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Volumn 31, Issue 4, 2006, Pages 223-230

New structural insights into the bacterial type III secretion system

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

EID: 33645976151     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2006.02.005     Document Type: Review
Times cited : (46)

References (53)
  • 1
    • 10344249890 scopus 로고    scopus 로고
    • Process of protein transport by the type III secretion system
    • Ghosh P. Process of protein transport by the type III secretion system. Microbiol. Mol. Biol. Rev. 68 (2004) 771-795
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 771-795
    • Ghosh, P.1
  • 2
    • 0032562678 scopus 로고    scopus 로고
    • Supramolecular structure of the Salmonella typhimurium type III protein secretion system
    • Kubori T., et al. Supramolecular structure of the Salmonella typhimurium type III protein secretion system. Science 280 (1998) 602-605
    • (1998) Science , vol.280 , pp. 602-605
    • Kubori, T.1
  • 3
    • 0035133489 scopus 로고    scopus 로고
    • Structure and composition of the Shigella flexneri 'needle complex', a part of its type III secreton
    • Blocker A., et al. Structure and composition of the Shigella flexneri 'needle complex', a part of its type III secreton. Mol. Microbiol. 39 (2001) 652-663
    • (2001) Mol. Microbiol. , vol.39 , pp. 652-663
    • Blocker, A.1
  • 4
    • 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., et al. 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 (2000) 3876-3887
    • (2000) EMBO J. , vol.19 , pp. 3876-3887
    • Tamano, K.1
  • 5
    • 0035949491 scopus 로고    scopus 로고
    • Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure
    • Sekiya K., et al. Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 11638-11643
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11638-11643
    • Sekiya, K.1
  • 6
    • 0035928718 scopus 로고    scopus 로고
    • Bacterial flagella and type III secretion systems
    • Aizawa S.I. Bacterial flagella and type III secretion systems. FEMS Microbiol. Lett. 202 (2001) 157-164
    • (2001) FEMS Microbiol. Lett. , vol.202 , pp. 157-164
    • Aizawa, S.I.1
  • 7
    • 8344258355 scopus 로고    scopus 로고
    • Structural insights into the assembly of the type III secretion needle complex
    • Marlovits T.C., et al. Structural insights into the assembly of the type III secretion needle complex. Science 306 (2004) 1040-1042
    • (2004) Science , vol.306 , pp. 1040-1042
    • Marlovits, T.C.1
  • 8
    • 20444488138 scopus 로고    scopus 로고
    • Structural characterization of the molecular platform for type III secretion system assembly
    • Yip C.K., et al. Structural characterization of the molecular platform for type III secretion system assembly. Nature 435 (2005) 702-707
    • (2005) Nature , vol.435 , pp. 702-707
    • Yip, C.K.1
  • 9
    • 0029998799 scopus 로고    scopus 로고
    • Unified nomenclature for broadly conserved hrp genes of phytopathogenic bacteria
    • Bogdanove A.J., et al. Unified nomenclature for broadly conserved hrp genes of phytopathogenic bacteria. Mol. Microbiol. 20 (1996) 681-683
    • (1996) Mol. Microbiol. , vol.20 , pp. 681-683
    • Bogdanove, A.J.1
  • 10
    • 0038608020 scopus 로고    scopus 로고
    • Helical structure of the needle of the type III secretion system of Shigella flexneri
    • Cordes F.S., et al. Helical structure of the needle of the type III secretion system of Shigella flexneri. J. Biol. Chem. 278 (2003) 17103-17107
    • (2003) J. Biol. Chem. , vol.278 , pp. 17103-17107
    • Cordes, F.S.1
  • 11
    • 0032835828 scopus 로고    scopus 로고
    • Insertion of a Yop translocation pore into the macrophage plasma membrane by Yersinia enterocolitica: requirement for translocators YopB and YopD, but not LcrG
