메뉴 건너뛰기




Volumn 91, Issue 6, 2014, Pages 1214-1226

Assembly and stoichiometry of FliF and FlhA in Salmonella flagellar basal body

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYAN FLUORESCENT PROTEIN; FLICE INHIBITORY PROTEIN; PROTEIN FLHA; PROTEIN FLHB; PROTEIN FLIF; PROTEIN FLIM; PROTEIN FLIN; PROTEIN FLIO; PROTEIN FLIQ; PROTEIN FLIR; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN;

EID: 84896702974     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12529     Document Type: Article
Times cited : (78)

References (53)
  • 2
    • 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., Kümmerer, 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    Kümmerer, N.2    Engel, C.3    Bozkurt, G.4    Wild, K.5    Sinning, I.6
  • 3
    • 84865596112 scopus 로고    scopus 로고
    • Cross-complementation study of the flagellar type III export apparatus membrane protein FlhB
    • Barker, C.S., and Samatey, F.A. (2012) Cross-complementation study of the flagellar type III export apparatus membrane protein FlhB. PLoS ONE 7: e44030.
    • (2012) PLoS ONE , vol.7
    • Barker, C.S.1    Samatey, F.A.2
  • 4
    • 78049427928 scopus 로고    scopus 로고
    • FliO regulation of FliP in the formation of the Salmonella enterica flagellum
    • Barker, C.S., Meshcheryakova, I.V., Kostyukova, A.S., and Samatey, F.A. (2010) FliO regulation of FliP in the formation of the Salmonella enterica flagellum. PLoS Genet 6: e1001143.
    • (2010) PLoS Genet , vol.6
    • Barker, C.S.1    Meshcheryakova, I.V.2    Kostyukova, A.S.3    Samatey, F.A.4
  • 6
    • 43849098574 scopus 로고    scopus 로고
    • Coordinating assembly of a bacterial macromolecular machine
    • Chevance, F.F., and Hughes, K.T. (2008) Coordinating assembly of a bacterial macromolecular machine. Nat Rev Microbiol 6: 455-465.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 455-465
    • Chevance, F.F.1    Hughes, K.T.2
  • 7
    • 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
  • 8
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 9
    • 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
  • 10
    • 0030701512 scopus 로고    scopus 로고
    • The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal body
    • Fan, F., Ohnishi, K., Francis, N.R., and Macnab, R.M. (1997) The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal body. Mol Microbiol 82: 1035-1046.
    • (1997) Mol Microbiol , vol.82 , pp. 1035-1046
    • Fan, F.1    Ohnishi, K.2    Francis, N.R.3    Macnab, R.M.4
  • 11
    • 0026740392 scopus 로고
    • Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-ring face of the basal body
    • Francis, N.R., Irikura, V.M., Yamaguchi, S., DeRosier, D.J., and Macnab, R.M. (1992) Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-ring face of the basal body. Proc Natl Acad Sci USA 89: 6304-6308.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6304-6308
    • Francis, N.R.1    Irikura, V.M.2    Yamaguchi, S.3    DeRosier, D.J.4    Macnab, R.M.5
  • 12
    • 0028274712 scopus 로고
    • Isolation, characterization, and structure of bacterial flagellar motors containing the switch complex
    • Francis, N.R., Sosinsky, G.E., Thomas, D., and DeRosier, D.J. (1994) Isolation, characterization, and structure of bacterial flagellar motors containing the switch complex. J Mol Biol 235: 1261-1270.
    • (1994) J Mol Biol , vol.235 , pp. 1261-1270
    • Francis, N.R.1    Sosinsky, G.E.2    Thomas, D.3    DeRosier, D.J.4
  • 13
    • 0038016732 scopus 로고    scopus 로고
    • Substrate specificity of type III flagellar protein export in Salmonella is controlled by subdomain interactions in FlhB
    • Fraser, G.M., Hirano, T., Ferris, H.U., Devgan, L.L., Kihara, M., and Macnab, R.M. (2003) Substrate specificity of type III flagellar protein export in Salmonella is controlled by subdomain interactions in FlhB. Mol Microbiol 48: 1043-1057.
    • (2003) Mol Microbiol , vol.48 , pp. 1043-1057
    • Fraser, G.M.1    Hirano, T.2    Ferris, H.U.3    Devgan, L.L.4    Kihara, M.5    Macnab, R.M.6
  • 14
    • 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., and Namba, K. (2006) Interactions between C ring proteins and export apparatus components: a possible mechanism for facilitating type III protein export. Mol Microbiol 60: 984-998.
