메뉴 건너뛰기




Volumn 195, Issue 3, 2013, Pages 474-481

Distinct roles of highly conserved charged residues at the MotA-FliG interface in bacterial flagellar motor rotation

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ASPARTIC ACID; BACTERIAL PROTEIN; FLIG PROTEIN; GREEN FLUORESCENT PROTEIN; MOTA PROTEIN; UNCLASSIFIED DRUG;

EID: 84873045159     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01971-12     Document Type: Article
Times cited : (74)

References (46)
  • 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
    • 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
  • 3
    • 0035980241 scopus 로고    scopus 로고
    • + channels in the stator complex
    • + channels in the stator complex. Biochemistry 40:13051-13059.
    • (2001) Biochemistry , vol.40 , pp. 13051-13059
    • Braun, T.1    Blair, D.F.2
  • 4
    • 0347357933 scopus 로고    scopus 로고
    • Solubilization and purification of the MotA/ MotB complex of Escherichia coli
    • Kojima S, Blair DF. 2004. Solubilization and purification of the MotA/ MotB complex of Escherichia coli. Biochemistry 43:26-34.
    • (2004) Biochemistry , vol.43 , pp. 26-34
    • Kojima, S.1    Blair, D.F.2
  • 5
    • 0346727448 scopus 로고    scopus 로고
    • Arrangement of core membrane segments in the MotA/MotB protein-channel complex of Escherichia coli
    • Braun TF, Al-Mawasawi LQ, Kojima S, Blair DF. 2004. Arrangement of core membrane segments in the MotA/MotB protein-channel complex of Escherichia coli. Biochemistry 43:35-45.
    • (2004) Biochemistry , vol.43 , pp. 35-45
    • Braun, T.F.1    Al-Mawasawi, L.Q.2    Kojima, S.3    Blair, D.F.4
  • 6
    • 0021280816 scopus 로고
    • Successive incorporation of force-generating units in the bacterial rotary motor
    • Block SM, Berg HC. 1984. Successive incorporation of force-generating units in the bacterial rotary motor. Nature 309:470-472.
    • (1984) Nature , vol.309 , pp. 470-472
    • Block, S.M.1    Berg, H.C.2
  • 7
    • 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
  • 8
    • 0025058346 scopus 로고
    • The MotA protein of Escherichia coli is a protonconducting component of the flagellar motor
    • Blair DF, Berg HC. 1990. The MotA protein of Escherichia 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
  • 9
    • 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
  • 10
    • 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
  • 11
    • 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
  • 13
    • 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
  • 14
    • 0022899744 scopus 로고
    • Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium
    • Yamaguchi S, Aizawa Kihara S-IM, 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    Kihara, S.-I.M.A.2    Isomura, M.3    Jones, C.J.4    Macnab, R.M.5
  • 15
    • 0034079196 scopus 로고    scopus 로고
    • Deletion analysis of the flagellar switch protein FliG of Salmonella
    • Kihara M, Miller GU, Macnab RM. 2000. Deletion analysis of the flagellar switch protein FliG of Salmonella. J. Bacteriol. 182:3022-3028.
    • (2000) J. Bacteriol. , vol.182 , pp. 3022-3028
    • Kihara, M.1    Miller, G.U.2    Macnab, R.M.3
  • 16
    • 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
  • 17
    • 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
  • 18
    • 78649598805 scopus 로고    scopus 로고
    • Charged residues in the cytoplasmic loop of MotA are required for stator assembly into the bacterial flagellar motor
    • Morimoto YV, Nakamura S, Kami-ike N, Namba K, Minamino T. 2010. Charged residues in the cytoplasmic loop of MotA are required for stator assembly into the bacterial flagellar motor. Mol. Microbiol. 78:1117-1129.
    • (2010) Mol. Microbiol. , vol.78 , pp. 1117-1129
    • Morimoto, Y.V.1    Nakamura, S.2    Kami-ike, N.3    Namba, K.4    Minamino, T.5
  • 19
    • 81055156686 scopus 로고    scopus 로고
    • Mutations targeting the C-terminal domain of FliG can disrupt motor assembly in the Na+-driven flagella
    • Kojima S, Nonoyma 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. J. Mol. Biol. 414:62-74.
    • (2011) J. Mol. Biol. , vol.414 , pp. 62-74
    • Kojima, S.1    Nonoyma, N.2    Takekawa, N.3    Fukuoka, H.4    Homma, M.5
