 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, 735774.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 735774
    • Cornelis, G.R.1    Van Gijsegem, F.2
  • 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. Micro- biol. 23, 861-867.
    • (1997) Mol. Micro- Biol. , vol.23 , pp. 861-867
    • Cornelis, G.R.1    Wolf-Watz, H.2
  • 20
    • 0031665154 scopus 로고    scopus 로고
    • Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization
    • Crago, A.M. and Koronakis, V. (1998). Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization. Mol. Microbiol. 30, 47-56.
    • (1998) Mol. Microbiol. , vol.30 , pp. 47-56
    • Crago, A.M.1    Koronakis, V.2
  • 21
    • 15944376254 scopus 로고    scopus 로고
    • Structural and functional studies of the enteropathogenic Escherichia coli type III needle complex protein EscJ
    • Crepin, V.F., Prasannan, S., Shaw, R.K., Wilson, R.K., Creasey, E., Abe, C.M., et al. (2005). Structural and functional studies of the enteropathogenic Escherichia coli type III needle complex protein EscJ. Mol. Microbiol. 55, 1658-1670.
    • (2005) Mol. Microbiol. , vol.55 , pp. 1658-1670
    • Crepin, V.F.1    Prasannan, S.2    Shaw, R.K.3    Wilson, R.K.4    Creasey, E.5    Abe, C.M.6
  • 22
    • 0031777144 scopus 로고    scopus 로고
    • The Salmonella typhimurium InvH protein is an outer membrane lipoprotein required for the proper localization of InvG
    • Daefler, S. and Russel, M. (1998). The Salmonella typhimurium InvH protein is an outer membrane lipoprotein required for the proper localization of InvG. Mol. Microbiol. 28, 1367-1380.
    • (1998) Mol. Microbiol. , vol.28 , pp. 1367-1380
    • Daefler, S.1    Russel, M.2
  • 24
    • 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., et al. (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
  • 25
    • 1242328668 scopus 로고    scopus 로고
    • The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague
    • Derewenda, U., Mateja, A., Devedjiev, Y., Routzahn, K.M., Evdo-kimov, A.G., Derewenda, Z.S., et al. (2004). The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague. Structure (Camb.) 12, 301-306.
    • (2004) Structure (Camb.) , vol.12 , pp. 301-306
    • Derewenda, U.1    Mateja, A.2    Devedjiev, Y.3    Routzahn, K.M.4    Evdo-Kimov, A.G.5    Derewenda, Z.S.6
  • 26
    • 0025374078 scopus 로고
    • Additional structures associated with bacterial flagellar basal body
    • Driks, A. and DeRosier, D.J. (1990). Additional structures associated with bacterial flagellar basal body. J. Mol. Biol. 211, 669-672.
    • (1990) J. Mol. Biol. , vol.211 , pp. 669-672
    • Driks, A.1    Derosier, D.J.2
  • 27
    • 74349129713 scopus 로고    scopus 로고
    • C-ring requirement in flagel-lar type III secretion is bypassed by FlhDC upregulation
    • Erhardt, M. and Hughes, K.T. (2010). C-ring requirement in flagel-lar type III secretion is bypassed by FlhDC upregulation. Mol. Microbiol. 75, 376-393.
    • Mol. Microbiol. , vol.2010 , Issue.75 , pp. 376-393
    • Erhardt, M.1    Hughes, K.T.2
  • 29
    • 33750992443 scopus 로고    scopus 로고
    • Flipping the switch: Bringing order to flagellar assembly
    • Ferris, H.U. and Minamino, T. (2006). Flipping the switch: bringing order to flagellar assembly. Trends Microbiol. 14, 519-526.
    • (2006) Trends Microbiol. , vol.14 , pp. 519-526
    • Ferris, H.U.1    Minamino, T.2
  • 30
    • 0028178610 scopus 로고
    • A low-Ca2q response (LCR) secretion (ysc) locus lies within the lcrB region of the LCR plasmid in Yersinia pestis
    • Fields, K.A., Plano, G.V., and Straley, S.C. (1994). A low-Ca2q response (LCR) secretion (ysc) locus lies within the lcrB region of the LCR plasmid in Yersinia pestis. J. Bacteriol. 176, 569579.