    • Neyt C., and Cornelis G.R. Insertion of a Yop translocation pore into the macrophage plasma membrane by Yersinia enterocolitica: requirement for translocators YopB and YopD, but not LcrG. Mol. Microbiol. 33 (1999) 971-981
    • (1999) Mol. Microbiol. , vol.33 , pp. 971-981
    • Neyt, C.1    Cornelis, G.R.2
  • 12
    • 25144451293 scopus 로고    scopus 로고
    • The Yersinia pestis type III secretion needle plays a role in the regulation of Yop secretion
    • Torruellas J., et al. The Yersinia pestis type III secretion needle plays a role in the regulation of Yop secretion. Mol. Microbiol. 57 (2005) 1719-1733
    • (2005) Mol. Microbiol. , vol.57 , pp. 1719-1733
    • Torruellas, J.1
  • 13
    • 30044445766 scopus 로고    scopus 로고
    • The needle component of the type III secreton of shigella regulates the activity of the secretion apparatus
    • Kenjale R., et al. The needle component of the type III secreton of shigella regulates the activity of the secretion apparatus. J. Biol. Chem. 280 (2005) 42929-42937
    • (2005) J. Biol. Chem. , vol.280 , pp. 42929-42937
    • Kenjale, R.1
  • 14
    • 27644467885 scopus 로고    scopus 로고
    • Helical packing of needles from functionally altered Shigella type III secretion systems
    • Cordes F.S., et al. Helical packing of needles from functionally altered Shigella type III secretion systems. J. Mol. Biol. 354 (2005) 206-211
    • (2005) J. Mol. Biol. , vol.354 , pp. 206-211
    • Cordes, F.S.1
  • 15
    • 0036178888 scopus 로고    scopus 로고
    • Shigella Spa32 is an essential secretory protein for functional type III secretion machinery and uniformity of its needle length
    • Tamano K., et al. Shigella Spa32 is an essential secretory protein for functional type III secretion machinery and uniformity of its needle length. J. Bacteriol. 184 (2002) 1244-1252
    • (2002) J. Bacteriol. , vol.184 , pp. 1244-1252
    • Tamano, K.1
  • 16
    • 0036437055 scopus 로고    scopus 로고
    • Molecular and functional analysis of the type III secretion signal of the Salmonella enterica InvJ protein
    • Russmann H., et al. Molecular and functional analysis of the type III secretion signal of the Salmonella enterica InvJ protein. Mol. Microbiol. 46 (2002) 769-779
    • (2002) Mol. Microbiol. , vol.46 , pp. 769-779
    • Russmann, H.1
  • 17
    • 0345600239 scopus 로고    scopus 로고
    • The needle length of bacterial injectisomes is determined by a molecular ruler
    • Journet L., et al. The needle length of bacterial injectisomes is determined by a molecular ruler. Science 302 (2003) 1757-1760
    • (2003) Science , vol.302 , pp. 1757-1760
    • Journet, L.1
  • 18
    • 20044380517 scopus 로고    scopus 로고
    • Bacterial injectisomes: needle length does matter
    • Mota L.J., et al. Bacterial injectisomes: needle length does matter. Science 307 (2005) 1278
    • (2005) Science , vol.307 , pp. 1278
    • Mota, L.J.1
  • 19
    • 20044379025 scopus 로고    scopus 로고
    • Optimization of virulence functions through glucosylation of Shigella LPS
    • West N.P., et al. Optimization of virulence functions through glucosylation of Shigella LPS. Science 307 (2005) 1313-1317
    • (2005) Science , vol.307 , pp. 1313-1317
    • West, N.P.1
  • 20
    • 27344457144 scopus 로고    scopus 로고
    • The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles
    • Mueller C.A., et al. The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles. Science 310 (2005) 674-676
    • (2005) Science , vol.310 , pp. 674-676
    • Mueller, C.A.1
  • 21
    • 1242328668 scopus 로고    scopus 로고
    • The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague
    • Derewenda U., et al. The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague. Structure 12 (2004) 301-306