  • 21
    • 1442326719 scopus 로고    scopus 로고
    • Structure of the rotor of the bacterial flagellar motor revealed by electron cryomicroscopy and singleparticle image analysis
    • Suzuki H, Yonekura K, Namba K. 2004. Structure of the rotor of the bacterial flagellar motor revealed by electron cryomicroscopy and singleparticle 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
  • 23
    • 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 JP, Minamino T, Namba K. 2010. Evidence for symmetry in the elementary process of bidirectional torque generation by the bacterial flagellar motor. Proc. Natl. Acad. Sci. U. S. A. 107:17616-17620.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 17616-17620
    • Nakamura, S.1    Kami-ike, N.2    Yokota, J.P.3    Minamino, T.4    Namba, K.5
  • 24
    • 16844367441 scopus 로고    scopus 로고
    • Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima
    • Brown PN, Mathews MA, Joss LA, Hill CP, Blair DF. 2005. Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima. J. Bacteriol. 187:2890-2902.
    • (2005) J. Bacteriol. , vol.187 , pp. 2890-2902
    • Brown, P.N.1    Mathews, M.A.2    Joss, L.A.3    Hill, C.P.4    Blair, D.F.5
  • 25
    • 33749608423 scopus 로고    scopus 로고
    • The threedimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar Typhimurium
    • Thomas DR, Francis NR, Chen X, DeRosier DJ. 2006. The threedimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar Typhimurium. J. Bacteriol. 188:7039-7048.
    • (2006) J. Bacteriol. , vol.188 , pp. 7039-7048
    • Thomas, D.R.1    Francis, N.R.2    Chen, X.3    DeRosier, D.J.4
  • 26
    • 0033614958 scopus 로고    scopus 로고
    • Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor
    • Lloyd SA, Whitby FG, Blair DF, Hill CP. 1999. Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor. Nature 400:472-475.
    • (1999) Nature , vol.400 , pp. 472-475
    • Lloyd, S.A.1    Whitby, F.G.2    Blair, D.F.3    Hill, C.P.4
  • 27
    • 0036646105 scopus 로고    scopus 로고
    • Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliG
    • Brown PN, Hill CP, Blair DF. 2002. Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliG. EMBO J. 21:3225-3234.
    • (2002) EMBO J. , vol.21 , pp. 3225-3234
    • Brown, P.N.1    Hill, C.P.2    Blair, D.F.3
  • 28
    • 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
  • 29
    • 79958063382 scopus 로고    scopus 로고
    • Structural insight into the rotational switching mechanism of the bacterial flagellar motor
    • doi:10.1371 /journal.pbio.1000616
    • Minamino T, Imada K, Kinoshita M, Nakamura S, Morimoto YV, Namba K. 2011. Structural insight into the rotational switching mechanism of the bacterial flagellar motor. PLoS Biol. 9:e1000616. doi:10.1371 /journal.pbio.1000616.
    • (2011) PLoS Biol. , vol.9
    • Minamino, T.1    Imada, K.2    Kinoshita, M.3    Nakamura, S.4    Morimoto, Y.V.5    Namba, K.6
  • 30
    • 33747063575 scopus 로고    scopus 로고
    • Structure of FliM provides insight into assembly of the switch complex in the bacterial flagella motor
    • Park SY, Lowder B, Bilwes AM, Blair DF, Crane BR. 2006. Structure of FliM provides insight into assembly of the switch complex in the bacterial flagella motor. Proc. Natl. Acad. Sci. U. S. A. 103:11886-11891.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 11886-11891
    • Park, S.Y.1    Lowder, B.2    Bilwes, A.M.3    Blair, D.F.4    Crane, B.R.5
  • 32
    • 33846207448 scopus 로고    scopus 로고
    • Mutational analysis of the flagellar rotor protein FliG: sites of interaction with FliM and implications for organization of the switch complex
    • Brown PN, Terrazas M, Paul K, Blair DF. 2007. Mutational analysis of the flagellar rotor protein FliG: sites of interaction with FliM and implications for organization of the switch complex. J. Bacteriol. 189:305-312.
    • (2007) J. Bacteriol. , vol.189 , pp. 305-312
    • Brown, P.N.1    Terrazas, M.2    Paul, K.3    Blair, D.F.4
  • 33
    • 0021347115 scopus 로고
    • Genetic analysis of H2, the structural gene for phase-2 flagellin in Salmonella
    • Yamaguchi S, Fujita H, Sugata K, Taira T, 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
