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Volumn 193, Issue 21, 2011, Pages 5914-5922

Adjusting the spokes of the flagellar motor with the DNA-binding Protein H-NS

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE LIKE NUCLEOID STRUCTURING PROTEIN; PROTEIN; PROTEIN STPA; PROTEIN SUBUNIT; PROTEIN YCGR; UNCLASSIFIED DRUG;

EID: 80055051384     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.05458-11     Document Type: Article
Times cited : (14)

References (70)
  • 1
    • 0037381991 scopus 로고    scopus 로고
    • Increased bending rigidity of single DNA molecules by HNS, a temperature and osmolarity sensor
    • Amit, R., A. B. Oppenheim, and J. Stavans. 2003. Increased bending rigidity of single DNA molecules by HNS, a temperature and osmolarity sensor. Biophys. J. 84:2467-2473.
    • (2003) Biophys. J. , vol.84 , pp. 2467-2473
    • Amit, R.1    Oppenheim, A.B.2    Stavans, J.3
  • 2
    • 0030972952 scopus 로고    scopus 로고
    • H-NS: a modulator of environmentally regulated gene expression
    • Atlung, t., and H. Ingmer. 1997. H-NS: a modulator of environmentally regulated gene expression. Mol. Microbiol. 24:7-17.
    • (1997) Mol. Microbiol. , vol.24 , pp. 7-17
    • Atlung, T.1    Ingmer, H.2
  • 3
    • 0041673353 scopus 로고    scopus 로고
    • The rotary motor of bacterial flagella
    • Berg, H. C. 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
  • 4
    • 0032960155 scopus 로고    scopus 로고
    • Torque generated by the flagellar motor of Escherichia coli while driven backward
    • Berry, R. M., and H. C. Berg. 1999. Torque generated by the flagellar motor of Escherichia coli while driven backward. Biophys. J. 76:580-587.
    • (1999) Biophys. J. , vol.76 , pp. 580-587
    • Berry, R.M.1    Berg, H.C.2
  • 5
    • 0027979044 scopus 로고
    • The H-NS protein is involved in the biogenesis of flagella in Escherichia coli
    • Bertin, P., et al. 1994. The H-NS protein is involved in the biogenesis of flagella in Escherichia coli. J. Bacteriol. 176:5537-5540.
    • (1994) J. Bacteriol. , vol.176 , pp. 5537-5540
    • Bertin, P.1
  • 6
    • 0025058346 scopus 로고
    • The MotA protein of E. coli is a protonconducting component of the flagellar motor
    • Blair, D. F., and H. C. Berg. 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
  • 7
    • 0024295536 scopus 로고
    • Restoration of torque in defective flagellar motors
    • Blair, D. F., and H. C. Berg. 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
    • 0037336248 scopus 로고    scopus 로고
    • The H-NS dimerization domain defines a new fold contributing to DNA recognition
    • Bloch, V., et al. 2003. The H-NS dimerization domain defines a new fold contributing to DNA recognition. Nat. Struct. Biol. 10:212-218.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 212-218
    • Bloch, V.1
  • 9
    • 0021280816 scopus 로고
    • Successive incorporation of forcegenerating units in the bacterial rotary motor
    • Block, S. M., and H. C. Berg. 1984. Successive incorporation of forcegenerating 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
  • 10
    • 77950928649 scopus 로고    scopus 로고
    • Second messenger-mediated adjustment of bacterial swimming velocity
    • Boehm, A., et al. 2010. Second messenger-mediated adjustment of bacterial swimming velocity. Cell 141:107-116.
