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Volumn 195, Issue 23, 2013, Pages 5285-5296

A distant homologue of the FlgT protein interacts with MotB and FliL and is essential for flagellar rotation in Rhodobacter sphaeroides

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN FLGT; PROTEIN FLIL; PROTEIN MOTB; UNCLASSIFIED DRUG;

EID: 84887525457     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00760-13     Document Type: Article
Times cited : (14)

References (93)
  • 1
    • 0041673353 scopus 로고    scopus 로고
    • The rotary motor of bacterial flagella
    • Berg HC. 2003. The rotary motor of bacterial flagella. Annu. Rev. Biochem. 72:19-54.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 19-54
    • Berg, H.C.1
  • 2
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab RM. 2003. How bacteria assemble flagella. Annu. Rev. Microbiol. 57:77-100.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 77-100
    • Macnab, R.M.1
  • 4
    • 57149114304 scopus 로고    scopus 로고
    • Flagellar motility in bacteria: structure and function of flagellar motor
    • Terashima H, Kojima S, Homma M. 2008. Flagellar motility in bacteria: structure and function of flagellar motor. Int. Rev. Cell Mol. Biol. 270:39-85.
    • (2008) Int. Rev. Cell Mol. Biol. , vol.270 , pp. 39-85
    • Terashima, H.1    Kojima, S.2    Homma, M.3
  • 5
    • 1842588296 scopus 로고    scopus 로고
    • The bacterial flagellar motor: structure and function of a complex molecular machine
    • Kojima S, Blair DF. 2004. The bacterial flagellar motor: structure and function of a complex molecular machine. Int. Rev. Cytol. 233:93-134.
    • (2004) Int. Rev. Cytol. , vol.233 , pp. 93-134
    • Kojima, S.1    Blair, D.F.2
  • 6
    • 0035342626 scopus 로고    scopus 로고
    • Na(+)-driven flagellar motor of Vibrio
    • Yorimitsu T, Homma M. 2001. Na(+)-driven flagellar motor of Vibrio. Biochim. Biophys. Acta 1505:82-93.
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 82-93
    • Yorimitsu, T.1    Homma, M.2
  • 7
    • 80053131520 scopus 로고    scopus 로고
    • Sodium-driven motor of the polar flagellum in marine bacteria Vibrio
    • Li N, Kojima S, Homma M. 2011. Sodium-driven motor of the polar flagellum in marine bacteria Vibrio. Genes Cells 16:985-999.
    • (2011) Genes Cells , vol.16 , pp. 985-999
    • Li, N.1    Kojima, S.2    Homma, M.3
  • 8
    • 0023055674 scopus 로고
    • The sodium cycle. I. Na+-dependent motility and modes of membrane energization in the marine alkalotolerant Vibrio alginolyticus
    • Dibrov PA, Kostryko VA, Lazarova RL, Skulachev VP, Smirnova IA. 1986. The sodium cycle. I. Na+-dependent motility and modes of membrane energization in the marine alkalotolerant Vibrio alginolyticus. Biochim. Biophys. Acta 850:449-457.
    • (1986) Biochim. Biophys. Acta , vol.850 , pp. 449-457
    • Dibrov, P.A.1    Kostryko, V.A.2    Lazarova, R.L.3    Skulachev, V.P.4    Smirnova, I.A.5
  • 10
    • 0028274712 scopus 로고
    • Isolation, characterization and structure of bacterial flagellar motors containing the switch complex
    • Francis NR, Sosinsky GE, Thomas D, DeRosier DJ. 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
  • 11
    • 0022899744 scopus 로고
    • Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium
    • Yamaguchi S, Aizawa S, Kihara M, Isomura M, Jones CJ, Macnab RM. 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.2    Kihara, M.3    Isomura, M.4    Jones, C.J.5    Macnab, R.M.6
  • 13
    • 0030069386 scopus 로고    scopus 로고
    • FliG and FliM distribution in the Salmonella typhimurium cell and flagellar basal bodies
    • Zhao R, Amsler CD, Matsumura P, Khan S. 1996. FliG and FliM distribution in the Salmonella typhimurium cell and flagellar basal bodies. J. Bacteriol. 178:258-265.
    • (1996) J. Bacteriol. , vol.178 , pp. 258-265
    • Zhao, R.1    Amsler, C.D.2    Matsumura, P.3    Khan, S.4
  • 14
    • 0031557399 scopus 로고    scopus 로고
    • Charged residues of the rotor protein FliG essential for torque generation in the flagellar motor of Escherichia coli
    • Lloyd SA, Blair DF. 1997. Charged residues of the rotor protein FliG essential for torque generation in the flagellar motor of Escherichia coli. J. Mol. Biol. 266:733-744.