    • (1994) J. Bacteriol. , vol.176 , pp. 569579
    • Fields, K.A.1    Plano, G.V.2    Straley, S.C.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
    • 0036041918 scopus 로고    scopus 로고
    • Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway
    • Gonzalez-Pedrajo, B., Fraser, G.M., Minamino, T., and Macnab, R.M. (2002). Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway. Mol. Microbiol. 45, 967-982.
    • (2002) Mol. Microbiol. , vol.45 , pp. 967-982
    • Gonzalez-Pedrajo, B.1    Fraser, G.M.2    Minamino, T.3    MacNab, R.M.4
  • 33
    • 0141430076 scopus 로고    scopus 로고
    • Bacterial type III secretion systems are ancient and evolved by multiple horizontal-transfer events
    • Gophna, U., Ron, E.Z., and Graur, D. (2003). Bacterial type III secretion systems are ancient and evolved by multiple horizontal-transfer events. Gene 312, 151-163.
    • (2003) Gene , vol.312 , pp. 151-163
    • Gophna, U.1    Ron, E.Z.2    Graur, D.3
  • 34
    • 3343006984 scopus 로고    scopus 로고
    • The v antigen of Pseudomonas aeruginosa is required for assembly of the functional PopB/PopD translocation pore in host cell membranes
    • Goure, J., Pastor, A., Faudry, E., Chabert, J., Dessen, A., and Attree, I. (2004). The V antigen of Pseudomonas aeruginosa is required for assembly of the functional PopB/PopD translocation pore in host cell membranes. Infect. Immun. 72, 4741-4750.
    • (2004) Infect. Immun. , vol.72 , pp. 4741-4750
    • Goure, J.1    Pastor, A.2    Faudry, E.3    Chabert, J.4    Dessen, A.5    Attree, I.6
  • 35
    • 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, 425-449.
    • (2006) Annu. Rev. Microbiol. , vol.60 , pp. 425-449
    • Grant, S.R.1    Fisher, E.J.2    Chang, J.H.3    Mole, B.M.4    Dangl, J.L.5
  • 36
    • 0029930059 scopus 로고    scopus 로고
    • The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane
    • Hakansson, S., Galyov, E.E., Rosqvist, R., and Wolf-Watz, H. (1996). The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane. Mol. Microbiol. 20, 593-603.
    • (1996) Mol. Microbiol. , vol.20 , pp. 593-603
    • Hakansson, S.1    Galyov, E.E.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 37
    • 0028093390 scopus 로고
    • Roles of FliK and FlhB in determination of flagellar hook length in Salmonella typhimurium
    • Hirano, T., Yamaguchi, S., Oosawa, K., and Aizawa, S. (1994). Roles of FliK and FlhB in determination of flagellar hook length in Salmonella typhimurium. J. Bacteriol. 176, 5439-5449.