    • (2006) Mol Microbiol , vol.60 , pp. 984-998
    • González-Pedrajo, B.1    Minamino, T.2    Kihara, M.3    Namba, K.4
  • 15
    • 79960463317 scopus 로고    scopus 로고
    • Genetic characterization of conserved charged residues in the bacterial flagellar type III export protein FlhA
    • Hara, N., Namba, K., and Minamino, T. (2011) Genetic characterization of conserved charged residues in the bacterial flagellar type III export protein FlhA. PLoS ONE 6: e22417.
    • (2011) PLoS ONE , vol.6
    • Hara, N.1    Namba, K.2    Minamino, T.3
  • 16
    • 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., and Minamino, T. (2012) 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) J Bacteriol , vol.194 , pp. 5353-5360
    • Hara, N.1    Morimoto, Y.V.2    Kawamoto, A.3    Namba, K.4    Minamino, T.5
  • 17
    • 79952359941 scopus 로고    scopus 로고
    • Common architecture between the flagellar protein export apparatus and F- and V-ATPases
    • Ibuki, T., Imada, K., Minamino, T., Kato, T., Miyata, T., and Namba, K. (2011) Common architecture between the flagellar protein export apparatus and F- and V-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
  • 18
    • 84873051807 scopus 로고    scopus 로고
    • Interaction between FliJ and FlhA, components of the bacterial flagellar type III export apparatus
    • Ibuki, T., Uchida, Y., Hironaka, Y., Namba, K., Imada, K., and Minamino, T. (2013) Interaction between FliJ and FlhA, components of the bacterial flagellar type III export apparatus. J Bacteriol 195: 466-473.
    • (2013) J Bacteriol , vol.195 , pp. 466-473
    • Ibuki, T.1    Uchida, Y.2    Hironaka, Y.3    Namba, K.4    Imada, K.5    Minamino, T.6
  • 19
    • 0025248415 scopus 로고
    • Flagellar assembly in Salmonella typhimurium: analysis with temperature-sensitive mutants
    • Jones, C.J., and Macnab, R.M. (1990) Flagellar assembly in Salmonella typhimurium: analysis with temperature-sensitive mutants. J Bacteriol 172: 3022-3028.
    • (1990) J Bacteriol , vol.172 , pp. 3022-3028
    • Jones, C.J.1    Macnab, R.M.2
  • 20
    • 84889777894 scopus 로고    scopus 로고
    • Common and distinct structural features of Salmonella injectisome and flagellar basal body
    • doi:10.1038/srep03369
    • Kawamoto, A., Morimoto, Y.V., Miyata, T., Minamino, T., Hughes, K.T., Kato, T., and Namba, K. (2013) Common and distinct structural features of Salmonella injectisome and flagellar basal body. Sci Rep 3: 3369. doi:10.1038/srep03369
    • (2013) Sci Rep , vol.3 , pp. 3369
    • Kawamoto, A.1    Morimoto, Y.V.2    Miyata, T.3    Minamino, T.4    Hughes, K.T.5    Kato, T.6    Namba, K.7
  • 21
    • 0034079196 scopus 로고    scopus 로고
    • Deletion analysis of the flagellar switch protein FliG of Salmonella
    • Kihara, M., Miller, G.U., and Macnab, R.M. (2000) Deletion analysis of the flagellar switch protein FliG of Salmonella. J Bacteriol 182: 1655-1662.
    • (2000) J Bacteriol , vol.182 , pp. 1655-1662
    • Kihara, M.1    Miller, G.U.2    Macnab, R.M.3
  • 22
    • 0035110827 scopus 로고    scopus 로고
    • Intergenic suppression between the flagellar MS ring protein FliF of Salmonella and FlhA, a membrane component of its export apparatus
    • Kihara, M., Minamino, T., Yamaguchi, S., and Macnab, R.M. (2001) Intergenic suppression between the flagellar MS ring protein FliF of Salmonella and FlhA, a membrane component of its export apparatus. J Bacteriol 183: 1655-1662.
    • (2001) J Bacteriol , vol.183 , pp. 1655-1662
    • Kihara, M.1    Minamino, T.2    Yamaguchi, S.3    Macnab, R.M.4
  • 23
    • 84890123592 scopus 로고    scopus 로고
    • Interactions of bacterial chaperone-substrate complexes with FlhA contribute to co-ordinating assembly of the flagellar filament
    • Kinoshita, M., Hara, N., Imada, K., Namba, K., and Minamino, T. (2013) Interactions of bacterial chaperone-substrate complexes with FlhA contribute to co-ordinating assembly of the flagellar filament. Mol Microbiol 90: 1249-1261.