    • (2010) Cell , vol.141 , pp. 107-116
    • Boehm, A.1
  • 11
    • 0036646105 scopus 로고    scopus 로고
    • Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliG
    • Brown, P. N., C. P. Hill, and D. F. Blair. 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
  • 12
    • 16844367441 scopus 로고    scopus 로고
    • Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima
    • Brown, P. N., M. A. A. Mathews, L. A. Joss, C. P. Hill, and D. F. Blair. 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.A.2    Joss, L.A.3    Hill, C.P.4    Blair, D.F.5
  • 13
    • 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, P. N., M. Terrazas, K. Paul, and D. F. Blair. 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
  • 14
    • 0034444676 scopus 로고    scopus 로고
    • Coupling of flagellar gene expression to flagellar assembly in Salmonella enterica serovar Typhimurium and Escherichia coli
    • Chilcott, G. S., and K. T. Hughes. 2000. Coupling of flagellar gene expression to flagellar assembly in Salmonella enterica serovar Typhimurium and Escherichia coli. Microbiol. Mol. Biol. Rev. 64:694-708.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 694-708
    • Chilcott, G.S.1    Hughes, K.T.2
  • 15
    • 0032508717 scopus 로고    scopus 로고
    • Enhanced binding of altered H-NS protein to flagellar rotor protein FliG causes increased flagellar rotational speed and hypermotility in Escherichia coli
    • Donato, G. M., and T. H. Kawula. 1998. Enhanced binding of altered H-NS protein to flagellar rotor protein FliG causes increased flagellar rotational speed and hypermotility in Escherichia coli. J. Biol. Chem. 273:24030-24036.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24030-24036
    • Donato, G.M.1    Kawula, T.H.2
  • 16
    • 77952813357 scopus 로고    scopus 로고
    • A post-translational, c-di-GMP-dependent mechanism regulating flagellar motility
    • Fang, X., and M. Gomelsky. 2010. A post-translational, c-di-GMP-dependent mechanism regulating flagellar motility. Mol. Microbiol. 76:1295-1305.
    • (2010) Mol. Microbiol. , vol.76 , pp. 1295-1305
    • Fang, X.1    Gomelsky, M.2
  • 17
    • 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., V. M. Irikura, S. Yamaguchi, D. J. DeRosier, and R. M. Macnab. 1992. Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-ring face of the basal body. Proc. Natl. Acad. Sci. U. S. A. 89:6304-6308.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 6304-6308
    • Francis, N.R.1    Irikura, V.M.2    Yamaguchi, S.3    DeRosier, D.J.4    Macnab, R.M.5
  • 18
    • 0028274712 scopus 로고
    • Isolation, characterization and structure of bacterial flagellar motors containing the switch complex
    • Francis, N. R., G. E. Sosinsky, D. Thomas, and D. J. DeRosier. 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
  • 19
    • 0017835741 scopus 로고
    • The proton pump is a molecular engine of motile bacteria
    • Glagolev, A. N., and V. P. Skulachev. 1978. The proton pump is a molecular engine of motile bacteria. Nature 272:280-282.
    • (1978) Nature , vol.272 , pp. 280-282
    • Glagolev, A.N.1    Skulachev, V.P.2
  • 20
    • 0028147156 scopus 로고
    • Bees aren't the only ones: swarming in Gram-negative bacteria
    • Harshey, R. M. 1994. Bees aren't the only ones: swarming in Gram-negative bacteria. Mol. Microbiol. 13:389-394.
    • (1994) Mol. Microbiol. , vol.13 , pp. 389-394
    • Harshey, R.M.1
  • 22
    • 0027407375 scopus 로고
    • Salmonella typhimurium fliG and fliN mutations causing defects in assembly, rotation, and switching of the flagellar motor
    • Irikura, V. M., M. Kihara, S. Yamaguchi, H. Sockett, and R. M. Macnab. 1993. Salmonella typhimurium fliG and fliN mutations causing defects in assembly, rotation, and switching of the flagellar motor. J. Bacteriol. 175:802-810.
    • (1993) J. Bacteriol. , vol.175 , pp. 802-810
    • Irikura, V.M.1    Kihara, M.2    Yamaguchi, S.3    Sockett, H.4    Macnab, R.M.5
  • 23
    • 0035078382 scopus 로고    scopus 로고
    • Heteromeric interactions among nucleoid-associated bacterial proteins: localization of Stp-A stabilizing regions in H-NS of Escherichia coli
    • Johansson, J., S. Eriksson, B. Sonden, S. N. Wai, and B. E. Uhlin. 2001. Heteromeric interactions among nucleoid-associated bacterial proteins: localization of Stp-A stabilizing regions in H-NS of Escherichia coli. J. Bacteriol. 183:2343-2347.