    • (2004) Structure , vol.12 , pp. 301-306
    • Derewenda, U.1
  • 22
    • 21244474421 scopus 로고    scopus 로고
    • Formation of a novel surface structure encoded by Salmonella pathogenicity island 2
    • Chakravortty D., et al. Formation of a novel surface structure encoded by Salmonella pathogenicity island 2. EMBO J. 24 (2005) 2043-2052
    • (2005) EMBO J. , vol.24 , pp. 2043-2052
    • Chakravortty, D.1
  • 23
    • 0038501996 scopus 로고    scopus 로고
    • 3D structure of EspA filaments from enteropathogenic Escherichia coli
    • Daniell S.J., et al. 3D structure of EspA filaments from enteropathogenic Escherichia coli. Mol. Microbiol. 49 (2003) 301-308
    • (2003) Mol. Microbiol. , vol.49 , pp. 301-308
    • Daniell, S.J.1
  • 24
    • 11444263137 scopus 로고    scopus 로고
    • Structural characterization of a type III secretion system filament protein in complex with its chaperone
    • Yip C.K., et al. Structural characterization of a type III secretion system filament protein in complex with its chaperone. Nat. Struct. Mol. Biol. 12 (2005) 75-81
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 75-81
    • Yip, C.K.1
  • 25
    • 0347513214 scopus 로고    scopus 로고
    • CesAB is an enteropathogenic Escherichia coli chaperone for the type-III translocator proteins EspA and EspB
    • Creasey E.A., et al. CesAB is an enteropathogenic Escherichia coli chaperone for the type-III translocator proteins EspA and EspB. Microbiology 149 (2003) 3639-3647
    • (2003) Microbiology , vol.149 , pp. 3639-3647
    • Creasey, E.A.1
  • 26
    • 0141618445 scopus 로고    scopus 로고
    • Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion
    • Evdokimov A.G., et al. Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion. Nat. Struct. Biol. 10 (2003) 789-793
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 789-793
    • Evdokimov, A.G.1
  • 27
    • 0035957518 scopus 로고    scopus 로고
    • Flagellin polymerisation control by a cytosolic export chaperone
    • Auvray F., et al. Flagellin polymerisation control by a cytosolic export chaperone. J. Mol. Biol. 308 (2001) 221-229
    • (2001) J. Mol. Biol. , vol.308 , pp. 221-229
    • Auvray, F.1
  • 28
    • 27744509836 scopus 로고    scopus 로고
    • The PscE-PscF-PscG complex controls type III secretion needle biogenesis in Pseudomonas aeruginosa
    • Quinaud M., et al. The PscE-PscF-PscG complex controls type III secretion needle biogenesis in Pseudomonas aeruginosa. J. Biol. Chem. 280 (2005) 36293-36300
    • (2005) J. Biol. Chem. , vol.280 , pp. 36293-36300
    • Quinaud, M.1
  • 29
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura K., et al. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 424 (2003) 643-650
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1
  • 30
    • 0033937939 scopus 로고    scopus 로고
    • Multiple pathways allow protein secretion across the bacterial outer membrane
    • Thanassi D.G., and Hultgren S.J. Multiple pathways allow protein secretion across the bacterial outer membrane. Curr. Opin. Cell Biol. 12 (2000) 420-430
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 420-430
    • Thanassi, D.G.1    Hultgren, S.J.2
  • 31
    • 1842293999 scopus 로고    scopus 로고
    • The filamentous phage pIV multimer visualized by scanning transmission electron microscopy
    • Linderoth N.A., et al. The filamentous phage pIV multimer visualized by scanning transmission electron microscopy. Science 278 (1997) 1635-1638
    • (1997) Science , vol.278 , pp. 1635-1638
    • Linderoth, N.A.1
  • 32
    • 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. Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization. Mol. Microbiol. 30 (1998) 47-56
    • (1998) Mol. Microbiol. , vol.30 , pp. 47-56