    • (1994) J. Bacteriol. , vol.176 , pp. 5439-5449
    • Hirano, T.1    Yamaguchi, S.2    Oosawa, K.3    Aizawa, S.4
  • 38
    • 66149119448 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of the Shigella T3SS transmembrane regions reveals 12-fold symmetry and novel features throughout
    • Hodgkinson, J.L., Horsley, A., Stabat, D., Simon, M., Johnson, S., da Fonseca, P.C., et al. (2009). Three-dimensional reconstruction of the Shigella T3SS transmembrane regions reveals 12-fold symmetry and novel features throughout. Nat. Struct. Mol. Biol. 16, 477-485.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 477-485
    • Hodgkinson, J.L.1    Horsley, A.2    Stabat, D.3    Simon, M.4    Johnson, S.5    Da Fonseca, P.C.6
  • 39
    • 0035836714 scopus 로고    scopus 로고
    • Polymerization of a single protein of the pathogen Yersinia enterocolitica into needles punctures eukaryotic cells
    • Hoiczyk, E. and Blobel, G. (2001). Polymerization of a single protein of the pathogen Yersinia enterocolitica into needles punctures eukaryotic cells. Proc. Natl. Acad. Sci. USA 98, 46694674.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 46694674
    • Hoiczyk, E.1    Blobel, G.2
  • 40
    • 0034193707 scopus 로고    scopus 로고
    • Interactions between type III secretion apparatus components from Yersinia pestis detected using the yeast two-hybrid system
    • Jackson, M.W. and Plano, G.V. (2000). Interactions between type III secretion apparatus components from Yersinia pestis detected using the yeast two-hybrid system. FEMS Microbiol. Lett. 186, 85-90.
    • (2000) FEMS Microbiol. Lett. , vol.186 , pp. 85-90
    • Jackson, M.W.1    Plano, G.V.2
  • 41
    • 0035930715 scopus 로고    scopus 로고
    • Role of the Hrp pilus in type III protein secretion in Pseudomonas syringae
    • Jin, Q. and He, S.Y. (2001). Role of the Hrp pilus in type III protein secretion in Pseudomonas syringae. Science 294, 2556-2558.
    • (2001) Science , vol.294 , pp. 2556-2558
    • Jin, Q.1    He, S.Y.2
  • 42
    • 0041663990 scopus 로고    scopus 로고
    • MxiK and MxiN interact with the Spa47 ATPase and are required for transit of the needle components MxiH and MxiI, but not of Ipa proteins, through the type III secretion apparatus of Shigella flexneri
    • Jouihri, N., Sory, M.P., Page, A.L., Gounon, P., Parsot, C., and Allaoui, A. (2003). MxiK and MxiN interact with the Spa47 ATPase and are required for transit of the needle components MxiH and MxiI, but not of Ipa proteins, through the type III secretion apparatus of Shigella flexneri. Mol. Microbiol. 49, 755-767.
    • (2003) Mol. Microbiol. , vol.49 , pp. 755-767
    • Jouihri, N.1    Sory, M.P.2    Page, A.L.3    Gounon, P.4    Parsot, C.5    Allaoui, A.6
  • 43
    • 0345600239 scopus 로고    scopus 로고
    • The needle length of bacterial injectisomes is determined by a molecular ruler
    • Journet, L., Agrain, C., Broz, P., and Cornelis, G.R. (2003). The needle length of bacterial injectisomes is determined by a molecular ruler. Science 302, 1757-1760.
    • (2003) Science , vol.302 , pp. 1757-1760
    • Journet, L.1    Agrain, C.2    Broz, P.3    Cornelis, G.R.4
  • 44
    • 0026720647 scopus 로고
    • The cytoplasmic component of the bacterial flagellar motor
    • Khan, I.H., Reese, T.S., and Khan, S. (1992). The cytoplasmic component of the bacterial flagellar motor. Proc. Natl. Acad. Sci. USA 89, 5956-5960.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5956-5960
    • Khan, I.H.1    Reese, T.S.2    Khan, S.3
  • 45
    • 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
  • 46
    • 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, 789797.
    • (1997) Mol. Microbiol. , vol.26 , pp. 789797
    • Koster, M.1    Bitter, W.2    De Cock, H.3    Allaoui, A.4    Cornelis, G.R.5    Tommassen, J.6
  • 47
    • 0031023773 scopus 로고    scopus 로고
    • Assembly of the switch complex onto the MS ring complex of Salmonella typhi-murium does not require any other flagellar proteins
    • Kubori, T., Yamaguchi, S., and Aizawa, S. (1997). Assembly of the switch complex onto the MS ring complex of Salmonella typhi-murium does not require any other flagellar proteins. J. Bacteriol. 179, 813-817.