    • (2001) J. Bacteriol. , vol.183 , pp. 2343-2347
    • Johansson, J.1    Eriksson, S.2    Sonden, B.3    Wai, S.N.4    Uhlin, B.E.5
  • 24
    • 0032825041 scopus 로고    scopus 로고
    • Differential protease-mediated turnover of H-NS and StpA revealed by a mutation altering protein stability and stationary-phase survival of Escherichia coli
    • Johansson, J., and B. E. Uhlin. 1999. Differential protease-mediated turnover of H-NS and StpA revealed by a mutation altering protein stability and stationary-phase survival of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 96:10776-10781.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10776-10781
    • Johansson, J.1    Uhlin, B.E.2
  • 25
    • 0023750050 scopus 로고
    • Effects of mot gene expression on the structure of the flagellar motor
    • Khan, S., M. Dapice, and T. S. Reese. 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
  • 26
    • 0034721950 scopus 로고    scopus 로고
    • Two novel flagellar components and H-NS are involved in the motor function of Escherichia coli
    • Ko, M., and C. Park. 2000. Two novel flagellar components and H-NS are involved in the motor function of Escherichia coli. J. Mol. Biol. 303:371-382.
    • (2000) J. Mol. Biol. , vol.303 , pp. 371-382
    • Ko, M.1    Park, C.2
  • 27
    • 0018780595 scopus 로고
    • Electrolyte effects on the activity of mutant enzymes in vivo and in vitro
    • Kohno, T., and J. R. Roth. 1979. Electrolyte effects on the activity of mutant enzymes in vivo and in vitro. Biochemistry 18:1386-1392.
    • (1979) Biochemistry , vol.18 , pp. 1386-1392
    • Kohno, T.1    Roth, J.R.2
  • 28
    • 0035980267 scopus 로고    scopus 로고
    • Conformational change in the stator of the bacterial flagellar motor
    • Kojima, S., and D. F. Blair. 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
  • 29
    • 0347357933 scopus 로고    scopus 로고
    • Solubilization and purification of the MotA/MotB complex of Escherichia coli
    • Kojima, S., and D. F. Blair. 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
  • 30
    • 0016219080 scopus 로고
    • Chemomechanical coupling without ATP: the source of energy for motility and chemotaxis in bacteria
    • Larsen, S. H., J. Adler, J. J. Gargus, and R. W. Hogg. 1974. Chemomechanical coupling without ATP: the source of energy for motility and chemotaxis in bacteria. Proc. Natl. Acad. Sci. U. S. A. 71:1239-1243.
    • (1974) Proc. Natl. Acad. Sci. U. S. A. , vol.71 , pp. 1239-1243
    • Larsen, S.H.1    Adler, J.2    Gargus, J.J.3    Hogg, R.W.4
  • 31
    • 77955924240 scopus 로고    scopus 로고
    • Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching
    • Lee, L. K., M. A. Ginsburg, C. Crovace, M. Donohoe, and D. Stock. 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
  • 32
    • 79955733488 scopus 로고    scopus 로고
    • Assembly and stability of flagellar motor in Escherichia coli
    • Li, H., and V. Sourjik. 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
  • 33
    • 76749118994 scopus 로고    scopus 로고
    • A divalent switch drives H-NS/DNA-binding conformations between stiffening and bridging modes
    • Liu, Y., H. Chen, L. J. Kenney, and J. Yan. 2010. A divalent switch drives H-NS/DNA-binding conformations between stiffening and bridging modes. Genes Dev. 24:339-344.
    • (2010) Genes Dev. , vol.24 , pp. 339-344
    • Liu, Y.1    Chen, H.2    Kenney, L.J.3    Yan, J.4
  • 34
    • 0031557399 scopus 로고    scopus 로고
    • Charged residues of the rotor protein FliG essential for torque generation in the flagellar motor of Escherichia coli
    • Lloyd, S. A., and D. F. Blair. 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
  • 35
    • 0030066344 scopus 로고    scopus 로고
    • Torque generation in the flagellar motor of Escherichia coli: evidence of a direct role for FliG but not for FliM or FliN
    • Lloyd, S. A., H. Tang, X. Wang, S. Billings, and D. F. Blair. 1996. Torque generation in the flagellar motor of Escherichia coli: evidence of a direct role for FliG but not for FliM or FliN. J. Bacteriol. 178:223-231.
    • (1996) J. Bacteriol. , vol.178 , pp. 223-231
    • Lloyd, S.A.1    Tang, H.2    Wang, X.3    Billings, S.4    Blair, D.F.5
  • 36
    • 23644449903 scopus 로고    scopus 로고
    • FliG subunit arrangement in the flagellar rotor probed by targeted cross-linking
    • Lowder, B. J., M. D. Duyvesteyn, and D. F. Blair. 2005. FliG subunit arrangement in the flagellar rotor probed by targeted cross-linking. J. Bacteriol. 187:5640-5647.