    • (1997) J. Mol. Biol. , vol.266 , pp. 733-744
    • Lloyd, S.A.1    Blair, D.F.2
  • 15
    • 0032568636 scopus 로고    scopus 로고
    • Electrostatic interactions between rotor and stator in the bacterial flagellar motor
    • Zhou J, Lloyd SA, Blair DF. 1998. Electrostatic interactions between rotor and stator in the bacterial flagellar motor. Proc. Natl. Acad. Sci. U.S.A. 95:6436-6441.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6436-6441
    • Zhou, J.1    Lloyd, S.A.2    Blair, D.F.3
  • 16
    • 84873045159 scopus 로고    scopus 로고
    • Distinct roles of highly conserved charged residues at the MotA-FliG interface in bacterial flagellar motor rotation
    • Morimoto YV, Nakamura S, Hiraoka KD, Namba K, 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
  • 17
    • 77955924240 scopus 로고    scopus 로고
    • Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching
    • Lee LK, Ginsburg MA, Crovace C, Donohoe M, Stock D. 2010. Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching. Nature 466:996-1000.
    • (2010) Nature , vol.466 , pp. 996-1000
    • Lee, L.K.1    Ginsburg, M.A.2    Crovace, C.3    Donohoe, M.4    Stock, D.5
  • 18
    • 81055156686 scopus 로고    scopus 로고
    • Mutations targeting the C-terminal domain of FliG can disrupt motor assembly in the Na(+)-driven flagella of Vibrio alginolyticus
    • Kojima S, Nonoyama N, Takekawa N, Fukuoka H, Homma M. 2011. Mutations targeting the C-terminal domain of FliG can disrupt motor assembly in the Na(+)-driven flagella of Vibrio alginolyticus. J. Mol. Biol. 414:62-74.
    • (2011) J. Mol. Biol. , vol.414 , pp. 62-74
    • Kojima, S.1    Nonoyama, N.2    Takekawa, N.3    Fukuoka, H.4    Homma, M.5
  • 19
    • 0025058346 scopus 로고
    • The MotA protein of E. coli is a protonconducting component of the flagellar motor
    • Blair DF, Berg HC. 1990. The MotA protein of E. coli is a protonconducting component of the flagellar motor. Cell 60:439-449.
    • (1990) Cell , vol.60 , pp. 439-449
    • Blair, D.F.1    Berg, H.C.2
  • 20
    • 0025718616 scopus 로고
    • Evidence for interactions between MotA and MotB, torque-generating elements of the flagellar motor of Escherichia coli
    • Stolz B, Berg HC. 1991. Evidence for interactions between MotA and MotB, torque-generating elements of the flagellar motor of Escherichia coli. J. Bacteriol. 173:7033-7037.
    • (1991) J. Bacteriol. , vol.173 , pp. 7033-7037
    • Stolz, B.1    Berg, H.C.2
  • 21
    • 0030590217 scopus 로고    scopus 로고
    • Motility protein complexes in the bacterial flagellar motor
    • Tang H, Braun TF, Blair DF. 1996. Motility protein complexes in the bacterial flagellar motor. J. Mol. Biol. 261:209-221.
    • (1996) J. Mol. Biol. , vol.261 , pp. 209-221
    • Tang, H.1    Braun, T.F.2    Blair, D.F.3
  • 23
    • 0023750050 scopus 로고
    • Effects of mot gene expression on the structure of the flagellar motor
    • Khan S, Dapice M, Reese TS. 1988. Effects of mot gene expression on the structure of the flagellar motor. J. Mol. Biol. 202:575-584.
    • (1988) J. Mol. Biol. , vol.202 , pp. 575-584
    • Khan, S.1    Dapice, M.2    Reese, T.S.3
  • 24
    • 0035980241 scopus 로고    scopus 로고
    • Targeted disulfide cross-linking of the MotB protein of Escherichia coli: evidence for two H(+) channels in the stator complex
    • Braun TF, Blair DF. 2001. Targeted disulfide cross-linking of the MotB protein of Escherichia coli: evidence for two H(+) channels in the stator complex. Biochemistry 40:13051-13059.
    • (2001) Biochemistry , vol.40 , pp. 13051-13059
    • Braun, T.F.1    Blair, D.F.2
  • 25
    • 0346727448 scopus 로고    scopus 로고
    • Arrangement of core membrane segments in the MotA/MotB proton-channel complex of Escherichia coli
    • Braun TF, Al-Mawsawi LQ, Kojima S, Blair DF. 2004. Arrangement of core membrane segments in the MotA/MotB proton-channel complex of Escherichia coli. Biochemistry 43:35-45.
    • (2004) Biochemistry , vol.43 , pp. 35-45
    • Braun, T.F.1    Al-Mawsawi, L.Q.2    Kojima, S.3    Blair, D.F.4
  • 26
    • 0026068420 scopus 로고
    • Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction
    • Blair DF, Berg HC. 1991. Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction. J. Mol. Biol. 221:1433-1442.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1433-1442
    • Blair, D.F.1    Berg, H.C.2
  • 27
    • 0021611311 scopus 로고
    • Gene sequence and predicted amino acid sequence of the MotA protein, a membrane-associated protein required for flagellar rotation in Escherichia coli
    • Dean GE, Macnab RM, Stader J, Matsumura P, Burks C. 1984. Gene sequence and predicted amino acid sequence of the MotA protein, a membrane-associated protein required for flagellar rotation in Escherichia coli. J. Bacteriol. 159:991-999.