    • (1997) J. Bacteriol. , vol.179 , pp. 813-817
    • Kubori, T.1    Yamaguchi, S.2    Aizawa, S.3
  • 48
    • 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., et al. (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
  • 49
    • 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
  • 50
    • 0037090775 scopus 로고    scopus 로고
    • The Hrp pilus of Pseudomonas syringae elongates from its tip and acts as a conduit for trans-location of the effector protein HrpZ
    • Li, C.M., Brown, I., Mansfield, J., Stevens, C., Boureau, T., Romantschuk, M., et al. (2002). The Hrp pilus of Pseudomonas syringae elongates from its tip and acts as a conduit for trans-location of the effector protein HrpZ. EMBO J. 21, 1909-1915.
    • (2002) EMBO J. , vol.21 , pp. 1909-1915
    • Li, C.M.1    Brown, I.2    Mansfield, J.3    Stevens, C.4    Boureau, T.5    Romantschuk, M.6
  • 51
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab, R.M. (2003). How bacteria assemble flagella. Annu. Rev. Microbiol. 57, 77-100.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 77-100
    • MacNab, R.M.1
  • 52
    • 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
  • 53
    • 33745279057 scopus 로고    scopus 로고
    • Assembly of the inner rod determines needle length in the type III secretion injectisome
    • Marlovits, T.C., Kubori, T., Lara-Tejero, M., Thomas, D., Unger, V.M., and Galan, J.E. (2006). Assembly of the inner rod determines needle length in the type III secretion injectisome. Nature 441, 637-640.
    • (2006) Nature , vol.441 , pp. 637-640
    • Marlovits, T.C.1    Kubori, T.2    Lara-Tejero, M.3    Thomas, D.4    Unger, V.M.5    Galan, J.E.6
  • 54
    • 0034011357 scopus 로고    scopus 로고
    • Interactions among components of the Salmonella flagellar export apparatus and its substrates
    • Minamino, T. and MacNab, R.M. (2000). Interactions among components of the Salmonella flagellar export apparatus and its substrates. Mol. Microbiol. 35, 1052-1064.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1052-1064
    • Minamino, T.1    MacNab, R.M.2
  • 55
    • 38549158887 scopus 로고    scopus 로고
    • Distinct roles of the FliI ATP- ase and proton motive force in bacterial flagellar protein export
    • Minamino, T. and Namba, K. (2008). Distinct roles of the FliI ATP- ase 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
  • 56
    • 0032827183 scopus 로고    scopus 로고
    • FliK, the protein responsible for fla-gellar hook length control in Salmonella, is exported during hook assembly
    • Minamino, T., Gonzalez-Pedrajo, B., Yamaguchi, K., Aizawa, S.I., and Macnab, R.M. (1999). FliK, the protein responsible for fla-gellar hook length control in Salmonella, is exported during hook assembly. Mol. Microbiol. 34, 295-304.
    • (1999) Mol. Microbiol. , vol.34 , pp. 295-304
    • Minamino, T.1    Gonzalez-Pedrajo, B.2    Yamaguchi, K.3    Aizawa, S.I.4    MacNab, R.M.5
  • 59
    • 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
  • 60
    • 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., et al. (2005). The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles. Science 310, 674676.
    • (2005) Science , vol.310 , pp. 674676
    • Mueller, C.A.1    Broz, P.2    Muller, S.A.3    Ringler, P.4    Erne-Brand, F.5    Sorg, I.6
  • 61
    • 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., et al. (2006). Double hexameric ring assembly of the type III protein translocase ATPase HrcN. Mol. Microbiol. 61, 119125.