    • (2005) J. Bacteriol. , vol.187 , pp. 5640-5647
    • Lowder, B.J.1    Duyvesteyn, M.D.2    Blair, D.F.3
  • 37
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab, R. M. 2003. How bacteria assemble flagella. Annu. Rev. Microbiol. 57:77-100.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 77-100
    • Macnab, R.M.1
  • 38
    • 0029932448 scopus 로고    scopus 로고
    • Interacting components of the flagellar motor of Escherichia coli revealed by the two-hybrid system in yeast
    • Marykwas, D. L., S. A. Schmidt, and H. C. Berg. 1996. Interacting components of the flagellar motor of Escherichia coli revealed by the two-hybrid system in yeast. J. Mol. Biol. 256:564-576.
    • (1996) J. Mol. Biol. , vol.256 , pp. 564-576
    • Marykwas, D.L.1    Schmidt, S.A.2    Berg, H.C.3
  • 39
    • 0031771710 scopus 로고    scopus 로고
    • Domain analysis of the FliM protein of Escherichia coli
    • Mathews, M. A. A., H. L. Tang, and D. F. Blair. 1998. Domain analysis of the FliM protein of Escherichia coli. J. Bacteriol. 180:5580-5590.
    • (1998) J. Bacteriol. , vol.180 , pp. 5580-5590
    • Mathews, M.A.A.1    Tang, H.L.2    Blair, D.F.3
  • 40
    • 79958063382 scopus 로고    scopus 로고
    • Structural insight into the rotational switching mechanism of the bacterial flagellar motor
    • Minamino, T., et al. 2011. Structural insight into the rotational switching mechanism of the bacterial flagellar motor. PLoS Biol. 9:e1000616.
    • (2011) PLoS Biol. , vol.9
    • Minamino, T.1
  • 41
    • 33747063575 scopus 로고    scopus 로고
    • Structure of FliM provides insight into assembly of the switch complex in the bacterial flagella motor
    • Park, S. Y., B. Lowder, A. M. Bilwes, D. F. Blair, and B. R. Crane. 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
  • 42
    • 33645233315 scopus 로고    scopus 로고
    • Organization of FliN subunits in the flagellar motor of E
    • Paul, K., and D. F. Blair. 2006. Organization of FliN subunits in the flagellar motor of E. coli. J. Bacteriol. 188:2502-2511.
    • (2006) coli. J. Bacteriol. , vol.188 , pp. 2502-2511
    • Paul, K.1    Blair, D.F.2
  • 44
    • 33745930219 scopus 로고    scopus 로고
    • Mutational analysis of the flagellar rotor protein FliN: identification of surfaces important for flagellar assembly and switching
    • Paul, K., J. Harmon, and D. F. Blair. 2006. Mutational analysis of the flagellar rotor protein FliN: identification of surfaces important for flagellar assembly and switching. J. Bacteriol. 188:5240-5248.
    • (2006) J. Bacteriol. , vol.188 , pp. 5240-5248
    • Paul, K.1    Harmon, J.2    Blair, D.F.3
  • 45
    • 77950370030 scopus 로고    scopus 로고
    • The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism
    • Paul, K., V. M. Nieto, W. Carlquist, D. F. Blair, and R. M. Harshey. 2010. The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism. Mol. Cell 38:128-139.
    • (2010) Mol. Cell , vol.38 , pp. 128-139
    • Paul, K.1    Nieto, V.M.2    Carlquist, W.3    Blair, D.F.4    Harshey, R.M.5
  • 46
    • 33744476417 scopus 로고    scopus 로고
    • The maximum number of torque-generating units in the flagellar motor of Escherichia coli is at least 11
    • Reid, S. W., et al. 2006. The maximum number of torque-generating units in the flagellar motor of Escherichia coli is at least 11. Proc. Natl. Acad. Sci. U. S. A. 103:8066-8071.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 8066-8071
    • Reid, S.W.1
  • 47
    • 1842453825 scopus 로고    scopus 로고
    • Structure of the histone-like protein H-NS and its role in regulation and genome superstructure
    • Rimsky, S. 2004. Structure of the histone-like protein H-NS and its role in regulation and genome superstructure. Curr. Opin. Microbiol. 7:109-114.
