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Volumn 3, Issue , 2013, Pages

Common and distinct structural features of Salmonella injectisome and flagellar basal body

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN;

EID: 84889777894     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep03369     Document Type: Article
Times cited : (115)

References (41)
  • 1
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • Hueck, C. J. Type III protein secretion systems in bacterial pathogens of animals and plants. Mol. Biol. Rev. 62, 379-433 (1998) (Pubitemid 28270280)
    • (1998) Microbiology and Molecular Biology Reviews , vol.62 , Issue.2 , pp. 379-433
    • Hueck, C.J.1
  • 3
    • 58149347646 scopus 로고    scopus 로고
    • Mechanisms of type III protein export for bacterial flagellar assembly
    • Minamino, T., Imada, K. & Namba, K. Mechanisms of type III protein export for bacterial flagellar assembly. Mol. Biosyst. 4, 1105-1115 (2008)
    • (2008) Mol. Biosyst , vol.4 , pp. 1105-1115
    • Minamino, T.1    Imada, K.2    Namba, K.3
  • 5
    • 79952262440 scopus 로고    scopus 로고
    • Three-dimensional model of Salmonella's needle complex at subnanometer resolution
    • Schraidt, O. & Marlovits, T. C. Three-dimensional model of Salmonella's needle complex at subnanometer resolution. Science. 331, 1192-1195 (2011)
    • (2011) Science , vol.331 , pp. 1192-1195
    • Schraidt, O.1    Marlovits, T.C.2
  • 6
    • 33749608423 scopus 로고    scopus 로고
    • The three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar typhimurium
    • DOI 10.1128/JB.00552-06
    • Thomas, D. R., Francis, N. R., Xu, C. & DeRosier, D. J. The three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar Typhimurium. J. Bacteriol. 188, 7039-7048 (2006) (Pubitemid 44547609)
    • (2006) Journal of Bacteriology , vol.188 , Issue.20 , pp. 7039-7048
    • Thomas, D.R.1    Francis, N.R.2    Xu, C.3    DeRosier, D.J.4
  • 7
    • 78049282477 scopus 로고    scopus 로고
    • Organization and coordinated assembly of the type III secretion export apparatus
    • Wagner, S. et al. Organization and coordinated assembly of the type III secretion export apparatus. Proc. Natl. Acad. Sci. U.S.A. 107, 17745-17750 (2010)
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 17745-17750
    • Wagner, S.1
  • 8
    • 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. & Galán, J. E. A sorting platform determines the order of protein secretion in bacterial type III systems. Science. 331, 1188-1191 (2011)
    • (2011) Science , vol.331 , pp. 1188-1191
    • Lara-Tejero, M.1    Kato, J.2    Wagner, S.3    Liu, X.4    Galán, J.E.5
  • 9
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type III secretion
    • DOI 10.1038/nature03992, PII N03992
    • Akeda, Y. & Galán, J. E. Chaperone release and unfolding of substrates in type III secretion. Nature. 437, 911-915 (2005) (Pubitemid 41486769)
    • (2005) Nature , vol.437 , Issue.7060 , pp. 911-915
    • Akeda, Y.1    Galan, J.E.2
  • 10
    • 33646435299 scopus 로고    scopus 로고
    • Interactions between C ring proteins and export apparatus components: A possible mechanism for facilitating type III protein export
    • González-Pedrajo, B., Minamino, T., Kihara, M. & Namba, K. Interactions between C ring proteins and export apparatus components: A possible mechanism for facilitating type III protein export. Mol. Micriobiol. 60, 984-998 (2006)
    • (2006) Mol. Micriobiol , vol.60 , pp. 984-998
    • González-Pedrajo, B.1    Minamino, T.2    Kihara, M.3    Namba, K.4
  • 11
    • 77954067915 scopus 로고    scopus 로고
    • Topology and organization of the Salmonella typhimurium type III secretion needle complex components
    • Schraidt, O. et al. Topology and organization of the Salmonella typhimurium type III secretion needle complex components. PLoS Pathog. 6, e1000824 (2010)
    • (2010) PLoS Pathog , vol.6
    • Schraidt, O.1
  • 12
    • 1442326719 scopus 로고    scopus 로고
    • Structure of the rotor of the bacterial flagellar motor revealed by electron cryomicroscopy and single-particle image analysis
    • DOI 10.1016/j.jmb.2004.01.034
    • Suzuki, H., Yonekura, K. & Namba, K. Structure of the rotor of the bacterial flagellar motor revealed by electron cryomicroscopy and single-particle image analysis. J. Mol. Biol. 337, 105-113 (2004) (Pubitemid 38270251)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.1 , pp. 105-113
    • Suzuki, H.1    Yonekura, K.2    Namba, K.3
  • 14
    • 84881044066 scopus 로고    scopus 로고
    • In situ structural analysis of the Yersinia enterocolitica injectisome