    • (2006) Mol. Microbiol. , vol.61 , pp. 119125
    • Muller, S.A.1    Pozidis, C.2    Stone, R.3    Meesters, C.4    Chami, M.5    Engel, A.6
  • 62
    • 0032835828 scopus 로고    scopus 로고
    • Insertion of a Yop translocation pore into the macrophage plasma membrane by Yersinia ente-rocolitica: Requirement for translocators YopB and YopD, but not LcrG
    • Neyt, C. and Cornelis, G.R. (1999). Insertion of a Yop translocation pore into the macrophage plasma membrane by Yersinia ente-rocolitica: 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
  • 63
    • 15944409588 scopus 로고    scopus 로고
    • Bioinforma- tics, genomics and evolution of non-flagellar type-III secretion systems: A Darwinian perspective
    • Pallen, M.J., Beatson, S.A., and Bailey, C.M. (2005). Bioinforma- tics, genomics and evolution of non-flagellar type-III secretion systems: a Darwinian perspective. 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
  • 64
    • 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
  • 65
    • 38549088345 scopus 로고    scopus 로고
    • Energy source of flagellar type III secretion
    • Paul, K., Erhardt, M., Hirano, T., Blair, D.F., and Hughes, K.T. (2008). Energy source of flagellar type III secretion. Nature 451, 489-492.
    • (2008) Nature , vol.451 , pp. 489-492
    • Paul, K.1    Erhardt, M.2    Hirano, T.3    Blair, D.F.4    Hughes, K.T.5
  • 66
    • 0027297680 scopus 로고
    • Multiple effects of lcrD mutations in Yersinia pestis
    • Plano, G.V. and Straley, S.C. (1993). Multiple effects of lcrD mutations in Yersinia pestis. J. Bacteriol. 175, 3536-3545.
    • (1993) J. Bacteriol. , vol.175 , pp. 3536-3545
    • Plano, G.V.1    Straley, S.C.2
  • 67
    • 0038507200 scopus 로고    scopus 로고
    • Type III protein trans-locase: HrcN is a peripheral ATPase that is activated by oligo- merization
    • Pozidis, C., Chalkiadaki, A., Gomez-Serrano, A., Stahlberg, H., Brown, I., Tampakaki, A.P., et al. (2003). Type III protein trans-locase: HrcN is a peripheral ATPase that is activated by oligo- merization. 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.P.6
  • 68
    • 0035877065 scopus 로고    scopus 로고
    • Type III protein secretion is associated with death in lower respiratory and systemic Pseu-domonas aeruginosa infections
    • Roy-Burman, A., Savel, R.H., Racine, S., Swanson, B.L., Revadi-gar, N.S., Fujimoto, J., et al. (2001). Type III protein secretion is associated with death in lower respiratory and systemic Pseu-domonas aeruginosa infections. J. Infect. Dis. 183, 1767-1774.
    • (2001) J. Infect. Dis. , vol.183 , pp. 1767-1774
    • Roy-Burman, A.1    Savel, R.H.2    Racine, S.3    Swanson, B.L.4    Revadi-Gar, N.S.5    Fujimoto, J.6
  • 69
    • 0027982566 scopus 로고
    • Phage assembly: A paradigm for bacterial virulence factor export?
    • Russel, M. (1994). Phage assembly: a paradigm for bacterial virulence factor export? Science 265, 612-614.
    • (1994) Science , vol.265 , pp. 612-614
    • Russel, M.1
  • 70
    • 33845869544 scopus 로고    scopus 로고
    • Structural organization of the needle complex of the type III secretion apparatus of Shigella flexneri
    • DOI 10.1016/j.micron.2006.04.007, PII S0968432806000722
    • 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. (Pubitemid 46027596)
    • (2007) Micron , vol.38 , Issue.3 , pp. 291-301
    • Sani, M.1    Allaoui, A.2    Fusetti, F.3    Oostergetel, G.T.4    Keegstra, W.5    Boekema, E.J.6
  • 71
    • 0035949491 scopus 로고    scopus 로고
    • Supermolecular structure of the enteropathogen-ic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure
    • Sekiya, K., Ohishi, M., Ogino, T., Tamano, K., Sasakawa, C., and Abe, A. (2001). Supermolecular structure of the enteropathogen-ic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure. Proc. Natl. Acad. Sci. USA 98, 11638-11643.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11638-11643
    • Sekiya, K.1    Ohishi, M.2    Ogino, T.3    Tamano, K.4    Sasakawa, C.5    Abe, A.6
  • 72
    • 34250840609 scopus 로고    scopus 로고
    • YscU recognizes translocators as export substrates of the Yersinia injectisome
    • Sorg, I., Wagner, S., Amstutz, M., Muller, S.A., Broz, P., Lussi, Y., 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    Wagner, S.2    Amstutz, M.3    Muller, S.A.4    Broz, P.5    Lussi, Y.6
  • 73
    • 70349672695 scopus 로고    scopus 로고
    • The Chlamydia type III secretion system C-ring engages a chaperone-effector protein complex
    • Spaeth, K.E., Chen, Y.S., and Valdivia, R.H. (2009). The Chlamydia type III secretion system C-ring engages a chaperone-effector protein complex. PLoS Pathog. 5, e1000579.