    • (1984) J. Bacteriol. , vol.159 , pp. 991-999
    • Dean, G.E.1    Macnab, R.M.2    Stader, J.3    Matsumura, P.4    Burks, C.5
  • 28
    • 0029165325 scopus 로고
    • Membrane topology of the MotA protein of Escherichia coli
    • Zhou J, Fazzio RT, Blair DF. 1995. Membrane topology of the MotA protein of Escherichia coli. J. Mol. Biol. 251:237-242.
    • (1995) J. Mol. Biol. , vol.251 , pp. 237-242
    • Zhou, J.1    Fazzio, R.T.2    Blair, D.F.3
  • 29
    • 0024286468 scopus 로고
    • Bacterial motility: membrane topology of the Escherichia coli MotB protein
    • Chun SY, Parkinson JS. 1988. Bacterial motility: membrane topology of the Escherichia coli MotB protein. Science 239:276-278.
    • (1988) Science , vol.239 , pp. 276-278
    • Chun, S.Y.1    Parkinson, J.S.2
  • 30
    • 68649085420 scopus 로고    scopus 로고
    • The peptidoglycan-binding (PGB) domain of the Escherichia coli Pal protein can also function as the PGB domain in E. coli flagellar motor protein MotB
    • Hizukuri Y, Morton JF, Yakushi T, Kojima S, Homma M. 2009. The peptidoglycan-binding (PGB) domain of the Escherichia coli Pal protein can also function as the PGB domain in E. coli flagellar motor protein MotB. J. Biochem. 146:219-229.
    • (2009) J. Biochem. , vol.146 , pp. 219-229
    • Hizukuri, Y.1    Morton, J.F.2    Yakushi, T.3    Kojima, S.4    Homma, M.5
  • 31
    • 48749111115 scopus 로고    scopus 로고
    • Crystal structure of the cell wall anchor domain of MotB, a stator component of the bacterial flagellar motor: implications for peptidoglycan recognition
    • Roujeinikova A. 2008. Crystal structure of the cell wall anchor domain of MotB, a stator component of the bacterial flagellar motor: implications for peptidoglycan recognition. Proc. Natl. Acad. Sci. U.S.A. 105:10348-10353.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 10348-10353
    • Roujeinikova, A.1
  • 32
    • 0030776508 scopus 로고    scopus 로고
    • Residues of the cytoplasmic domain of MotA essential for torque generation in the bacterial flagellar motor
    • Zhou J, Blair DF. 1997. Residues of the cytoplasmic domain of MotA essential for torque generation in the bacterial flagellar motor. J. Mol. Biol. 273:428-439.
    • (1997) J. Mol. Biol. , vol.273 , pp. 428-439
    • Zhou, J.1    Blair, D.F.2
  • 33
    • 54849421748 scopus 로고    scopus 로고
    • Membrane segment organization in the stator complex of the flagellar motor: implications for proton flow and proton-induced conformational change
    • Kim EA, Price-Carter M, Carlquist WC, Blair DF. 2008. Membrane segment organization in the stator complex of the flagellar motor: implications for proton flow and proton-induced conformational change. Biochemistry 47:11332-11339.
    • (2008) Biochemistry , vol.47 , pp. 11332-11339
    • Kim, E.A.1    Price-Carter, M.2    Carlquist, W.C.3    Blair, D.F.4
  • 34
    • 53849145309 scopus 로고    scopus 로고
    • Suppressor analysis of the MotB(D33E) mutation to probe bacterial flagellar motor dynamics coupled with proton translocation
    • Che YS, Nakamura S, Kojima S, Kami-ike N, Namba K, Minamino T. 2008. Suppressor analysis of the MotB(D33E) mutation to probe bacterial flagellar motor dynamics coupled with proton translocation. J. Bacteriol. 190:6660-6667.
    • (2008) J. Bacteriol. , vol.190 , pp. 6660-6667
    • Che, Y.S.1    Nakamura, S.2    Kojima, S.3    Kami-ike, N.4    Namba, K.5    Minamino, T.6
  • 35
    • 0031944413 scopus 로고    scopus 로고
    • Function of protonatable residues in the flagellar motor of Escherichia coli: a critical role for Asp 32 of MotB
    • Zhou J, Sharp LL, Tang HL, Lloyd SA, Billings S, Braun TF, Blair DF. 1998. Function of protonatable residues in the flagellar motor of Escherichia coli: a critical role for Asp 32 of MotB. J. Bacteriol. 180:2729-2735.