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 109-114
    • Rimsky, S.1
  • 48
    • 77952679686 scopus 로고    scopus 로고
    • Chemotaxis signaling protein CheY binds to the rotor protein FliN to control the direction of flagellar rotation in Escherichia coli
    • Sarkar, M. K., K. Paul, and D. Blair. 2010. Chemotaxis signaling protein CheY binds to the rotor protein FliN to control the direction of flagellar rotation in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 107:9370-9375.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 9370-9375
    • Sarkar, M.K.1    Paul, K.2    Blair, D.3
  • 49
    • 73649145486 scopus 로고    scopus 로고
    • Subunit organization and reversal-associated movements in the flagellar switch of Escherichia coli
    • Sarkar, M. K., K. Paul, and D. F. Blair. 2010. Subunit organization and reversal-associated movements in the flagellar switch of Escherichia coli. J. Biol. Chem. 285:675-684.
    • (2010) J. Biol. Chem. , vol.285 , pp. 675-684
    • Sarkar, M.K.1    Paul, K.2    Blair, D.F.3
  • 50
    • 0034051670 scopus 로고    scopus 로고
    • +-driven polar flagellar motor component of Vibrio alginolyticus
    • +-driven polar flagellar motor component of Vibrio alginolyticus. J. Biol. Chem. 275:5718-5722.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5718-5722
    • Sato, K.1    Homma, M.2
  • 51
    • 0028900971 scopus 로고
    • Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli
    • Shindo, H., et al. 1995. Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli. FEBS Lett. 360:125-131.
    • (1995) FEBS Lett. , vol.360 , pp. 125-131
    • Shindo, H.1
  • 52
    • 0026541539 scopus 로고
    • Molecular analysis of the flagellar switch protein FliM of Salmonella typhimurium
    • Sockett, H., S. Yamaguchi, M. Kihara, V. M. Irikura, and R. M. Macnab. 1992. Molecular analysis of the flagellar switch protein FliM of Salmonella typhimurium. J. Bacteriol. 174:793-806.
    • (1992) J. Bacteriol. , vol.174 , pp. 793-806
    • Sockett, H.1    Yamaguchi, S.2    Kihara, M.3    Irikura, V.M.4    Macnab, R.M.5
  • 53
    • 0032796421 scopus 로고    scopus 로고
    • Multiple control of flagellum biosynthesis in Escherichia coli: role of H-NS protein and the cyclic AMP-catabolite activator protein complex in transcription of the flhDC master operon
    • Soutourina, O., et al. 1999. Multiple control of flagellum biosynthesis in Escherichia coli: role of H-NS protein and the cyclic AMP-catabolite activator protein complex in transcription of the flhDC master operon. J. Bacteriol. 181:7500-7508.
    • (1999) J. Bacteriol. , vol.181 , pp. 7500-7508
    • Soutourina, O.1
  • 54
    • 1442326719 scopus 로고    scopus 로고
    • Structure of the rotor of the bacterial flagellar motor revealed by electron cryo-microscopy and singleparticle image analysis
    • Suzuki, H., K. Yonekura, and K. Namba. 2004. Structure of the rotor of the bacterial flagellar motor revealed by electron cryo-microscopy 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
  • 55
    • 0029009964 scopus 로고
    • Regulated underexpression and overexpression of the FliN protein of Escherichia coli and evidence for an interaction between FliN and FliM in the flagellar motor
    • Tang, H., S. Billings, X. Wang, L. Sharp, and D. F. Blair. 1995. Regulated underexpression and overexpression of the FliN protein of Escherichia coli and evidence for an interaction between FliN and FliM in the flagellar motor. J. Bacteriol. 177:3496-3503.
    • (1995) J. Bacteriol. , vol.177 , pp. 3496-3503
    • Tang, H.1    Billings, S.2    Wang, X.3    Sharp, L.4    Blair, D.F.5
  • 56
    • 0029070133 scopus 로고
    • Regulated underexpression of the FliM protein of Escherichia coli and evidence for a location in the flagellar motor distinct from the MotA/MotB torque generators
    • Tang, H., and D. F. Blair. 1995. Regulated underexpression of the FliM protein of Escherichia coli and evidence for a location in the flagellar motor distinct from the MotA/MotB torque generators. J. Bacteriol. 177:3485-3495.
