메뉴 건너뛰기




Volumn 51, Issue 25, 2012, Pages 5052-5060

Structural insights into the interaction between the bacterial flagellar motor proteins FliF and FliG

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL FLAGELLAR; BACTERIAL FLAGELLUM; CONFORMATIONAL CHANGE; CYTOPLASMIC PROTEINS; HETERODIMERIC COMPLEXES; HYDROPHOBIC PATCH; INTERACTION SITE; N-TERMINAL DOMAINS; NANOMOLAR RANGE; NMR DATA; OLIGOMERIC STATE; ROTATIONAL DIRECTIONS; STRUCTURAL INSIGHTS; THERMOTOGA MARITIMA; TRANS-MEMBRANE PROTEINS; TRANSMEMBRANES; UPPER BOUND;

EID: 84862904491     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3004582     Document Type: Article
Times cited : (37)

References (45)
  • 1
    • 0041673353 scopus 로고    scopus 로고
    • The rotary motor of bacterial flagella
    • DOI 10.1146/annurev.biochem.72.121801.161737
    • Berg, H. C. (2003) The rotary motor of bacterial flagella Annu. Rev. Biochem. 72, 19-54 (Pubitemid 36930440)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 19-54
    • Berg, H.C.1
  • 2
    • 52649147435 scopus 로고    scopus 로고
    • Bacterial flagellar motor
    • Sowa, Y. and Berry, R. M. (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
    • 0025272595 scopus 로고
    • Stoichiometric analysis of the flagellar hook-(basal-body) complex of Salmonella typhimurium
    • Jones, C. J., Macnab, R. M., Okino, H., and Aizawa, S.-I. (1990) Stoichiometric analysis of the flagellar hook-(basal-body) complex of Salmonella typhimurium J. Mol. Biol. 212, 377-387 (Pubitemid 20130735)
    • (1990) Journal of Molecular Biology , vol.212 , Issue.2 , pp. 377-387
    • Jones, C.J.1    Macnab, R.M.2    Okino, H.3    Aizawa, S.-I.4
  • 4
    • 0030069386 scopus 로고    scopus 로고
    • FliG and FliM distribution in the Salmonella typhimurium cell and flagellar basal bodies
    • Zhao, R., Amsler, C. D., Matsumura, P., and Khan, S. (1996) FliG and FliM distribution in the Salmonella typhimurium cell and flagellar basal bodies J. Bacteriol. 178, 258-265 (Pubitemid 26006088)
    • (1996) Journal of Bacteriology , vol.178 , Issue.1 , pp. 258-265
    • Zhao, R.1    Amsler, C.D.2    Matsumura, P.3    Khan, S.4
  • 6
    • 33749608423 scopus 로고    scopus 로고
    • The three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar typhimurium
    • DOI 10.1128/JB.00552-06
    • Thomas, D. R., Francis, N. R., Xu, C., and DeRosier, D. J. (2006) The three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar Typhimurium J. Bacteriol. 188, 7039-7048 (Pubitemid 44547609)
    • (2006) Journal of Bacteriology , vol.188 , Issue.20 , pp. 7039-7048
    • Thomas, D.R.1    Francis, N.R.2    Xu, C.3    DeRosier, D.J.4
  • 7
    • 0030590265 scopus 로고    scopus 로고
    • FliN is a major structural protein of the C-ring in the Salmonella typhimurium flagellar basal body
    • DOI 10.1006/jmbi.1996.0452
    • Zhao, R., Pathak, N., Jaffe, H., Reese, T. S., and Khan, S. (1996) FliN is a major structural protein of the C-ring in the Salmonella typhimurium flagellar basal body J. Mol. Biol. 261, 195-208 (Pubitemid 26275802)
    • (1996) Journal of Molecular Biology , vol.261 , Issue.2 , pp. 195-208
    • Zhao, R.1    Pathak, N.2    Jaffe, H.3    Reese, T.S.4    Khan, S.5
  • 8
    • 16844367441 scopus 로고    scopus 로고
    • Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima
    • DOI 10.1128/JB.187.8.2890-2902.2005
    • Brown, P. N., Mathews, M. A. A., Joss, L. A., Hill, C. P., and Blair, D. F. (2005) Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima J. Bacteriol. 187, 2890-2902 (Pubitemid 40490393)
    • (2005) Journal of Bacteriology , vol.187 , Issue.8 , pp. 2890-2902