    • Crago, A.M.1    Koronakis, V.2
  • 33
    • 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., et al. The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex. Mol. Microbiol. 26 (1997) 789-797
    • (1997) Mol. Microbiol. , vol.26 , pp. 789-797
    • Koster, M.1
  • 34
    • 0034973703 scopus 로고    scopus 로고
    • Analysis of the PilQ secretin from Neisseria meningitidis by transmission electron microscopy reveals a dodecameric quaternary structure
    • Collins R.F., et al. Analysis of the PilQ secretin from Neisseria meningitidis by transmission electron microscopy reveals a dodecameric quaternary structure. J. Bacteriol. 183 (2001) 3825-3832
    • (2001) J. Bacteriol. , vol.183 , pp. 3825-3832
    • Collins, R.F.1
  • 35
    • 3042812521 scopus 로고    scopus 로고
    • Structure and electrophysiological properties of the YscC secretin from the type III secretion system of Yersinia enterocolitica
    • Burghout P., et al. Structure and electrophysiological properties of the YscC secretin from the type III secretion system of Yersinia enterocolitica. J. Bacteriol. 186 (2004) 4645-4654
    • (2004) J. Bacteriol. , vol.186 , pp. 4645-4654
    • Burghout, P.1
  • 36
    • 27844581702 scopus 로고    scopus 로고
    • Structural insights into the secretin PulD and its trypsin-resistant core
    • Chami M., et al. Structural insights into the secretin PulD and its trypsin-resistant core. J. Biol. Chem. 280 (2005) 37732-37741
    • (2005) J. Biol. Chem. , vol.280 , pp. 37732-37741
    • Chami, M.1
  • 37
    • 17144387844 scopus 로고    scopus 로고
    • Structure and biochemical analysis of a secretin pilot protein
    • Lario P.I., et al. Structure and biochemical analysis of a secretin pilot protein. EMBO J. 24 (2005) 1111-1121
    • (2005) EMBO J. , vol.24 , pp. 1111-1121
    • Lario, P.I.1
  • 38
    • 0035145235 scopus 로고    scopus 로고
    • Genetic analysis of assembly of the Salmonella enterica serovar Typhimurium type III secretion-associated needle complex
    • Sukhan A., et al. Genetic analysis of assembly of the Salmonella enterica serovar Typhimurium type III secretion-associated needle complex. J. Bacteriol. 183 (2001) 1159-1167
    • (2001) J. Bacteriol. , vol.183 , pp. 1159-1167
    • Sukhan, A.1
  • 39
    • 0034718542 scopus 로고    scopus 로고
    • Contribution of Salmonella typhimurium type III secretion components to needle complex formation
    • Kimbrough T.G., and Miller S.I. Contribution of Salmonella typhimurium type III secretion components to needle complex formation. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 11008-11013
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 11008-11013
    • Kimbrough, T.G.1    Miller, S.I.2
  • 40
    • 15944376254 scopus 로고    scopus 로고
    • Structural and functional studies of the enteropathogenic Escherichia coli type III needle complex protein Esc
    • Crepin V.F., et al. Structural and functional studies of the enteropathogenic Escherichia coli type III needle complex protein Esc. J. Mol. Microbiol. 55 (2005) 1658-1670
    • (2005) J. Mol. Microbiol. , vol.55 , pp. 1658-1670
    • Crepin, V.F.1
  • 41
    • 1442326719 scopus 로고    scopus 로고
    • Structure of the rotor of the bacterial flagellar motor revealed by electron cryomicroscopy and single-particle image analysis
    • Suzuki H., et al. Structure of the rotor of the bacterial flagellar motor revealed by electron cryomicroscopy and single-particle image analysis. J. Mol. Biol. 337 (2004) 105-113
    • (2004) J. Mol. Biol. , vol.337 , pp. 105-113
    • Suzuki, H.1
  • 42
    • 0029978352 scopus 로고    scopus 로고
    • Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deep-etch replica images
    • Katayama E., et al. Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deep-etch replica images. J. Mol. Biol. 255 (1996) 458-475