    • (1998) J. Bacteriol. , vol.180 , pp. 2729-2735
    • Zhou, J.1    Sharp, L.L.2    Tang, H.L.3    Lloyd, S.A.4    Billings, S.5    Braun, T.F.6    Blair, D.F.7
  • 36
    • 0035980267 scopus 로고    scopus 로고
    • Conformational change in the stator of the bacterial flagellar motor
    • Kojima S, Blair DF. 2001. Conformational change in the stator of the bacterial flagellar motor. Biochemistry 40:13041-13050.
    • (2001) Biochemistry , vol.40 , pp. 13041-13050
    • Kojima, S.1    Blair, D.F.2
  • 37
    • 52649147435 scopus 로고    scopus 로고
    • Bacterial flagellar motor
    • Sowa Y, Berry RM. 2008. Bacterial flagellar motor. Q. Rev. Biophys. 41:103-132.
    • (2008) Q. Rev. Biophys. , vol.41 , pp. 103-132
    • Sowa, Y.1    Berry, R.M.2
  • 38
    • 0037715359 scopus 로고    scopus 로고
    • Flagellar movement driven by proton translocation
    • Blair DF. 2003. Flagellar movement driven by proton translocation. FEBS Lett. 545:86-95.
    • (2003) FEBS Lett. , vol.545 , pp. 86-95
    • Blair, D.F.1
  • 39
    • 0024295536 scopus 로고
    • Restoration of torque in defective flagellar motors
    • Blair DF, Berg HC. 1988. Restoration of torque in defective flagellar motors. Science 242:1678-1681.
    • (1988) Science , vol.242 , pp. 1678-1681
    • Blair, D.F.1    Berg, H.C.2
  • 41
    • 0025339204 scopus 로고
    • Co-overproduction and localization of the Escherichia coli motility proteins MotA and MotB
    • Wilson ML, Macnab RM. 1990. Co-overproduction and localization of the Escherichia coli motility proteins MotA and MotB. J. Bacteriol. 172:3932-3939.
    • (1990) J. Bacteriol. , vol.172 , pp. 3932-3939
    • Wilson, M.L.1    Macnab, R.M.2
  • 43
    • 0034677671 scopus 로고    scopus 로고
    • Mot protein assembly into the bacterial flagellum: a model based on mutational analysis of the motB gene
    • Van Way SM, Hosking ER, Braun TF, Manson MD. 2000. Mot protein assembly into the bacterial flagellum: a model based on mutational analysis of the motB gene. J. Mol. Biol. 297:7-24.
    • (2000) J. Mol. Biol. , vol.297 , pp. 7-24
    • Van Way, S.M.1    Hosking, E.R.2    Braun, T.F.3    Manson, M.D.4
  • 44
    • 77950369485 scopus 로고    scopus 로고
    • Protonconductivity assay of plugged and unplugged MotA/B proton channel by cytoplasmic pHluorin expressed in Salmonella
    • Morimoto YV, Che YS, Minamino T, Namba K. 2010. Protonconductivity assay of plugged and unplugged MotA/B proton channel by cytoplasmic pHluorin expressed in Salmonella. FEBS Lett. 584:1268-1272.
    • (2010) FEBS Lett. , vol.584 , pp. 1268-1272
    • Morimoto, Y.V.1    Che, Y.S.2    Minamino, T.3    Namba, K.4
  • 45
    • 82455210507 scopus 로고    scopus 로고
    • Role of the MotB linker in the assembly and activation of the bacterial flagellar motor. Acta Crystallogr
    • O'Neill J, Xie M, Hijnen M, Roujeinikova A. 2011. Role of the MotB linker in the assembly and activation of the bacterial flagellar motor. Acta Crystallogr. D Biol. Crystallogr. 67:1009-1016.
    • (2011) D Biol. Crystallogr. , vol.67 , pp. 1009-1016
    • O'Neill, J.1    Xie, M.2    Hijnen, M.3    Roujeinikova, A.4
  • 47
    • 34247895585 scopus 로고    scopus 로고
    • A complete set of flagellar genes acquired by horizontal transfer coexists with the endogenous flagellar system in Rhodobacter sphaeroides
    • Poggio S, Abreu-Goodger C, Fabela S, Osorio A, Dreyfus G, Vinuesa P, Camarena L. 2007. A complete set of flagellar genes acquired by horizontal transfer coexists with the endogenous flagellar system in Rhodobacter sphaeroides. J. Bacteriol. 189:3208-3216.
    • (2007) J. Bacteriol. , vol.189 , pp. 3208-3216
    • Poggio, S.1    Abreu-Goodger, C.2    Fabela, S.3    Osorio, A.4    Dreyfus, G.5    Vinuesa, P.6    Camarena, L.7
  • 48
    • 84855406611 scopus 로고    scopus 로고
    • In Rhodobacter sphaeroides, chemotactic operon 1 regulates rotation of the flagellar system 2
    • Martinez-del Campo A, Ballado T, Camarena L, Dreyfus G. 2011. In Rhodobacter sphaeroides, chemotactic operon 1 regulates rotation of the flagellar system 2. J. Bacteriol. 193:6781-6786.