    • Brown, P.N.1    Mathews, M.A.A.2    Joss, L.A.3    Hill, C.P.4    Blair, D.F.5
  • 9
    • 0034079196 scopus 로고    scopus 로고
    • Deletion analysis of the flagellar switch protein FliG of Salmonella
    • DOI 10.1128/JB.182.11.3022-3028.2000
    • Kihara, M., Miller, G. U., and Macnab, R. M. (2000) Deletion analysis of the flagellar switch protein FliG of Salmonella J. Bacteriol. 182, 3022-3028 (Pubitemid 30326914)
    • (2000) Journal of Bacteriology , vol.182 , Issue.11 , pp. 3022-3028
    • Kihara, M.1    Miller, G.U.2    Macnab, R.M.3
  • 10
    • 0036646105 scopus 로고    scopus 로고
    • Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliG
    • DOI 10.1093/emboj/cdf332
    • Brown, P. N., Hill, C. P., and Blair, D. F. (2002) Crystal structure of the middle and C-terminal domains of the flagellar rotor protein FliG EMBO J. 21, 3225-3234 (Pubitemid 34760555)
    • (2002) EMBO Journal , vol.21 , Issue.13 , pp. 3225-3234
    • Brown, P.N.1    Hill, C.P.2    Blair, D.F.3
  • 11
    • 0031557399 scopus 로고    scopus 로고
    • Charged residues of the rotor protein FliG essential for torque generation in the flagellar motor of Escherichia coli
    • DOI 10.1006/jmbi.1996.0836
    • Lloyd, S. A. and Blair, D. F. (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 (Pubitemid 27113213)
    • (1997) Journal of Molecular Biology , vol.266 , Issue.4 , pp. 733-744
    • Lloyd, S.A.1    Blair, D.F.2
  • 12
    • 0026541539 scopus 로고
    • Molecular analysis of the flagellar switch protein FliM of Salmonella typhimurium
    • Sockett, H., Yamaguchi, S., Kihara, M., Irikura, V. M., and Macnab, R. M. (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
  • 13
    • 0029913699 scopus 로고    scopus 로고
    • A mutational analysis of the interaction between FliG and FliM, two components of the flagellar motor of Escherichia coli
    • Marykwas, D. L. and Berg, H. C. (1996) A mutational analysis of the interaction between FliG and FliM, two components of the flagellar motor of Escherichia coli J. Bacteriol. 178, 1289-1294 (Pubitemid 26073384)
    • (1996) Journal of Bacteriology , vol.178 , Issue.5 , pp. 1289-1294
    • Marykwas, D.L.1    Berg, H.C.2
  • 14
    • 63649154351 scopus 로고    scopus 로고
    • A molecular mechanism of bacterial flagellar motor switching
    • Dyer, C. M., Vartanian, A. S., Zhou, H., and Dahlquist, F. W. (2009) A molecular mechanism of bacterial flagellar motor switching J. Mol. Biol. 388, 71-84
    • (2009) J. Mol. Biol. , vol.388 , pp. 71-84
    • Dyer, C.M.1    Vartanian, A.S.2    Zhou, H.3    Dahlquist, F.W.4
  • 15
    • 77955924240 scopus 로고    scopus 로고
    • Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching
    • Lee, L. K., Ginsburg, M. A., Crovace, C., Donohoe, M., and 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
  • 17
    • 80054722813 scopus 로고    scopus 로고
    • A molecular mechanism of direction switching in the flagellar motor of Escherichia coli
    • Paul, K., Brunstetter, D., Titen, S., and Blair, D. F. (2011) A molecular mechanism of direction switching in the flagellar motor of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 108, 17171-17176
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 17171-17176
    • Paul, K.1    Brunstetter, D.2    Titen, S.3    Blair, D.F.4
  • 18
    • 33745930219 scopus 로고    scopus 로고
    • Mutational analysis of the flagellar rotor protein FliN: Identification of surfaces important for flagellar assembly and switching
    • DOI 10.1128/JB.00110-06
