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Volumn 4, Issue , 2014, Pages

Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; FLII PROTEIN, BACTERIA; PHOTOPROTEIN; PROTEIN BINDING; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; YELLOW FLUORESCENT PROTEIN, BACTERIA;

EID: 84923284551     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep06528     Document Type: Article
Times cited : (66)

References (49)
  • 1
    • 43849098574 scopus 로고    scopus 로고
    • Coordinating assembly of a bacterial macromolecular machine
    • Chevance, F. F. & Hughes, K. T. Coordinating assembly of a bacterial macromolecular machine. Nat. Rev. Microbiol. 6, 455-465 (2008).
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 455-465
    • Chevance, F.F.1    Hughes, K.T.2
  • 2
    • 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
  • 3
    • 84902327129 scopus 로고    scopus 로고
    • Protein export through the bacterial flagellar type III export pathway
    • Minamino, T. Protein export through the bacterial flagellar type III export pathway. Biochim. Biophys. Acta. 1843, 1642-1648 (2014).
    • (2014) Biochim. Biophys. Acta. , vol.1843 , pp. 1642-1648
    • Minamino, T.1
  • 4
    • 0028274712 scopus 로고
    • Isolation, characterization, and structure of bacterial flagellar motors containing the switch complex
    • 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).
    • (1994) J. Mol. Biol. , vol.235 , pp. 1261-1270
    • Francis, N.R.1    Sosinsky, G.E.2    Thomas, D.3    DeRosier, D.J.4
  • 5
    • 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. Microbiol. 60, 984-998 (2006).
    • (2006) Mol. Microbiol. , vol.60 , pp. 984-998
    • González-Pedrajo, B.1    Minamino, T.2    Kihara, M.3    Namba, K.4
  • 6
    • 33750110911 scopus 로고    scopus 로고
    • The type III secretion injectisome
    • Cornelis, G. R. The type III secretion injectisome. Nat. Rev. Microbiol. 4, 811-825 (2006).
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 811-825
    • Cornelis, G.R.1
  • 7
    • 0034011357 scopus 로고    scopus 로고
    • Interactions among components of the Salmonella flagellar export apparatus and its substrates
    • Minamino, T. & Macnab, R. M. Interactions among components of the Salmonella flagellar export apparatus and its substrates. Mol. Microbiol. 35, 1052-1064 (2000).
    • (2000) Mol. Microbiol. , vol.35 , pp. 1052-1064
    • Minamino, T.1    Macnab, R.M.2
  • 8
    • 77949662091 scopus 로고    scopus 로고
    • Role of the C-terminal cytoplasmic domain of FlhA in bacterial flagellar type III protein export
    • Minamino, T. et al. Role of the C-terminal cytoplasmic domain of FlhA in bacterial flagellar type III protein export. J. Bacteriol. 192, 1929-1936 (2010).
    • (2010) J. Bacteriol. , vol.192 , pp. 1929-1936
    • Minamino, T.1
  • 9
    • 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. et al. Interaction of a bacterial flagellar chaperone FlgN with FlhA is required for efficient export of its cognate substrates. Mol. Microbiol. 83, 775-788 (2012).
    • (2012) Mol. Microbiol. , vol.83 , pp. 775-788
    • Minamino, T.1
  • 10
    • 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. et al. 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).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 11295-11300
    • Bange, G.1
  • 11
    • 84890123592 scopus 로고    scopus 로고
    • Interactions of bacterial chaperone-substrate complexes with FlhA contribute to coordinating assembly of the flagellar filament
    • Kinoshita, M., Hara, N., Imada, K., Namba, K. & Minamino, T. Interactions of bacterial chaperone-substrate complexes with FlhA contribute to coordinating assembly of the flagellar filament. Mo.l Microbiol. 90, 1249-1261 (2013).