    • (2011) J. Bacteriol. , vol.193 , pp. 6781-6786
    • Martinez-del Campo, A.1    Ballado, T.2    Camarena, L.3    Dreyfus, G.4
  • 49
    • 0023112062 scopus 로고
    • Unidirectional, intermittent rotation of the flagellum of Rhodobacter sphaeroides
    • Armitage JP, Macnab RM. 1987. Unidirectional, intermittent rotation of the flagellum of Rhodobacter sphaeroides. J. Bacteriol. 169:514-518.
    • (1987) J. Bacteriol. , vol.169 , pp. 514-518
    • Armitage, J.P.1    Macnab, R.M.2
  • 51
    • 0031876827 scopus 로고    scopus 로고
    • The flagellar switch genes fliM and fliN of Rhodobacter sphaeroides are contained in a large flagellar gene cluster
    • Garcia N, Campos A, Osorio A, Poggio S, Gonzalez-Pedrajo B, Camarena L, Dreyfus G. 1998. The flagellar switch genes fliM and fliN of Rhodobacter sphaeroides are contained in a large flagellar gene cluster. J. Bacteriol. 180:3978-3982.
    • (1998) J. Bacteriol. , vol.180 , pp. 3978-3982
    • Garcia, N.1    Campos, A.2    Osorio, A.3    Poggio, S.4    Gonzalez-Pedrajo, B.5    Camarena, L.6    Dreyfus, G.7
  • 52
    • 0035111139 scopus 로고    scopus 로고
    • The hook gene (flgE) is expressed from the flgBCDEF operon in Rhodobacter sphaeroides: study of an flgE mutant
    • Ballado T, Camarena L, Gonzalez-Pedrajo B, Silva-Herzog E, Dreyfus G. 2001. The hook gene (flgE) is expressed from the flgBCDEF operon in Rhodobacter sphaeroides: study of an flgE mutant. J. Bacteriol. 183:1680-1687.
    • (2001) J. Bacteriol. , vol.183 , pp. 1680-1687
    • Ballado, T.1    Camarena, L.2    Gonzalez-Pedrajo, B.3    Silva-Herzog, E.4    Dreyfus, G.5
  • 53
    • 0037073119 scopus 로고    scopus 로고
    • Characterization of the flgG operon of Rhodobacter sphaeroides WS8 and its role in flagellum biosynthesis
    • Gonzalez-Pedrajo B, de la Mora J, Ballado T, Camarena L, Dreyfus G. 2002. Characterization of the flgG operon of Rhodobacter sphaeroides WS8 and its role in flagellum biosynthesis. Biochim. Biophys. Acta 1579:55-63.
    • (2002) Biochim. Biophys. Acta , vol.1579 , pp. 55-63
    • Gonzalez-Pedrajo, B.1    de la Mora, J.2    Ballado, T.3    Camarena, L.4    Dreyfus, G.5
  • 54
    • 0028812856 scopus 로고
    • Analysis of the motA flagellar motor gene from Rhodobacter sphaeroides, a bacterium with a unidirectional, stopstart flagellum
    • Shah DS, Sockett RE. 1995. Analysis of the motA flagellar motor gene from Rhodobacter sphaeroides, a bacterium with a unidirectional, stopstart flagellum. Mol. Microbiol. 17:961-969.
    • (1995) Mol. Microbiol. , vol.17 , pp. 961-969
    • Shah, D.S.1    Sockett, R.E.2
  • 55
    • 0029016716 scopus 로고
    • Rhodobacter sphaeroides WS8 expresses a polypeptide that is similar to MotB of Escherichia coli
    • Shah DS, Armitage JP, Sockett RE. 1995. Rhodobacter sphaeroides WS8 expresses a polypeptide that is similar to MotB of Escherichia coli. J. Bacteriol. 177:2929-2932.
    • (1995) J. Bacteriol. , vol.177 , pp. 2929-2932
    • Shah, D.S.1    Armitage, J.P.2    Sockett, R.E.3
  • 57
    • 0028125086 scopus 로고
    • Caulobacter flagellar function, but not assembly, requires FliL, a non-polarly localized membrane protein present in all cell types
    • Jenal U, White J, Shapiro L. 1994. Caulobacter flagellar function, but not assembly, requires FliL, a non-polarly localized membrane protein present in all cell types. J. Mol. Biol. 243:227-244.
    • (1994) J. Mol. Biol. , vol.243 , pp. 227-244
    • Jenal, U.1    White, J.2    Shapiro, L.3
  • 58
    • 67649454946 scopus 로고    scopus 로고
    • Genetic determinants of Silicibacter sp. TM1040 motility
    • Belas R, Horikawa E, Aizawa S, Suvanasuthi R. 2009. Genetic determinants of Silicibacter sp. TM1040 motility. J. Bacteriol. 191:4502-4512.
