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Volumn 5, Issue 4, 2014, Pages

Stoichiometry and turnover of the bacterial flagellar switch protein FliN

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN FLIM; PROTEIN FLIN; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; FLIN PROTEIN, BACTERIA; MOLECULAR MOTOR;

EID: 84908265407     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.01216-14     Document Type: Article
Times cited : (65)

References (24)
  • 1
    • 52649147435 scopus 로고    scopus 로고
    • Bacterial flagellar motor
    • Sowa Y, Berry RM. 2008. Bacterial flagellar motor. Q. Rev. Biophys. 41:103-132. http://dx.doi.org/10.1017/S0033583508004691.
    • (2008) Q. Rev. Biophys , vol.41 , pp. 103-132
    • Sowa, Y.1    Berry, R.M.2
  • 2
    • 79951852204 scopus 로고    scopus 로고
    • Signal processing in complex chemotaxis pathways
    • Porter SL, Wadhams GH, Armitage JP. 2011. Signal processing in complex chemotaxis pathways. Nat. Rev. Microbiol. 9:153-165. http://dx.doi.org/10.1038/nrmicro2505.
    • (2011) Nat. Rev. Microbiol , vol.9 , pp. 153-165
    • Porter, S.L.1    Wadhams, G.H.2    Armitage, J.P.3
  • 3
    • 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. http://dx.doi.org/10.1021/bi011264g.
    • (2001) Biochemistry , vol.40 , pp. 13051-13059
    • Braun, T.F.1    Blair, D.F.2
  • 4
    • 0041806636 scopus 로고    scopus 로고
    • The speed of the flagellar rotary motor of Escherichia coli varies linearly with protonmotive force
    • Gabel CV, Berg HC. 2003. The speed of the flagellar rotary motor of Escherichia coli varies linearly with protonmotive force. Proc. Natl. Acad. Sci. U. S. A. 100:8748-8751. http://dx.doi.org/10.1073/pnas.1533395100.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 8748-8751
    • Gabel, C.V.1    Berg, H.C.2
  • 5
    • 33748926752 scopus 로고    scopus 로고
    • Stoichiometry and turnover in single, functioning membrane protein complexes
    • Leake MC, Chandler JH, Wadhams GH, Bai F, Berry RM, Armitage JP. 2006. Stoichiometry and turnover in single, functioning membrane protein complexes. Nature 443:355-358. http://dx.doi.org/10.1038/nature05135.
    • (2006) Nature , vol.443 , pp. 355-358
    • Leake, M.C.1    Chandler, J.H.2    Wadhams, G.H.3    Bai, F.4    Berry, R.M.5    Armitage, J.P.6
  • 7
    • 84859619467 scopus 로고    scopus 로고
    • Adaptation at the output of the chemotaxis signalling pathway
    • Yuan J, Branch RW, Hosu BG, Berg HC. 2012. Adaptation at the output of the chemotaxis signalling pathway. Nature 484:233-236. http://dx.doi.org/10.1038/nature10964.
    • (2012) Nature , vol.484 , pp. 233-236
    • Yuan, J.1    Branch, R.W.2    Hosu, B.G.3    Berg, H.C.4
  • 8
    • 84870599344 scopus 로고    scopus 로고
    • Mechanism for adaptive remodeling of the bacterial flagellar switch
    • Lele PP, Branch RW, Nathan VS, Berg HC. 2012. Mechanism for adaptive remodeling of the bacterial flagellar switch. Proc. Natl. Acad. Sci. U. S. A. 109:20018-20022. http://dx.doi.org/10.1073/pnas.1212327109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A , vol.109 , pp. 20018-20022
    • Lele, P.P.1    Branch, R.W.2    Nathan, V.S.3    Berg, H.C.4
  • 9
    • 84872371364 scopus 로고    scopus 로고
    • Quantification of flagellar motor stator dynamics through in vivo protonmotive force control
    • Tipping MJ, Steel BC, Delalez NJ, Berry RM, Armitage JP. 2013. Quantification of flagellar motor stator dynamics through in vivo protonmotive force control. Mol. Microbiol. 87:338-347. http://dx.doi.org/10.1111/mmi.12098.
    • (2013) Mol. Microbiol , vol.87 , pp. 338-347
    • Tipping, M.J.1    Steel, B.C.2    Delalez, N.J.3    Berry, R.M.4    Armitage, J.P.5
  • 10
    • 84883436048 scopus 로고    scopus 로고
    • Loaddependent assembly of the bacterial flagellar motor
    • Tipping MJ, Delalez NJ, Lim R, Berry RM, Armitage JP. 2013. Loaddependent assembly of the bacterial flagellar motor. mBio 4(4):e00551-13. http://dx.doi.org/10.1128/mBio.00551-13.
    • (2013) mBio , vol.4 , Issue.4 , pp. 00551-00613
    • Tipping, M.J.1    Delalez, N.J.2    Lim, R.3    Berry, R.M.4    Armitage, J.P.5
  • 11
    • 84880387422 scopus 로고    scopus 로고
    • Dynamics of mechanosensing in the bacterial flagellar motor
    • Lele PP, Hosu BG, Berg HC. 2013. Dynamics of mechanosensing in the bacterial flagellar motor. Proc. Natl. Acad. Sci. U. S. A. 110:11839-11844. http://dx.doi.org/10.1073/pnas.1305885110.