    • Paul, K., Harmon, J. G., and Blair, D. F. (2006) Mutational analysis of the flagellar rotor protein FliN: Identification of surfaces important for flagellar assembly and switching J. Bacteriol. 188, 5240-5248 (Pubitemid 44051490)
    • (2006) Journal of Bacteriology , vol.188 , Issue.14 , pp. 5240-5248
    • Paul, K.1    Harmon, J.G.2    Blair, D.F.3
  • 19
    • 73649145486 scopus 로고    scopus 로고
    • Subunit organization and reversal-associated movements in the flagellar switch of Escherichia coli
    • Sarkar, M. K., Paul, K., and Blair, D. F. (2010) Subunit organization and reversal-associated movements in the flagellar switch of Escherichia coli J. Biol. Chem. 285, 675
    • (2010) J. Biol. Chem. , vol.285 , pp. 675
    • Sarkar, M.K.1    Paul, K.2    Blair, D.F.3
  • 20
    • 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
  • 21
    • 2642559479 scopus 로고    scopus 로고
    • Self-assembly and type III protein export of the bacterial flagellum
    • DOI 10.1159/000077865
    • Minamino, T. and Namba, K. (2004) Self-assembly and type III protein export of the bacterial flagellum J. Mol. Microbiol. Biotechnol. 7, 5-17 (Pubitemid 38721126)
    • (2004) Journal of Molecular Microbiology and Biotechnology , vol.7 , Issue.1-2 , pp. 5-17
    • Minamino, T.1    Namba, K.2
  • 22
    • 0026752989 scopus 로고
    • Morphological pathway of flagellar assembly in Salmonella typhimurium
    • Kubori, T., Shimamoto, N., Yamaguchi, S., Namba, K., and Aizawa, S.-I. (1992) Morphological pathway of flagellar assembly in Salmonella typhimurium J. Mol. Biol. 226, 433-446
    • (1992) J. Mol. Biol. , vol.226 , pp. 433-446
    • Kubori, T.1    Shimamoto, N.2    Yamaguchi, S.3    Namba, K.4    Aizawa, S.-I.5
  • 23
    • 33646435299 scopus 로고    scopus 로고
    • Interactions between C ring proteins and export apparatus components: A possible mechanism for facilitating type III protein export
    • González-Pedrajo, B., Minamino, T., Kihara, M., and Namba, K. (2006) Interactions between C ring proteins and export apparatus components: A possible mechanism for facilitating type III protein export Mol. Microbiol. 60, 984-998
    • (2006) Mol. Microbiol. , vol.60 , pp. 984-998
    • González-Pedrajo, B.1    Minamino, T.2    Kihara, M.3    Namba, K.4
  • 24
    • 0029932448 scopus 로고    scopus 로고
    • Interacting components of the flagellar motor of Escherichia coli revealed by the two-hybrid system in yeast
    • DOI 10.1006/jmbi.1996.0109
    • Marykwas, D. L., Schmidt, S. A., and Berg, H. C. (1996) Interacting components of the flagellar motor of Escherichia coli revealed by the two-hybrid system in yeast J. Mol. Biol. 256, 564-576 (Pubitemid 26107206)
    • (1996) Journal of Molecular Biology , vol.256 , Issue.3 , pp. 564-576
    • Marykwas, D.L.1    Schmidt, S.A.2    Berg, H.C.3
  • 25
    • 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., Irikuvra, V. M., Yamaguchi, S., DeRosier, D. J., and Macnab, R. M. (1992) Localization of the Salmonella typhimurium flagellar switch protein FliG to the cytoplasmic M-Ring face of the basal body Proc. Natl. Acad. Sci. U.S.A. 89, 6304-6308
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6304-6308
    • Francis, N.R.1    Irikuvra, V.M.2    Yamaguchi, S.3    Derosier, D.J.4    MacNab, R.M.5
  • 26
    • 0035681962 scopus 로고    scopus 로고
    • Structures of bacterial flagellar motors from two FliF-FliG gene fusion mutants
    • DOI 10.1128/JB.183.21.6404-6412.2001
    • Thomas, D., Morgan, D. G., and DeRosier, D. J. (2001) Structures of bacterial flagellar motors from two FliF-FliG gene fusion mutants J. Bacteriol. 183, 6404-6412 (Pubitemid 34059414)