    • (2013) Mo.L Microbiol. , vol.90 , pp. 1249-1261
    • Kinoshita, M.1    Hara, N.2    Imada, K.3    Namba, K.4    Minamino, T.5
  • 12
    • 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 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 99-104
    • Abrusci, P.1
  • 13
    • 84889777894 scopus 로고    scopus 로고
    • Common and distinct structural features of Salmonella injectisome and flagellar basal body
    • Kawamoto, A. et al. Common and distinct structural features of Salmonella injectisome and flagellar basal body. Sci. Rep. 3, 3369 (2013).
    • (2013) Sci. Rep. , vol.3 , pp. 3369
    • Kawamoto, A.1
  • 14
    • 84896702974 scopus 로고    scopus 로고
    • Assembly and stoichiometry of FliF and FlhA in Salmonella flagellar basal body
    • Morimoto, Y. V. et al. Assembly and stoichiometry of FliF and FlhA in Salmonella flagellar basal body. Mol. Microbiol. 91, 1214-1226 (2014).
    • (2014) Mol. Microbiol. , vol.91 , pp. 1214-1226
    • Morimoto, Y.V.1
  • 15
    • 38549158887 scopus 로고    scopus 로고
    • Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export
    • Minamino, T. & Namba, K. Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export. Nature 451, 485-488 (2008).
    • (2008) Nature , vol.451 , pp. 485-488
    • Minamino, T.1    Namba, K.2
  • 16
    • 38549088345 scopus 로고    scopus 로고
    • Energy source of the flagellar type III secretion
    • Paul, K., Erhardt, M., Hirano, T., Blair, D. F. & Hughes, K. T. Energy source of the flagellar type III secretion. Nature 451, 489-492 (2008).
    • (2008) Nature , vol.451 , pp. 489-492
    • Paul, K.1    Erhardt, M.2    Hirano, T.3    Blair, D.F.4    Hughes, K.T.5
  • 17
    • 0029730706 scopus 로고    scopus 로고
    • Enzymatic characterization of FliI: An ATPase involved in flagellar assembly in Salmonella typhimurium
    • Fan, F. & Macnab, R. M. Enzymatic characterization of FliI: an ATPase involved in flagellar assembly in Salmonella typhimurium. J. Biol. Chem. 271, 31981-31988 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 31981-31988
    • Fan, F.1    Macnab, R.M.2
  • 18
    • 0038460046 scopus 로고    scopus 로고
    • Oligomerisation and activation of the FliI ATPase central to the bacterial flagellum assembly
    • Claret, L., Susannah, C. R., Higgins, M. & Huges, C. Oligomerisation and activation of the FliI ATPase central to the bacterial flagellum assembly. Mol. Microbiol. 48, 1349-1355 (2003).
    • (2003) Mol. Microbiol. , vol.48 , pp. 1349-1355
    • Claret, L.1    Susannah, C.R.2    Higgins, M.3    Huges, C.4
  • 19
    • 79952359941 scopus 로고    scopus 로고
    • Common architecture between the flagellar protein export apparatus and F- and V-ATPases
    • Ibuki, T. et al. Common architecture between the flagellar protein export apparatus and F- and V-ATPases. Nat. Struct. Mol. Biol. 18, 277-282 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 277-282
    • Ibuki, T.1
  • 20
    • 33846314672 scopus 로고    scopus 로고
    • Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits
    • Imada, K., Minamino, T., Tahara, A. & Namba, K. Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits. Proc. Natl. Acad. Sci. USA 104, 485-490 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 485-490
    • Imada, K.1    Minamino, T.2    Tahara, A.3    Namba, K.4
  • 21
    • 84878377906 scopus 로고    scopus 로고
    • Common evolutionary origin for the rotor domain of rotary ATPases and flagellar protein export apparatus
    • Kishikawa, J. et al. Common evolutionary origin for the rotor domain of rotary ATPases and flagellar protein export apparatus. PLoS One. 8, e64695 (2013).
    • (2013) PLoS One. , vol.8 , pp. e64695
    • Kishikawa, J.1
  • 22
    • 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. & Macnab, R. M. 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).