    • (2013) Mol Microbiol , vol.90 , pp. 1249-1261
    • Kinoshita, M.1    Hara, N.2    Imada, K.3    Namba, K.4    Minamino, T.5
  • 24
    • 0026752989 scopus 로고
    • Morphological pathway of flagellar assembly in Salmonella typhimurium
    • Kubori, T., Shimamoto, N., Yamaguchi, S., Namba, K., and Aizwa, S. (1992) Morphological pathway of flagellar assembly in Salmonella typhimurium. J Mol Biol 226: 433-446.
    • (1992) J Mol Biol , vol.226 , pp. 433-446
    • Kubori, T.1    Shimamoto, N.2    Yamaguchi, S.3    Namba, K.4    Aizwa, S.5
  • 25
    • 0031023773 scopus 로고    scopus 로고
    • Assembly of the switch complex onto the MS ring complex of Salmonella typhimurium does not require any other flagellar proteins
    • Kubori, T., Yamaguchi, S., and Aizwa, S. (1997) Assembly of the switch complex onto the MS ring complex of Salmonella typhimurium 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    Aizwa, S.3
  • 26
    • 0025019775 scopus 로고
    • Transcriptional analysis of the flagellar regulon of Salmonella typhimurium
    • Kutsukake, K., Ohya, Y., and Iino, T. (1990) Transcriptional analysis of the flagellar regulon of Salmonella typhimurium. J Bacteriol 172: 741-747.
    • (1990) J Bacteriol , vol.172 , pp. 741-747
    • Kutsukake, K.1    Ohya, Y.2    Iino, T.3
  • 27
    • 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
  • 28
    • 7744223028 scopus 로고    scopus 로고
    • Analysis of the cytoplasmic domain of Salmonella FlhA and interactions with components of the flagellar export machinery
    • McMurry, J.L., Van Arnam, J.S., Kihara, M., and Macnab, R.M. (2004) Analysis of the cytoplasmic domain of Salmonella FlhA and interactions with components of the flagellar export machinery. J Bacteriol 186: 7586-7592.
    • (2004) J Bacteriol , vol.186 , pp. 7586-7592
    • McMurry, J.L.1    Van Arnam, J.S.2    Kihara, M.3    Macnab, R.M.4
  • 29
    • 84902327129 scopus 로고    scopus 로고
    • Protein export through the bacterial flagellar type III export pathway
    • pii: S0167-4889(13)00327-3, doi:10.1016/j.bbamcr.2013.09.005
    • Minamino, T. (2013) Protein export through the bacterial flagellar type III export pathway. Biochim Biophys Acta pii: S0167-4889(13)00327-3, doi:10.1016/j.bbamcr.2013.09.005
    • (2013) Biochim Biophys Acta
    • Minamino, T.1
  • 30
    • 0033059596 scopus 로고    scopus 로고
    • Components of the Salmonella flagellar export apparatus and classification of export substrates
    • Minamino, T., and Macnab, R.M. (1999) Components of the Salmonella flagellar export apparatus and classification of export substrates. J Bacteriol 181: 1388-1394.
    • (1999) J Bacteriol , vol.181 , pp. 1388-1394
    • Minamino, T.1    Macnab, R.M.2
  • 31
    • 0034011357 scopus 로고    scopus 로고
    • Interactions among components of the Salmonella flagellar export apparatus and its substrates
    • Minamino, T., and Macnab, R.M. (2000a) 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
  • 32
    • 0033779545 scopus 로고    scopus 로고
    • FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity
    • Minamino, T., and Macnab, R.M. (2000b) FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity. Mol Microbiol 37: 1494-1503.
    • (2000) Mol Microbiol , vol.37 , pp. 1494-1503
    • Minamino, T.1    Macnab, R.M.2
  • 33
    • 38549158887 scopus 로고    scopus 로고
    • Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export
    • Minamino, T., and Namba, K. (2008) Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export. Nature 451: 485-488.
    • (2008) Nature , vol.451 , pp. 485-488
    • Minamino, T.1    Namba, K.2
  • 34
    • 0037701404 scopus 로고    scopus 로고
    • The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator FliH
    • Minamino, T., González-Pedrajo, B., Kihara, M., Namba, K., and Macnab, R.M. (2003) The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator FliH. J Bacteriol 185: 3983-3988.