    • (2009) PLoS Pathog , vol.5
    • Spaeth, K.E.1    Chen, Y.S.2    Valdivia, R.H.3
  • 74
    • 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., et al. (2009). A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system. Nat. Struct. Mol. Biol. 16, 468-476.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 468-476
    • Spreter, T.1    Yip, C.K.2    Sanowar, S.3    Andre, I.4    Kimbrough, T.G.5    Vuckovic, M.6
  • 75
    • 0035145235 scopus 로고    scopus 로고
    • Genetic analysis of assembly of the Salmonella enterica serovar Typhi-murium 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 Typhi-murium type III secretion-associated needle complex. J. Bacte-riol. 183, 1159-1167.
    • (2001) J. Bacte-riol. , vol.183 , pp. 1159-1167
    • Sukhan, A.1    Kubori, T.2    Wilson, J.3    Galan, J.E.4
  • 76
    • 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
  • 77
    • 0034254475 scopus 로고    scopus 로고
    • Supramolecular structure of the Shigella type III secretion machinery: The needle part is changeable in length and essential for delivery of effectors
    • Tamano, K., Aizawa, S., Katayama, E., Nonaka, T., Imajoh-Ohmi, S., Kuwae, A., et al. (2000). Supramolecular structure of the Shigella type III secretion machinery: the needle part is changeable in length and essential for delivery of effectors. EMBO J. 19, 3876-3887.
    • (2000) EMBO J. , vol.19 , pp. 3876-3887
    • Tamano, K.1    Aizawa, S.2    Katayama, E.3    Nonaka, T.4    Imajoh-Ohmi, S.5    Kuwae, A.6
  • 78
    • 33749608423 scopus 로고    scopus 로고
    • The three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar Typhi- murium
    • Thomas, D.R., Francis, N.R., Xu, C., and DeRosier, D.J. (2006). The three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar Typhi- murium. J. Bacteriol. 188, 7039-7048.
    • (2006) J. Bacteriol. , vol.188 , pp. 7039-7048
    • Thomas, D.R.1    Francis, N.R.2    Xu, C.3    Derosier, D.J.4
  • 79
    • 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, 326339.
    • (2005) Physiology (Bethesda) , vol.20 , pp. 326339
    • Troisfontaines, P.1    Cornelis, G.R.2
  • 80
    • 0028210772 scopus 로고
    • Domain structures of the MS ring component protein (FliF) of the flagellar basal body of Salmonella typhimurium
    • Ueno, T., Oosawa, K., and Aizawa, S. (1994). Domain structures of the MS ring component protein (FliF) of the flagellar basal body of Salmonella typhimurium. J. Mol. Biol. 236, 546-555.