    • (2009) J. Bacteriol. , vol.191 , pp. 4502-4512
    • Belas, R.1    Horikawa, E.2    Aizawa, S.3    Suvanasuthi, R.4
  • 59
    • 0034972538 scopus 로고    scopus 로고
    • Mutations in genes involved in the flagellar export apparatus of the solvent-tolerant Pseudomonas putida DOT-T1E strain impair motility and lead to hypersensitivity to toluene shocks
    • Segura A, Duque E, Hurtado A, Ramos JL. 2001. Mutations in genes involved in the flagellar export apparatus of the solvent-tolerant Pseudomonas putida DOT-T1E strain impair motility and lead to hypersensitivity to toluene shocks. J. Bacteriol. 183:4127-4133.
    • (2001) J. Bacteriol. , vol.183 , pp. 4127-4133
    • Segura, A.1    Duque, E.2    Hurtado, A.3    Ramos, J.L.4
  • 60
    • 41049106588 scopus 로고    scopus 로고
    • FliL is essential for swarming: motor rotation in absence of FliL fractures the flagellar rod in swarmer cells of Salmonella enterica
    • Attmannspacher U, Scharf BE, Harshey RM. 2008. FliL is essential for swarming: motor rotation in absence of FliL fractures the flagellar rod in swarmer cells of Salmonella enterica. Mol. Microbiol. 68:328-341.
    • (2008) Mol. Microbiol. , vol.68 , pp. 328-341
    • Attmannspacher, U.1    Scharf, B.E.2    Harshey, R.M.3
  • 61
    • 84873541778 scopus 로고    scopus 로고
    • More than motility: Salmonella flagella contribute to overriding friction and facilitating colony hydration during swarming
    • Partridge JD, Harshey RM. 2013. More than motility: Salmonella flagella contribute to overriding friction and facilitating colony hydration during swarming. J. Bacteriol. 195:919-929.
    • (2013) J. Bacteriol. , vol.195 , pp. 919-929
    • Partridge, J.D.1    Harshey, R.M.2
  • 62
    • 84873539650 scopus 로고    scopus 로고
    • Activity of Proteus mirabilis FliL is viscosity dependent and requires extragenic DNA
    • Lee YY, Patellis J, Belas R. 2013. Activity of Proteus mirabilis FliL is viscosity dependent and requires extragenic DNA. J. Bacteriol. 195:823-832.
    • (2013) J. Bacteriol. , vol.195 , pp. 823-832
    • Lee, Y.Y.1    Patellis, J.2    Belas, R.3
  • 63
    • 84869145315 scopus 로고    scopus 로고
    • A novel component of the Rhodobacter sphaeroides Fla1 flagellum is essential for motor rotation
    • Ramirez-Cabrera V, Poggio S, Domenzain C, Osorio A, Dreyfus G, Camarena L. 2012. A novel component of the Rhodobacter sphaeroides Fla1 flagellum is essential for motor rotation. J. Bacteriol. 194:6174-6183.
    • (2012) J. Bacteriol. , vol.194 , pp. 6174-6183
    • Ramirez-Cabrera, V.1    Poggio, S.2    Domenzain, C.3    Osorio, A.4    Dreyfus, G.5    Camarena, L.6
  • 64
    • 78049356099 scopus 로고    scopus 로고
    • The flagellar basal body-associated protein FlgT is essential for a novel ring structure in the sodium-driven Vibrio motor
    • Terashima H, Koike M, Kojima S, Homma M. 2010. The flagellar basal body-associated protein FlgT is essential for a novel ring structure in the sodium-driven Vibrio motor. J. Bacteriol. 192:5609-5615.
    • (2010) J. Bacteriol. , vol.192 , pp. 5609-5615
    • Terashima, H.1    Koike, M.2    Kojima, S.3    Homma, M.4
  • 65
    • 0000571531 scopus 로고
    • Molecular biology of the Rhodobacter sphaeroides flagellum
    • Sockett RE, Foster JCA, Armitage JP. 1990. Molecular biology of the Rhodobacter sphaeroides flagellum. FEMS Symp. 53:473-479.
    • (1990) FEMS Symp. , vol.53 , pp. 473-479
    • Sockett, R.E.1    Foster, J.C.A.2    Armitage, J.P.3
  • 66
    • 0000618907 scopus 로고
    • The kinetics of the synthesis of photopigments in Rhodopseudomonas sphaeroides
    • Sistrom WR. 1962. The kinetics of the synthesis of photopigments in Rhodopseudomonas sphaeroides. J. Gen. Microbiol. 28:607-616.
    • (1962) J. Gen. Microbiol. , vol.28 , pp. 607-616
    • Sistrom, W.R.1
  • 67
    • 0027248699 scopus 로고
    • Construction of new beta-glucuronidase cassettes for making transcriptional fusions and their use with new methods for allele replacement
    • Metcalf WW, Wanner BL. 1993. Construction of new beta-glucuronidase cassettes for making transcriptional fusions and their use with new methods for allele replacement. Gene 129:17-25.