    • (2001) Journal of Bacteriology , vol.183 , Issue.21 , pp. 6404-6412
    • Thomas, D.1    Morgan, D.G.2    DeRosier, D.J.3
  • 27
    • 0037373067 scopus 로고    scopus 로고
    • Role of the cytoplasmic C terminus of the FliF motor protein in flagellar assembly and rotation
    • DOI 10.1128/JB.185.5.1624-1633.2003
    • Grunenfelder, B., Gehrig, S., and Jenal, U. (2003) Role of the cytoplasmic C terminus of the FliF motor protein in flagellar assembly and rotation J. Bacteriol. 185, 1624-1633 (Pubitemid 36245965)
    • (2003) Journal of Bacteriology , vol.185 , Issue.5 , pp. 1624-1633
    • Grunenfelder, B.1    Gehrig, S.2    Jena, U.3
  • 28
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the α- And β-carbon resonances in proteins
    • Wittekind, M. and Mueller, L. (1993) HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the α- and β-carbon resonances in proteins J. Magn. Reson., Ser. B 101, 201-205
    • (1993) J. Magn. Reson., Ser. B , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 29
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram, D. R. and Kay, L. E. (1994) Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity J. Magn. Reson., Ser. B 103, 203-216
    • (1994) J. Magn. Reson., Ser. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 30
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek, S. and Bax, A. (1992) Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR J. Am. Chem. Soc. 114, 6291-6293
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 32
    • 0032840124 scopus 로고    scopus 로고
    • Improved lineshape and sensitivity in the HNCO-family of triple resonance experiments
    • DOI 10.1023/A:1008381929212
    • Yang, D. and Kay, L. (1999) Improved lineshape and sensitivity in the HNCO-family of triple resonance experiments J. Biomol. NMR 14, 273-276 (Pubitemid 29396485)
    • (1999) Journal of Biomolecular NMR , vol.14 , Issue.3 , pp. 273-276
    • Yang, D.1    Kay, L.E.2
  • 33
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 34
    • 0001250026 scopus 로고
    • 1H 2D NMR spectra by interactive computer graphics
    • 1H 2D NMR spectra by interactive computer graphics J. Magn. Reson. 84, 627-633
    • (1989) J. Magn. Reson. , vol.84 , pp. 627-633
    • Kraulis, P.1
  • 38
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D. S., Sykes, B. D., and Richards, F. M. (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure J. Mol. Biol. 222, 311-333 (Pubitemid 121004009)
    • (1991) Journal of Molecular Biology , vol.222 , Issue.2 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 39
    • 0027407375 scopus 로고
    • Salmonella typhimurium fliG and fliN mutations causing defects in assembly, rotation, and switching of the flagellar motor
    • Irikura, V. M., Kihara, M., Yamaguchi, S., Sockett, H., and Macnab, R. M. (1993) Salmonella typhimurium fliG and fliN mutations causing defects in assembly, rotation, and switching of the flagellar motor J. Bacteriol. 175, 802-810 (Pubitemid 23046944)
    • (1993) Journal of Bacteriology , vol.175 , Issue.3 , pp. 802-810
    • Irikura, V.M.1    Kihara, M.2    Yamaguchi, S.3    Sockett, H.4    Macnab, R.M.5
  • 42
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2: A multiple sequence alignment editor and analysis workbench
    • Waterhouse, A. M., Procter, J. B., Martin, D. M. A., Clamp, M., and Barton, G. J. (2009) Jalview Version 2: A multiple sequence alignment editor and analysis workbench Bioinformatics 25, 1189-1191
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.A.3    Clamp, M.4    Barton, G.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.