    • (1994) J. Mol. Biol. , vol.236 , pp. 546-555
    • Ueno, T.1    Oosawa, K.2    Aizawa, S.3
  • 81
    • 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., et al. (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
  • 82
    • 58649109819 scopus 로고    scopus 로고
    • The helical content of the YscP molecular ruler determines the length of the Yersinia injecti- some
    • Wagner, S., Sorg, I., Degiacomi, M., Journet, L., Dal Peraro, M., and Cornelis, G.R. (2009). The helical content of the YscP molecular ruler determines the length of the Yersinia injecti- some. Mol. Microbiol. 71, 692-701.
    • (2009) Mol. Microbiol. , vol.71 , pp. 692-701
    • Wagner, S.1    Sorg, I.2    Degiacomi, M.3    Journet, L.4    Dal Peraro, M.5    Cornelis, G.R.6
  • 83
    • 58149112120 scopus 로고    scopus 로고
    • Structure of the type III secretion recognition protein YscU from Yersinia enterocolitica
    • Wiesand, U., Sorg, I., Amstutz, M., Wagner, S., van den Heuvel, J., Luhrs, T., et al. (2009). Structure of the type III secretion recognition protein YscU from Yersinia enterocolitica. J. Mol. Biol. 385, 854-866.
    • (2009) J. Mol. Biol. , vol.385 , pp. 854-866
    • Wiesand, U.1    Sorg, I.2    Amstutz, M.3    Wagner, S.4    Van Den Heuvel, J.5    Luhrs, T.6
  • 84
    • 3042692057 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion depends on the proton motive force but not on the flagellar motor components MotA and MotB
    • Wilharm, G., Lehmann, V., Krauss, K., Lehnert, B., Richter, S., Ruckdeschel, K., et al. (2004). Yersinia enterocolitica type III secretion depends on the proton motive force but not on the flagellar motor components MotA and MotB. Infect. Immun. 72, 4004-4009.
    • (2004) Infect. Immun. , vol.72 , pp. 4004-4009
    • Wilharm, G.1    Lehmann, V.2    Krauss, K.3    Lehnert, B.4    Richter, S.5    Ruckdeschel, K.6
  • 85
    • 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
  • 86
    • 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
  • 87
    • 20444488138 scopus 로고    scopus 로고
    • Structural characterization of the molecular platform for type III secretion system assembly
    • Yip, C.K., Kimbrough, T.G., Felise, H.B., Vuckovic, M., Thomas, N.A., Pfuetzner, R.A., et al. (2005). Structural characterization of the molecular platform for type III secretion system assembly. Nature 435, 702-707.
    • (2005) Nature , vol.435 , pp. 702-707
    • Yip, C.K.1    Kimbrough, T.G.2    Felise, H.B.3    Vuckovic, M.4    Thomas, N.A.5    Pfuetzner, R.A.6
  • 88
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryo-microscopy
    • Yonekura, K., Maki-Yonekura, S., and Namba, K. (2003). Complete atomic model of the bacterial flagellar filament by electron cryo-microscopy. Nature 424, 643-650.
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 89
    • 12244302174 scopus 로고    scopus 로고
    • Variable symmetry in Salmonella typhimurium flagellar motors
    • Young, H.S., Dang, H., Lai, Y., DeRosier, D.J., and Khan, S. (2003). Variable symmetry in Salmonella typhimurium flagellar motors. Biophys. J. 84, 571-577.
    • (2003) Biophys. J. , vol.84 , pp. 571-577
    • Young, H.S.1    Dang, H.2    Lai, Y.3    Derosier, D.J.4    Khan, S.5
  • 91
    • 43049127811 scopus 로고    scopus 로고
    • Structural analysis of the essential self-cleaving type III secretion proteins EscU and SpaS
    • Zarivach, R., Deng, W., Vuckovic, M., Felise, H.B., Nguyen, H.V., Miller, S.I., et al. (2008). Structural analysis of the essential self-cleaving type III secretion proteins EscU and SpaS. Nature 453, 124-127.
    • (2008) Nature , vol.453 , pp. 124-127
    • Zarivach, R.1    Deng, W.2    Vuckovic, M.3    Felise, H.B.4    Nguyen, H.V.5    Miller, S.I.6


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