  • 34
    • 0032704053 scopus 로고    scopus 로고
    • Flagellar proteins and type III-exported virulence factors are the predominant proteins secreted into the culture media of Salmonella typhimurium
    • Komoriya K, Shibano N, Higano T, Azuma N, Yamaguchi SAizawa S-I. 1999. Flagellar proteins and type III-exported virulence factors are the predominant proteins secreted into the culture media of Salmonella typhimurium. Mol. Microbiol. 34:767-779.
    • (1999) Mol. Microbiol. , vol.34 , pp. 767-779
    • Komoriya, K.1    Shibano, N.2    Higano, T.3    Azuma, N.4    Saizawa, S.-I.Y.5
  • 35
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, Beckwith J. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 36
    • 77950369485 scopus 로고    scopus 로고
    • Protonconductivity assay of plugged and unplugged MotA/B proton channel by cytoplasmic pHluorin expressed in Salmonella
    • Morimoto YV, Che Minamino Y-ST, 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    Minamino, Y.-S.T.C.2    Namba, K.3
  • 37
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 38
    • 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 RM, 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
  • 39
    • 79960463317 scopus 로고    scopus 로고
    • Genetic characterization of conserved charged residues in the bacterial flagellar type III export protein FlhA
    • doi:10.1371/journal.pone.0022417
    • Hara N, Namba K, Minamino T. 2011. Genetic characterization of conserved charged residues in the bacterial flagellar type III export protein FlhA. PLoS One 6:e22417. doi:10.1371/journal.pone.0022417.
    • (2011) PLoS One , vol.6
    • Hara, N.1    Namba, K.2    Minamino, T.3
  • 40
    • 0033059596 scopus 로고    scopus 로고
    • Components of the Salmonella flagellar export apparatus and classification of export substrates
    • Minamino T, Macnab RM. 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
  • 41
    • 0037317217 scopus 로고    scopus 로고
    • Effect of intracellular pH on rotational speed of bacterial flagellar motors
    • Minamino T, Imae Y, Oosawa F, Kobayashi Y, Oosawa K. 2003. Effect of intracellular pH on rotational speed of bacterial flagellar motors. J. Bacteriol. 185:1190-1194.
    • (2003) J. Bacteriol. , vol.185 , pp. 1190-1194
    • Minamino, T.1    Imae, Y.2    Oosawa, F.3    Kobayashi, Y.4    Oosawa, K.5
  • 42
    • 53849145309 scopus 로고    scopus 로고
    • Suppressor analysis of the MotB(D33E) mutation to probe the bacterial flagellar motor dynamics coupled with proton translocation
    • Che Y-S, Nakamura S, Kojima S, Kami-ike N, Namba K, Minamino T. 2008. Suppressor analysis of the MotB(D33E) mutation to probe the 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
  • 43
    • 59149087248 scopus 로고    scopus 로고
    • Effect of intracellular pH on the torque-speed relationship of bacterial proton-driven flagellar motor
    • Nakamura S, Kami-ike N, Yokota JP, Kudo S, Minamino T, Namba K. 2009. Effect of intracellular pH on the torque-speed relationship of bacterial proton-driven flagellar motor. J. Mol. Biol. 386:332-338.
    • (2009) J. Mol. Biol. , vol.386 , pp. 332-338
    • Nakamura, S.1    Kami-ike, N.2    Yokota, J.P.3    Kudo, S.4    Minamino, T.5    Namba, K.6
  • 44
    • 0032500053 scopus 로고    scopus 로고
    • Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
    • Miesenböck G, De Angelis DA, Rothman JE. 1998. Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 394:192-195.
    • (1998) Nature , vol.394 , pp. 192-195
    • Miesenböck, G.1    De Angelis, D.A.2    Rothman, J.E.3
  • 46
    • 70349431086 scopus 로고    scopus 로고
    • Role of a conserved prolyl residue (Pro-173) of MotA in the mechanochemical reaction cycle of the proton-driven flagellar motor of Salmonella
    • Nakamura S, Morimoto YV, Kami-ike N, Minamino T, Namba K. 2009. Role of a conserved prolyl residue (Pro-173) of MotA in the mechanochemical reaction cycle of the proton-driven flagellar motor of Salmonella. J. Mol. Biol. 393:300-307.
    • (2009) J. Mol. Biol. , vol.393 , pp. 300-307
    • Nakamura, S.1    Morimoto, Y.V.2    Kami-ike, N.3    Minamino, T.4    Namba, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.