    • (1995) J. Bacteriol. , vol.177 , pp. 3485-3495
    • Tang, H.1    Blair, D.F.2
  • 57
    • 0030590217 scopus 로고    scopus 로고
    • Motility protein complexes in the bacterial flagellar motor
    • Tang, H., T. F. Braun, and D. F. Blair. 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
  • 58
    • 33749608423 scopus 로고    scopus 로고
    • The threedimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar Typhimurium
    • Thomas, D. R., N. R. Francis, C. Xu, and D. J. DeRosier. 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    Xu, C.3    DeRosier, D.J.4
  • 59
    • 0033621062 scopus 로고    scopus 로고
    • Rotational symmetry of the C ring and a mechanism for the flagellar rotary motor
    • Thomas, D. R., D. G. Morgan, and D. J. DeRosier. 1999. Rotational symmetry of the C ring and a mechanism for the flagellar rotary motor. Proc. Natl. Acad. Sci. U. S. A. 96:10134-10139.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10134-10139
    • Thomas, D.R.1    Morgan, D.G.2    DeRosier, D.J.3
  • 60
    • 0030601826 scopus 로고    scopus 로고
    • Systematic mutational analysis revealing the functional domain organization of Escherichia coli nucleoid protein H-NS
    • Ueguchi, C., T. Suzuki, T. Yoshida, K. Tanaka, and T. Mizuno. 1996. Systematic mutational analysis revealing the functional domain organization of Escherichia coli nucleoid protein H-NS. J. Mol. Biol. 263:149-162.
    • (1996) J. Mol. Biol. , vol.263 , pp. 149-162
    • Ueguchi, C.1    Suzuki, T.2    Yoshida, T.3    Tanaka, K.4    Mizuno, T.5
  • 61
    • 0027517812 scopus 로고
    • Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria
    • Welch, M., K. Oosawa, S.-I. Aizawa, and M. Eisenbach. 1993. Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. Proc. Natl. Acad. Sci. U. S. A. 90:8787-8791.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 8787-8791
    • Welch, M.1    Oosawa, K.2    Aizawa, S.-I.3    Eisenbach, M.4
  • 62
    • 63449108030 scopus 로고    scopus 로고
    • Genome-wide identification of H-NS-controlled, temperature-regulated genes in Escherichia coli K-12
    • White-Ziegler, C., and T. R. Davis. 2009. Genome-wide identification of H-NS-controlled, temperature-regulated genes in Escherichia coli K-12. J. Bacteriol. 191:1106-1110.
    • (2009) J. Bacteriol. , vol.191 , pp. 1106-1110
    • White-Ziegler, C.1    Davis, T.R.2
  • 63
    • 0031573039 scopus 로고    scopus 로고
    • Molecular aspects of the Escherichia coli nucleoid protein, H-HS: a central controller of gene regulatory networks
    • Williams, R. M., and S. Rimsky. 1997. Molecular aspects of the Escherichia coli nucleoid protein, H-HS: a central controller of gene regulatory networks. FEMS Microbiol. Lett. 156:175-185.
    • (1997) FEMS Microbiol. Lett. , vol.156 , pp. 175-185
    • Williams, R.M.1    Rimsky, S.2
  • 65
    • 0022899744 scopus 로고
    • Genetic evidence for a switching and energytransducing complex in the flagellar motor of Salmonella typhimurium
    • Yamaguchi, S., et al. 1986. Genetic evidence for a switching and energytransducing complex in the flagellar motor of Salmonella typhimurium. J. Bacteriol. 168:1172-1179.
    • (1986) J. Bacteriol. , vol.168 , pp. 1172-1179
    • Yamaguchi, S.1
  • 66
    • 12244302174 scopus 로고    scopus 로고
    • Variable symmetry in Salmonella typhimurium flagellar motors
    • Young, H. S., H. Dang, Y. Lai, D. J. DeRosier, and S. Khan. 2003. Variable symmetry in Salmonella typhimurium flagellar motors. Biophys. J. 84:571-577.
    • (2003) Biophys. J. , vol.84 , pp. 571-577
    • Young, H.S.1    Dang, H.2    Lai, Y.3    DeRosier, D.J.4    Khan, S.5
  • 67
    • 0030069386 scopus 로고    scopus 로고
    • FliG and FliM distribution in the Salmonella typhimurium cell and flagellar basal bodies
    • Zhao, R., C. D. Amsler, P. Matsumura, and S. Khan. 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
  • 68
    • 0030776508 scopus 로고    scopus 로고
    • Residues of the cytoplasmic domain of MotA essential for torque generation in the bacterial flagellar motor
    • Zhou, J., and D. F. Blair. 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
  • 69
    • 0032568636 scopus 로고    scopus 로고
    • Electrostatic interactions between rotor and stator in the bacterial flagellar motor
    • Zhou, J., S. A. Lloyd, and D. F. Blair. 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
  • 70
    • 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., et al. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.