    • Kudryashev, M. et al. In situ structural analysis of the Yersinia enterocolitica injectisome. eLife. 2, e00792 (2013)
    • (2013) ELife , vol.2
    • Kudryashev, M.1
  • 15
    • 79960620016 scopus 로고    scopus 로고
    • Structure diversity of bacterial flagellar motors
    • Chen, S. et al. Structure diversity of bacterial flagellar motors. EMBO J. 30, 2972-2981 (2011)
    • (2011) EMBO J , vol.30 , pp. 2972-2981
    • Chen, S.1
  • 16
    • 84872007514 scopus 로고    scopus 로고
    • Architecture of the major component of the type III secretion system export apparatus
    • Abrusci, P. et al. Architecture of the major component of the type III secretion system export apparatus. Nat. Struct. Mol. Biol. 20, 99-104 (2012)
    • (2012) Nat. Struct. Mol. Biol , vol.20 , pp. 99-104
    • Abrusci, P.1
  • 17
    • 77950244006 scopus 로고    scopus 로고
    • Structure of the cytoplasmic domain of FlhA and implication for flagellar type III protein export
    • Saijo-Hamano, Y. et al. Structure of the cytoplasmic domain of FlhA and implication for flagellar type III protein export. Mol. Microbiol. 76, 260-268 (2010)
    • (2010) Mol. Microbiol , vol.76 , pp. 260-268
    • Saijo-Hamano, Y.1
  • 19
    • 84876840449 scopus 로고    scopus 로고
    • A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly
    • Bergeron, J. R. C. et al. A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly. PLOS Pathog. 9, e1003307 (2013)
    • (2013) PLOS Pathog , vol.9
    • Bergeron, J.R.C.1
  • 20
    • 72049109167 scopus 로고    scopus 로고
    • Roles of the extreme N-terminal region of FliH for efficient localization of the FliH-FliI complex to the bacterial flagellar type III export apparatus
    • Minamino, T. et al. Roles of the extreme N-terminal region of FliH for efficient localization of the FliH-FliI complex to the bacterial flagellar type III export apparatus. Mol. Microbiol. 74, 1471-1483 (2009)
    • (2009) Mol. Microbiol , vol.74 , pp. 1471-1483
    • Minamino, T.1
  • 22
    • 16844367441 scopus 로고    scopus 로고
    • Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima
    • Brown, P. N., Mathews, M. A. A., Joss, L. A., Hill, C. P. & Blair, D. F. Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima. J. Bacteriol. 187, 2890 (2005)
    • (2005) J. Bacteriol , vol.187 , pp. 2890
    • Brown, P.N.1    Mathews, M.A.A.2    Joss, L.A.3    Hill, C.P.4    Blair, D.F.5
  • 23
    • 77953123027 scopus 로고    scopus 로고
    • Deciphering the assembly of the Yersinia type III secretion injectisome
    • Diepold, A. et al. Deciphering the assembly of the Yersinia type III secretion injectisome. EMBO J. 29, 1928-1940 (2010)
    • (2010) EMBO J , vol.29 , pp. 1928-1940
    • Diepold, A.1
  • 24
    • 38549158887 scopus 로고    scopus 로고
    • Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export
    • DOI 10.1038/nature06449, PII NATURE06449
    • Minamino, T. & Namba, K. Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export. Nature. 451, 485-488 (2008) (Pubitemid 351158881)
    • (2008) Nature , vol.451 , Issue.7177 , pp. 485-488
    • Minamino, T.1    Namba, K.2
  • 25
    • 80053415915 scopus 로고    scopus 로고
    • An energy transduction mechanism used in bacterial flagellar type III protein export
    • Minamino, T., Morimoto, Y. V., Hara, N. & Namba, K. An energy transduction mechanism used in bacterial flagellar type III protein export. Nat. Commun. 2, 475 (2011)
    • (2011) Nat. Commun , vol.2 , pp. 475
    • Minamino, T.1    Morimoto, Y.V.2    Hara, N.3    Namba, K.4
  • 26
    • 84873051807 scopus 로고    scopus 로고
    • Interaction between FliJ and FlhA, components of the bacterial flagellar type III export apparatus
    • Ibuki, T. et al. Interaction between FliJ and FlhA, components of the bacterial flagellar type III export apparatus. J. Bacteriol. 195, 466-473 (2013)
    • (2013) J. Bacteriol , vol.195 , pp. 466-473
    • Ibuki, T.1
  • 27
    • 84868305790 scopus 로고    scopus 로고
    • Interaction of the extreme N-terminal region of FliH with FlhA is required for efficient bacterial flagellar protein export
    • Hara, N.,Morimoto, Y. V., Kawamoto, A.,Namba, K. &Minamino, T. Interaction of the extreme N-terminal region of FliH with FlhA is required for efficient bacterial flagellar protein export. J. Bacteriol. 194, 5353-5360 (2012)
    • (2012) J. Bacteriol , vol.194 , pp. 5353-5360
    • Hara, N.1    Morimoto, Y.V.2    Kawamoto, A.3    Namba, K.4    Minamino, T.5
  • 28
    • 79952359941 scopus 로고    scopus 로고
    • Common architecture of the flagellar type III protein export apparatus and F-and V-type ATPases
    • Ibuki, T. et al. Common architecture of the flagellar type III protein export apparatus and F-and V-type ATPases. Nat. Struct. Mol. Biol. 18, 277-282 (2011)