    • (2003) J Bacteriol , vol.185 , pp. 3983-3988
    • Minamino, T.1    González-Pedrajo, B.2    Kihara, M.3    Namba, K.4    Macnab, R.M.5
  • 35
    • 58149347646 scopus 로고    scopus 로고
    • Mechanisms of type III protein export for bacterial flagellar assembly
    • Minamino, T., Imada, K., and Namba, K. (2008a) Mechanisms of type III protein export for bacterial flagellar assembly. Mol Biosyst 4: 1105-1115.
    • (2008) Mol Biosyst , vol.4 , pp. 1105-1115
    • Minamino, T.1    Imada, K.2    Namba, K.3
  • 36
    • 57049169137 scopus 로고    scopus 로고
    • Molecular motors of the bacterial flagella
    • Minamino, T., Imada, K., and Namba, K. (2008b) Molecular motors of the bacterial flagella. Curr Opin Struct Biol 18: 693-701.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 693-701
    • Minamino, T.1    Imada, K.2    Namba, K.3
  • 37
    • 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., Yoshimura, S.D.J., Morimoto, Y.V., González-Pedrajo, B., Kami-ike, N., and Namba, K. (2009) 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) Mol Microbiol , vol.74 , pp. 1471-1483
    • Minamino, T.1    Yoshimura, S.D.J.2    Morimoto, Y.V.3    González-Pedrajo, B.4    Kami-ike, N.5    Namba, K.6
  • 38
    • 77949662091 scopus 로고    scopus 로고
    • Role of the C-terminal cytoplasmic domain of FlhA in bacterial flagellar type III protein export
    • Minamino, T., Shimada, M., Okabe, M., Saijo-Hamano, Y., Imada, K., Kihara, M., and Namba, K. (2010) Role of the C-terminal cytoplasmic domain of FlhA in bacterial flagellar type III protein export. J Bacteriol 192: 1929-1936.
    • (2010) J Bacteriol , vol.192 , pp. 1929-1936
    • Minamino, T.1    Shimada, M.2    Okabe, M.3    Saijo-Hamano, Y.4    Imada, K.5    Kihara, M.6    Namba, K.7
  • 39
    • 80053415915 scopus 로고    scopus 로고
    • An energy transduction mechanism used in bacterial type III protein export
    • Minamino, T., Morimoto, Y.V., Hara, N., and Namba, K. (2011) An energy transduction mechanism used in bacterial type III protein export. Nat Commun 2: 475.
    • (2011) Nat Commun , vol.2 , pp. 475
    • Minamino, T.1    Morimoto, Y.V.2    Hara, N.3    Namba, K.4
  • 40
    • 84856560992 scopus 로고    scopus 로고
    • Interaction of a bacterial flagellar chaperone FlgN with FlhA is required for efficient export of its cognate substrates
    • Minamino, T., Kinoshita, M., Hara, N., Takeuchi, S., Hida, A., Koya, S., etal. (2012) Interaction of a bacterial flagellar chaperone FlgN with FlhA is required for efficient export of its cognate substrates. Mol Microbiol 83: 775-788.
    • (2012) Mol Microbiol , vol.83 , pp. 775-788
    • Minamino, T.1    Kinoshita, M.2    Hara, N.3    Takeuchi, S.4    Hida, A.5    Koya, S.6
  • 41
    • 84873045159 scopus 로고    scopus 로고
    • Distinct roles of highly conserved charged residues at the MotA-FliG interface in bacterial flagellar motor rotation
    • Morimoto, Y.V., Nakamura, S., Hiraoka, K.D., Namba, K., and Minamino, T. (2013) Distinct roles of highly conserved charged residues at the MotA-FliG interface in bacterial flagellar motor rotation. J Bacteriol 195: 474-481.
    • (2013) J Bacteriol , vol.195 , pp. 474-481
    • Morimoto, Y.V.1    Nakamura, S.2    Hiraoka, K.D.3    Namba, K.4    Minamino, T.5
  • 42
    • 78049309085 scopus 로고    scopus 로고
    • Evidence for symmetry in the elementary process of bidirectional torque generation by the bacterial flagellar motor
    • Nakamura, S., Kami-ike, N., Yokota, J.P., Minamino, T., and Namba, K. (2010) Evidence for symmetry in the elementary process of bidirectional torque generation by the bacterial flagellar motor. Proc Natl Acad Sci USA 107: 17616-17620.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 17616-17620
    • Nakamura, S.1    Kami-ike, N.2    Yokota, J.P.3    Minamino, T.4    Namba, K.5
  • 43
    • 0028329280 scopus 로고
    • FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium
    • Ohnishi, K., Ohto, Y., Aizawa, S.-I., Macnab, R.M., and Iino, T. (1994) FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium. J Bacteriol 176: 2272-2281.