    • (1996) J. Mol. Biol. , vol.255 , pp. 458-475
    • Katayama, E.1
  • 43
    • 0033230438 scopus 로고    scopus 로고
    • The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes
    • Blocker A., et al. The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes. J. Cell Biol. 147 (1999) 683-693
    • (1999) J. Cell Biol. , vol.147 , pp. 683-693
    • Blocker, A.1
  • 44
    • 33644860766 scopus 로고    scopus 로고
    • Shigella Spa33 is an essential C-ring component of type III secretion machinery
    • Morita-Ishihara T., et al. Shigella Spa33 is an essential C-ring component of type III secretion machinery. J. Biol. Chem. 281 (2005) 599-607
    • (2005) J. Biol. Chem. , vol.281 , pp. 599-607
    • Morita-Ishihara, T.1
  • 45
    • 0345827609 scopus 로고    scopus 로고
    • Structure of HrcQB-C, a conserved component of the bacterial type III secretion systems
    • Fadouloglou V.E., et al. Structure of HrcQB-C, a conserved component of the bacterial type III secretion systems. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 70-75
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 70-75
    • Fadouloglou, V.E.1
  • 46
    • 16844367441 scopus 로고    scopus 로고
    • Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima
    • Brown P.N., et al. Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima. J. Bacteriol. 187 (2005) 2890-2902
    • (2005) J. Bacteriol. , vol.187 , pp. 2890-2902
    • Brown, P.N.1
  • 47
    • 0037469577 scopus 로고    scopus 로고
    • The multitalented type III chaperones: all you can do with 15 kDa
    • Feldman M.F., and Cornelis G.R. The multitalented type III chaperones: all you can do with 15 kDa. FEMS Microbiol. Lett. 219 (2003) 151-158
    • (2003) FEMS Microbiol. Lett. , vol.219 , pp. 151-158
    • Feldman, M.F.1    Cornelis, G.R.2
  • 48
    • 0345633461 scopus 로고    scopus 로고
    • The various and varying roles of specific chaperones in type III secretion systems
    • Parsot C., et al. The various and varying roles of specific chaperones in type III secretion systems. Curr. Opin. Microbiol. 6 (2003) 7-14
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 7-14
    • Parsot, C.1
  • 49
    • 0034864508 scopus 로고    scopus 로고
    • Regulated secretion of YopN by the type III machinery of Yersinia enterocolitica
    • Cheng L.W., et al. Regulated secretion of YopN by the type III machinery of Yersinia enterocolitica. J. Bacteriol. 183 (2001) 5293-5301
    • (2001) J. Bacteriol. , vol.183 , pp. 5293-5301
    • Cheng, L.W.1
  • 50
    • 13444303937 scopus 로고    scopus 로고
    • Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis
    • Schubot F.D., et al. Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis. J. Mol. Biol. 346 (2005) 1147-1161
    • (2005) J. Mol. Biol. , vol.346 , pp. 1147-1161
    • Schubot, F.D.1
  • 51
    • 0038507200 scopus 로고    scopus 로고
    • Type III protein translocase: HrcN is a peripheral ATPase that is activated by oligomerization
    • Pozidis C., et al. Type III protein translocase: HrcN is a peripheral ATPase that is activated by oligomerization. J. Biol. Chem. 278 (2003) 25816-25824
    • (2003) J. Biol. Chem. , vol.278 , pp. 25816-25824
    • Pozidis, C.1
  • 52
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type III secretion
    • Akeda Y., and Galan J.E. Chaperone release and unfolding of substrates in type III secretion. Nature 437 (2005) 911-915
    • (2005) Nature , vol.437 , pp. 911-915
    • Akeda, Y.1    Galan, J.E.2
  • 53
    • 5344269437 scopus 로고    scopus 로고
    • + proteases and disassembly machines
    • + proteases and disassembly machines. Cell 119 (2004) 9-18
    • (2004) Cell , vol.119 , pp. 9-18
    • Sauer, R.T.1


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