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 277-282
    • Ibuki, T.1
  • 29
    • 33745927123 scopus 로고    scopus 로고
    • Sigma28-dependent transcription in Salmonella enterica is independent of flagellar shearing
    • Rosu, V. & Hughes, K. T. sigma28-dependent transcription in Salmonella enterica is independent of flagellar shearing. J. Bacteriol. 188, 5196 (2006)
    • (2006) J. Bacteriol , vol.188 , pp. 5196
    • Rosu, V.1    Hughes, K.T.2
  • 30
    • 0022454124 scopus 로고
    • Subdivision of flagellar genes of Salmonella typhimurium into regions responsible for assembly, rotation, and switching
    • Yamaguchi, S., Fujita, H., Ishihara, A., Aizawa, S. &Macnab, R.M. Subdivision of flagellar genes of Salmonella typhimurium into regions responsible for assembly, rotation, and switching. J. Bacteriol. 166, 187-193 (1986) (Pubitemid 16043299)
    • (1986) Journal of Bacteriology , vol.166 , Issue.1 , pp. 187-193
    • Yamaguchi, S.1    Fujita, H.2    Ishihara, A.3
  • 31
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., Belin, D., Carson, M. J. & Beckwith, J. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177, 4121-4130 (1995)
    • (1995) J. Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 32
    • 84863229607 scopus 로고    scopus 로고
    • Bacterial chemoreceptor arrays are hexagonally packed trimmers of receptor dimers networked by rings of kinase and coupling proteins
    • Briegel, A. et al. Bacterial chemoreceptor arrays are hexagonally packed trimmers of receptor dimers networked by rings of kinase and coupling proteins. Proc Natl Acad Sci USA. 109, 3766-3771 (2012)
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 3766-3771
    • Briegel, A.1
  • 33
    • 78649598805 scopus 로고    scopus 로고
    • Charged residues in the cytoplasmic loop of MotA are required for stator assembly into the bacterial flagellar motor
    • Morimoto, V. Y., Nakamura, S., Kami-ike, N., Namba, K. & Minamino, T. Charged residues in the cytoplasmic loop of MotA are required for stator assembly into the bacterial flagellar motor. Mol. Microbiol. 78, 1117-1129 (2010)
    • (2010) Mol. Microbiol , vol.78 , pp. 1117-1129
    • Morimoto, V.Y.1    Nakamura, S.2    Kami-Ike, N.3    Namba, K.4    Minamino, T.5
  • 34
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • DOI 10.1006/jsbi.1996.0013
    • Kremer, J. R., Mastronarde, D. N. & McIntosh, J. R. Computer visualization of three-dimensional image data using IMOD. J. Struct Biol. 116, 71-76 (1996) (Pubitemid 26093126)
    • (1996) Journal of Structural Biology , vol.116 , Issue.1 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 35
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • DOI 10.1006/jsbi.1999.4174
    • Ludtke, S. J., Baldwin, P. R. & Chiu, W. EMAN: semiautomated software for highresolution single particle reconstructions. J. Struct. Biol. 128, 82-97 (1999) (Pubitemid 30013436)
    • (1999) Journal of Structural Biology , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 37
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera -A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera -a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004)
    • (2004) J. Comput. Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 38
    • 0021362454 scopus 로고
    • Hook-associated proteins essential for flagellar filament formation in Salmonella typhimurium
    • Homma, M., Kutsukake, K., Iino, T. & Yamaguchi, S. Hook-associated proteins essential for flagellar filament formation in Salmonella typhimurium. J. Bacteriol. 157, 100108 (1984)
    • (1984) J. Bacteriol , vol.157 , pp. 100108
    • Homma, M.1    Kutsukake, K.2    Iino, T.3    Yamaguchi, S.4
  • 40
    • 0028274712 scopus 로고
    • Isolation, characterization and structure of bacterial flagellar motors containing the switch complex
    • DOI 10.1006/jmbi.1994.1079
    • Francis, N. R., Sosinsky, G. E., Thomas, D. & DeRosier, D. J. Isolation, characterization and structure of bacterial flagellar motors containing the switch complex. J. Mol. Biol. 235, 1261-1270 (1994) (Pubitemid 24148928)
    • (1994) Journal of Molecular Biology , vol.235 , Issue.4 , pp. 1261-1270
    • Francis, N.R.1    Sosinsky, G.E.2    Thomas, D.3    DeRosier, D.J.4
  • 41
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • DOI 10.1016/S1047-8477(03)00069-8
    • Mindell, J. A. & Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003) (Pubitemid 36638267)
    • (2003) Journal of Structural Biology , vol.142 , Issue.3 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2


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