    • (2000) Mol. Microbiol. , vol.37 , pp. 1494-1503
    • Minamino, T.1    Macnab, R.M.2
  • 23
    • 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. & Beatson, S. A. 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).
    • (2006) Protein Sci. , vol.15 , pp. 935-941
    • Pallen, M.J.1    Bailey, C.M.2    Beatson, S.A.3
  • 24
    • 1642305413 scopus 로고    scopus 로고
    • Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export
    • Thomas, J., Stafford, G. P. & Hughes, C. Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export. Proc. Natl. Acad. Sci. USA 101, 3945-3950 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3945-3950
    • Thomas, J.1    Stafford, G.P.2    Hughes, C.3
  • 25
    • 84155162801 scopus 로고    scopus 로고
    • Interaction between FliI ATPase and a flagellar chaperone FliT during bacterial flagellar protein export
    • Minamino, T., Kinoshita, M., Imada, K. & Namba, K. Interaction between FliI ATPase and a flagellar chaperone FliT during bacterial flagellar protein export. Mol. Microbiol. 83, 168-178 (2012).
    • (2012) Mol. Microbiol. , vol.83 , pp. 168-178
    • Minamino, T.1    Kinoshita, M.2    Imada, K.3    Namba, K.4
  • 26
    • 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
  • 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
    • 80053415915 scopus 로고    scopus 로고
    • An energy transduction mechanism used in bacterial type III protein export
    • Minamino, T., Morimoto, Y. V., Hara, N. & Namba, K. An energy transduction mechanism used in bacterial 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
  • 29
    • 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
  • 31
    • 79955733488 scopus 로고    scopus 로고
    • Assembly and stability of flagellar motor in Escherichia coli
    • Li, H. & Sourjik, V. Assembly and stability of flagellar motor in Escherichia coli. Mol. Microbiol. 80, 886-899 (2011).
    • (2011) Mol. Microbiol. , vol.80 , pp. 886-899
    • Li, H.1    Sourjik, V.2
  • 32
    • 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. & Macnab, R. M. 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).
    • (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
  • 33
    • 33749330451 scopus 로고    scopus 로고
    • The FliN-FliH interaction mediates localization of flagellar export ATPase FliI to the C ring complex
    • McMurry, J. L., Murphy, J. W. & González-Pedrajo, B. The FliN-FliH interaction mediates localization of flagellar export ATPase FliI to the C ring complex. Biochemistry 45, 11790-11798 (2006).
    • (2006) Biochemistry , vol.45 , pp. 11790-11798
    • McMurry, J.L.1    Murphy, J.W.2    González-Pedrajo, B.3
  • 34
    • 55749095038 scopus 로고    scopus 로고
    • Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging
    • Leake, M. C. et al. Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging. Proc. Natl. Acad. Sci. USA 105, 15376-15381 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15376-15381
    • Leake, M.C.1
  • 35
    • 33748926752 scopus 로고    scopus 로고
    • Stoichiometry and turnover in single, functioning membrane protein complexes
    • Leake, M. C. et al. Stoichiometry and turnover in single, functioning membrane protein complexes. Nature 443, 355-358 (2006).
    • (2006) Nature , vol.443 , pp. 355-358
    • Leake, M.C.1
  • 36
    • 77954921897 scopus 로고    scopus 로고
    • Signal-dependent turnover of the bacterial flagellar switch protein FliM
    • Delalez, N. J. et al. Signal-dependent turnover of the bacterial flagellar switch protein FliM. Proc. Natl. Acad. Sci. USA 107, 11347-11351 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 11347-11351
    • Delalez, N.J.1
  • 37
    • 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. & 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).
    • (2004) J. Mol. Biol. , vol.337 , pp. 105-113
    • Suzuki, H.1    Yonekura, K.2    Namba, K.3
  • 38
    • 35748929649 scopus 로고    scopus 로고
    • Sorting of early and late flagellar subunits after docking at the membrane ATPase of the type III export pathway
    • Stafford, G. P. et al. Sorting of early and late flagellar subunits after docking at the membrane ATPase of the type III export pathway. J. Mol. Biol. 374, 877-882 (2007).