    • (1993) Gene , vol.129 , pp. 17-25
    • Metcalf, W.W.1    Wanner, B.L.2
  • 68
    • 0027158657 scopus 로고
    • Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria
    • Quandt J, Hynes MF. 1993. Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria. Gene 127:15-21.
    • (1993) Gene , vol.127 , pp. 15-21
    • Quandt, J.1    Hynes, M.F.2
  • 69
    • 0023703922 scopus 로고
    • Construction, characterization, and complementation of a Puf- mutant of Rhodobacter sphaeroides
    • Davis J, Donohue TJ, Kaplan S. 1988. Construction, characterization, and complementation of a Puf- mutant of Rhodobacter sphaeroides. J. Bacteriol. 170:320-329.
    • (1988) J. Bacteriol. , vol.170 , pp. 320-329
    • Davis, J.1    Donohue, T.J.2    Kaplan, S.3
  • 70
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetics engineering: transposon mutagenesis in Gramnegative bacteria
    • Simon R, Priefer U, Phüler A. 1983. A broad host range mobilization system for in vivo genetics engineering: transposon mutagenesis in Gramnegative bacteria. Biotechnology 1:784-791.
    • (1983) Biotechnology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Phüler, A.3
  • 71
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • doi:10.1186/1471-2105-9-40
    • Zhang Y. 2008. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9:40. doi:10.1186/1471-2105-9-40.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 72
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, Zhang Y. 2010. I-TASSER: a unified platform for automated protein structure and function prediction. Nat. Protoc. 5:725-738.
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 73
    • 84864460609 scopus 로고    scopus 로고
    • COFACTOR: an accurate comparative algorithm for structure-based protein function annotation
    • doi:10.1093/nar/gks372
    • Roy A, Yang J, Zhang Y. 2012. COFACTOR: an accurate comparative algorithm for structure-based protein function annotation. Nucleic Acids Res. 40:W471-W477. doi:10.1093/nar/gks372.
    • (2012) Nucleic Acids Res. , vol.40
    • Roy, A.1    Yang, J.2    Zhang, Y.3
  • 74
    • 0023715368 scopus 로고
    • Improved broadhost-range plasmids for DNA cloning in Gram-negative bacteria
    • Keen NT, Tamaki S, Kobayashi D, Trollinger D. 1988. Improved broadhost-range plasmids for DNA cloning in Gram-negative bacteria. Gene 70:191-197.
    • (1988) Gene , vol.70 , pp. 191-197
    • Keen, N.T.1    Tamaki, S.2    Kobayashi, D.3    Trollinger, D.4
  • 75
    • 0035876407 scopus 로고    scopus 로고
    • Terminal proteins essential for the replication of linear plasmids and chromosomes in Streptomyces
    • Bao K, Cohen SN. 2001. Terminal proteins essential for the replication of linear plasmids and chromosomes in Streptomyces. Genes Dev. 15:1518-1527.
    • (2001) Genes Dev. , vol.15 , pp. 1518-1527
    • Bao, K.1    Cohen, S.N.2
  • 77
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 78
    • 33644853360 scopus 로고    scopus 로고
    • Molecular basis of the interaction between the flagellar export proteins FliI and FliH from Helicobacter pylori
    • Lane MC, O'Toole PW, Moore SA. 2006. Molecular basis of the interaction between the flagellar export proteins FliI and FliH from Helicobacter pylori. J. Biol. Chem. 281:508-517.
    • (2006) J. Biol. Chem. , vol.281 , pp. 508-517
    • Lane, M.C.1    O'Toole, P.W.2    Moore, S.A.3
  • 79
    • 0021913736 scopus 로고
    • Purification and characterization of the flagellar hook-basal body complex of Salmonella typhimurium
    • Aizawa SI, Dean GE, Jones CJ, Macnab RM, Yamaguchi S. 1985. Purification and characterization of the flagellar hook-basal body complex of Salmonella typhimurium. J. Bacteriol. 161:836-849.
    • (1985) J. Bacteriol. , vol.161 , pp. 836-849
    • Aizawa, S.I.1    Dean, G.E.2    Jones, C.J.3    Macnab, R.M.4    Yamaguchi, S.5
  • 80
    • 33845956897 scopus 로고    scopus 로고
    • Analysis of the roles of FlgP and FlgQ in flagellar motility of Campylobacter jejuni
    • Sommerlad SM, Hendrixson DR. 2007. Analysis of the roles of FlgP and FlgQ in flagellar motility of Campylobacter jejuni. J. Bacteriol. 189:179-186.
    • (2007) J. Bacteriol. , vol.189 , pp. 179-186
    • Sommerlad, S.M.1    Hendrixson, D.R.2
  • 81
    • 69949094466 scopus 로고    scopus 로고
    • Characterization of two outer membrane proteins, FlgO and FlgP, that influence Vibrio cholerae motility
    • Martinez RM, Dharmasena MN, Kirn TJ, Taylor RK. 2009. Characterization of two outer membrane proteins, FlgO and FlgP, that influence Vibrio cholerae motility. J. Bacteriol. 191:5669-5679.