    • (1994) J Bacteriol , vol.176 , pp. 2272-2281
    • Ohnishi, K.1    Ohto, Y.2    Aizawa, S.-I.3    Macnab, R.M.4    Iino, T.5
  • 44
    • 0028340515 scopus 로고
    • Overproduction of the bacterial flagellar switch proteins and their interactions with the MS ring complex in vitro
    • Oosawa, K., Ueno, T., and Azawa, S. (1994) Overproduction of the bacterial flagellar switch proteins and their interactions with the MS ring complex in vitro. J Bacteriol 176: 3638-3691.
    • (1994) J Bacteriol , vol.176 , pp. 3638-3691
    • Oosawa, K.1    Ueno, T.2    Azawa, S.3
  • 45
    • 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
  • 46
    • 4644346442 scopus 로고    scopus 로고
    • Structural and functional analysis of the C-terminal cytoplasmic domain of FlhA, an integral membrane component of the type III flagellar protein export apparatus in Salmonella
    • Saijo-Hamano, Y., Minamino, T., Macnab, R.M., and Namba, K. (2004) Structural and functional analysis of the C-terminal cytoplasmic domain of FlhA, an integral membrane component of the type III flagellar protein export apparatus in Salmonella. J Mol Biol 343: 457-466.
    • (2004) J Mol Biol , vol.343 , pp. 457-466
    • Saijo-Hamano, Y.1    Minamino, T.2    Macnab, R.M.3    Namba, K.4
  • 47
    • 77950244006 scopus 로고    scopus 로고
    • Structure of the cytoplasmic domain of FlhA and implication for flagellar type III protein export
    • Saijo-Hamano, Y., Imada, K., Minamino, T., Kihara, M., Shimada, M., Kitao, A., and Namba, K. (2010) Structure of the cytoplasmic domain of FlhA and implication for flagellar type III protein export. Mol Microbiol 76: 260-268.
    • (2010) Mol Microbiol , vol.76 , pp. 260-268
    • Saijo-Hamano, Y.1    Imada, K.2    Minamino, T.3    Kihara, M.4    Shimada, M.5    Kitao, A.6    Namba, K.7
  • 48
    • 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., Yonekura, K., and Namba, K. (2004) 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) J Mol Biol , vol.337 , pp. 105-113
    • Suzuki, H.1    Yonekura, K.2    Namba, K.3
  • 49
    • 0026792838 scopus 로고
    • M ring, S ring and proximal rod of the flagellar basal body of Salmonella typhimurium are composed of subunits of a single protein, FliF
    • Ueno, T., Oosawa, K., and Aizawa, S. (1992) M ring, S ring and proximal rod of the flagellar basal body of Salmonella typhimurium are composed of subunits of a single protein, FliF. J Mol Biol 227: 672-677.
    • (1992) J Mol Biol , vol.227 , pp. 672-677
    • Ueno, T.1    Oosawa, K.2    Aizawa, S.3
  • 50
    • 1842454268 scopus 로고    scopus 로고
    • Analysis of an engineered Salmonella flagellar fusion protein, FliR-FlhB
    • Van Arnam, J.S., McMurry, J.L., Kihara, M., and Macnab, R.M. (2004) Analysis of an engineered Salmonella flagellar fusion protein, FliR-FlhB. J Bacteriol 186: 2495-2498.
    • (2004) J Bacteriol , vol.186 , pp. 2495-2498
    • Van Arnam, J.S.1    McMurry, J.L.2    Kihara, M.3    Macnab, R.M.4
  • 52
    • 0021347115 scopus 로고
    • Genetic analysis of H2, the structural gene for phase-2 flagellin in Salmonella
    • Yamaguchi, S., Fujita, H., Sugata, K., Taira, T., and Iino, T. (1984) Genetic analysis of H2, the structural gene for phase-2 flagellin in Salmonella. J Gen Microbiol 130: 255-265.
    • (1984) J Gen Microbiol , vol.130 , pp. 255-265
    • Yamaguchi, S.1    Fujita, H.2    Sugata, K.3    Taira, T.4    Iino, T.5
  • 53
    • 0022899744 scopus 로고
    • Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium
    • Yamaguchi, S., Aizawa, S.-I., Kihara, M., Isomura, M., Jones, C.J., and Macnab, R.M. (1986) Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium. J Bacteriol 168: 1172-1179.
    • (1986) J Bacteriol , vol.168 , pp. 1172-1179
    • Yamaguchi, S.1    Aizawa, S.-I.2    Kihara, M.3    Isomura, M.4    Jones, C.J.5    Macnab, R.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.