    • (2007) J. Mol. Biol. , vol.374 , pp. 877-882
    • Stafford, G.P.1
  • 40
    • 79960620016 scopus 로고    scopus 로고
    • Structural diversity of bacterial flagellar motors
    • Chen, S. et al. Structural diversity of bacterial flagellar motors. EMBO J. 30, 2972-2981 (2011).
    • (2011) EMBO J. , vol.30 , pp. 2972-2981
    • Chen, S.1
  • 41
    • 33745930219 scopus 로고    scopus 로고
    • Mutational analysis of the flagellar rotor protein FliN: Identification of surfaces important for flagellar assembly and switching
    • Paul, K., Harmon, J. G. & Blair, D. F. Mutational analysis of the flagellar rotor protein FliN: identification of surfaces important for flagellar assembly and switching. J. Bacteriol. 188, 5240-5248 (2006).
    • (2006) J. Bacteriol. , vol.188 , pp. 5240-5248
    • Paul, K.1    Harmon, J.G.2    Blair, D.F.3
  • 42
    • 0016370644 scopus 로고
    • Assembly of Salmonella flagellin in vitro and in vivo
    • Iino, T. Assembly of Salmonella flagellin in vitro and in vivo. J. Supramol. Struct. 2, 372-384 (1974).
    • (1974) J. Supramol. Struct. , vol.2 , pp. 372-384
    • Iino, T.1
  • 43
    • 0031735650 scopus 로고    scopus 로고
    • Bacterial flagellation and cell division
    • Aizawa, S. & Kubori, T. Bacterial flagellation and cell division. Genes Cells 3, 625-634 (1998).
    • (1998) Genes Cells , vol.3 , pp. 625-634
    • Aizawa, S.1    Kubori, T.2
  • 44
    • 79960463317 scopus 로고    scopus 로고
    • Genetic characterization of conserved charged residues in the bacterial flagellar type III export protein FlhA
    • Hara, N., Namba, K. & Minamino, T. Genetic characterization of conserved charged residues in the bacterial flagellar type III export protein FlhA. PLoS One 6, e22417 (2011).
    • (2011) PLoS One , vol.6 , pp. e22417
    • Hara, N.1    Namba, K.2    Minamino, T.3
  • 45
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A. & Wanner, B. L. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97, 6640-6645 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 46
    • 0033059596 scopus 로고    scopus 로고
    • Components of the Salmonella flagellar export apparatus and classification of export substrates
    • Minamino, T. & Macnab, R. M. Components of the Salmonella flagellar export apparatus and classification of export substrates. J. Bacteriol. 181, 1388-1394 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 1388-1394
    • Minamino, T.1    Macnab, R.M.2
  • 47
    • 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. & Namba,K. 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).
    • (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
  • 48
    • 33745276514 scopus 로고    scopus 로고
    • Oligomerization of the bacterial flagellar ATPase FliI is controlled by its extreme N-terminal region
    • Minamino, T. et al . Oligomerization of the bacterial flagellar ATPase FliI is controlled by its extreme N-terminal region. J. Mol. Biol. 360, 510-519 (2006).
    • (2006) J. Mol. Biol. , vol.360 , pp. 510-519
    • Minamino, T.1
  • 49
    • 0026752989 scopus 로고
    • Morphological pathway of flagellar assembly in Salmonella typhimurium
    • Kubori, T., Shimamoto, N., Yamaguchi, S., Namba, K. & Aizwa, S. Morphological pathway of flagellar assembly in Salmonella typhimurium. J. Mol. Biol. 226, 433-446 (1992).
    • (1992) J. Mol. Biol. , vol.226 , pp. 433-446
    • Kubori, T.1    Shimamoto, N.2    Yamaguchi, S.3    Namba, K.4    Aizwa, S.5


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