    • (2009) J. Bacteriol. , vol.191 , pp. 5669-5679
    • Martinez, R.M.1    Dharmasena, M.N.2    Kirn, T.J.3    Taylor, R.K.4
  • 82
    • 84876043827 scopus 로고    scopus 로고
    • Insight into the assembly mechanism in the supramolecular rings of the sodium-driven Vibrio flagellar motor from the structure of FlgT
    • Terashima H, Li N, Sakuma M, Koike M, Kojima S, Homma M, Imada K. 2013. Insight into the assembly mechanism in the supramolecular rings of the sodium-driven Vibrio flagellar motor from the structure of FlgT. Proc. Natl. Acad. Sci. U.S.A. 110:6133-6138.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 6133-6138
    • Terashima, H.1    Li, N.2    Sakuma, M.3    Koike, M.4    Kojima, S.5    Homma, M.6    Imada, K.7
  • 84
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen TN, Brunak S, von Heijne G, Nielsen H. 2011. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 8:785-786.
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 85
    • 27944478488 scopus 로고    scopus 로고
    • The flagellar hierarchy of Rhodobacter sphaeroides is controlled by the concerted action of two enhancer-binding proteins
    • Poggio S, Osorio A, Dreyfus G, Camarena L. 2005. The flagellar hierarchy of Rhodobacter sphaeroides is controlled by the concerted action of two enhancer-binding proteins. Mol. Microbiol. 58:969-983.
    • (2005) Mol. Microbiol. , vol.58 , pp. 969-983
    • Poggio, S.1    Osorio, A.2    Dreyfus, G.3    Camarena, L.4
  • 86
    • 33751118241 scopus 로고    scopus 로고
    • Two chemosensory operons of Rhodobacter sphaeroides are regulated independently by sigma 28 and sigma 54
    • Martin AC, Gould M, Byles E, Roberts MA, Armitage JP. 2006. Two chemosensory operons of Rhodobacter sphaeroides are regulated independently by sigma 28 and sigma 54. J. Bacteriol. 188:7932-7940.
    • (2006) J. Bacteriol. , vol.188 , pp. 7932-7940
    • Martin, A.C.1    Gould, M.2    Byles, E.3    Roberts, M.A.4    Armitage, J.P.5
  • 87
    • 47249101480 scopus 로고    scopus 로고
    • A defined transposon mutant library and its use in identifying motility genes in Vibrio cholerae
    • Cameron DE, Urbach JM, Mekalanos JJ. 2008. A defined transposon mutant library and its use in identifying motility genes in Vibrio cholerae. Proc. Natl. Acad. Sci. U.S.A. 105:8736-8741.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 8736-8741
    • Cameron, D.E.1    Urbach, J.M.2    Mekalanos, J.J.3
  • 89
    • 0031590252 scopus 로고    scopus 로고
    • Isolation and ultrastructural study of the flagellar basal body complex from Rhodobacter sphaeroides WS8 (wild type) and a polyhook mutant PG
    • West MA, Dreyfus G. 1997. Isolation and ultrastructural study of the flagellar basal body complex from Rhodobacter sphaeroides WS8 (wild type) and a polyhook mutant PG. Biochem. Biophys. Res. Commun. 238:733-737.
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 733-737
    • West, M.A.1    Dreyfus, G.2
  • 91
    • 77956435557 scopus 로고    scopus 로고
    • Disulphide cross-linking between the stator and the bearing components in the bacterial flagellar motor
    • Hizukuri Y, Kojima S, Homma M. 2010. Disulphide cross-linking between the stator and the bearing components in the bacterial flagellar motor. J. Biochem. 148:309-318.
    • (2010) J. Biochem. , vol.148 , pp. 309-318
    • Hizukuri, Y.1    Kojima, S.2    Homma, M.3
  • 92
    • 21844451390 scopus 로고    scopus 로고
    • Interactions of MotX with MotY and with the PomA/PomB sodium ion channel complex of the Vibrio alginolyticus polar flagellum
    • Okabe M, Yakushi T, Homma M. 2005. Interactions of MotX with MotY and with the PomA/PomB sodium ion channel complex of the Vibrio alginolyticus polar flagellum. J. Biol. Chem. 280:25659-25664.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25659-25664
    • Okabe, M.1    Yakushi, T.2    Homma, M.3
  • 93
    • 33750464866 scopus 로고    scopus 로고
    • The Vibrio motor proteins, MotX and MotY, are associated with the basal body of Na-driven flagella and required for stator formation
    • Terashima H, Fukuoka H, Yakushi T, Kojima S, Homma M. 2006. The Vibrio motor proteins, MotX and MotY, are associated with the basal body of Na-driven flagella and required for stator formation. Mol. Microbiol. 62:1170-1180.
    • (2006) Mol. Microbiol. , vol.62 , pp. 1170-1180
    • Terashima, H.1    Fukuoka, H.2    Yakushi, T.3    Kojima, S.4    Homma, M.5


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