    • (2013) Proc. Natl. Acad. Sci. U. S. A , vol.110 , pp. 11839-11844
    • Lele, P.P.1    Hosu, B.G.2    Berg, H.C.3
  • 12
    • 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 MK, Paul K, Blair D. 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. http://dx.doi.org/10.1073/pnas.1000935107.
    • (2010) Proc. Natl. Acad. Sci. U. S. A , vol.107 , pp. 9370-9375
    • Sarkar, M.K.1    Paul, K.2    Blair, D.3
  • 13
    • 0032496388 scopus 로고    scopus 로고
    • The N terminus of the flagellar switch protein, FliM, is the binding domain for the chemotactic response regulator, CheY
    • Bren A, Eisenbach M. 1998. The N terminus of the flagellar switch protein, FliM, is the binding domain for the chemotactic response regulator, CheY. J. Mol. Biol. 278:507-514. http://dx.doi.org/10.1006/jmbi.1998.1730.
    • (1998) J. Mol. Biol , vol.278 , pp. 507-514
    • Bren, A.1    Eisenbach, M.2
  • 14
    • 0033603635 scopus 로고    scopus 로고
    • Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein FliM
    • McEvoy MM, Bren A, Eisenbach M, Dahlquist FW. 1999. Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein FliM. J. Mol. Biol. 289:1423-1433. http://dx.doi.org/10.1006/jmbi.1999.2830.
    • (1999) J. Mol. Biol , vol.289 , pp. 1423-1433
    • McEvoy, M.M.1    Bren, A.2    Eisenbach, M.3    Dahlquist, F.W.4
  • 15
    • 0027517812 scopus 로고
    • Phosphorylationdependent binding of a signal molecule to the flagellar switch of bacteria
    • Welch M, Oosawa K, Aizawa S, Eisenbach M. 1993. Phosphorylationdependent binding of a signal molecule to the flagellar switch of bacteria. Proc. Natl. Acad. Sci. U. S. A. 90:8787-8791. http://dx.doi.org/10.1073/pnas.90.19.8787.
    • (1993) Proc. Natl. Acad. Sci. U. S. A , vol.90 , pp. 8787-8791
    • Welch, M.1    Oosawa, K.2    Aizawa, S.3    Eisenbach, M.4
  • 16
    • 0034009901 scopus 로고    scopus 로고
    • An ultrasensitive bacterial motor revealed by monitoring signaling proteins in single cells
    • Cluzel P, Surette M, Leibler S. 2000. An ultrasensitive bacterial motor revealed by monitoring signaling proteins in single cells. Science 287: 1652-1655. http://dx.doi.org/10.1126/science.287.5458.1652.
    • (2000) Science , vol.287 , pp. 1652-1655
    • Cluzel, P.1    Surette, M.2    Leibler, S.3
  • 17
    • 0033621062 scopus 로고    scopus 로고
    • Rotational symmetry of the C ring and a mechanism for the flagellar rotary motor
    • Thomas DR, Morgan DG, DeRosier DJ. 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. http://dx.doi.org/10.1073/pnas.96.18.10134.
    • (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
  • 18
    • 12244302174 scopus 로고    scopus 로고
    • Variable symmetry in Salmonella typhimurium flagellar motors
    • Young HS, Dang H, Lai Y, DeRosier DJ, Khan S. 2003. Variable symmetry in Salmonella typhimurium flagellar motors. Biophys. J. 84: 571-577. http://dx.doi.org/10.1016/S0006-3495(03)74877-2.
    • (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
  • 19
    • 33749608423 scopus 로고    scopus 로고
    • The threedimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar
    • Thomas DR, Francis NR, Xu C, 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. http://dx.doi.org/10.1128/JB.00552-06.
    • (2006) Typhimurium. J. Bacteriol , vol.188 , pp. 7039-7048
    • Thomas, D.R.1    Francis, N.R.2    Xu, C.3    Derosier, D.J.4
  • 20
    • 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. http://dx.doi.org/10.1128/JB.187.8.2890-2902.2005.
    • (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
  • 21
    • 33645233315 scopus 로고    scopus 로고
    • Organization of FliN subunits in the flagellar motor of Escherichia coli
    • Paul K, Blair DF. 2006. Organization of FliN subunits in the flagellar motor of Escherichia coli. J. Bacteriol. 188:2502-2511. http://dx.doi.org/10.1128/JB.188.7.2502-2511.2006.
    • (2006) J. Bacteriol , vol.188 , pp. 2502-2511
    • Paul, K.1    Blair, D.F.2
  • 22
    • 73649145486 scopus 로고    scopus 로고
    • Subunit organization and reversalassociated movements in the flagellar switch of Escherichia coli
    • Sarkar MK, Paul K, Blair DF. 2010. Subunit organization and reversalassociated movements in the flagellar switch of Escherichia coli. J. Biol. Chem. 285:675-684. http://dx.doi.org/10.1074/jbc.M109.068676.
    • (2010) J. Biol. Chem , vol.285 , pp. 675-684
    • Sarkar, M.K.1    Paul, K.2    Blair, D.F.3
  • 23
    • 79955733488 scopus 로고    scopus 로고
    • Assembly and stability of flagellar motor in Escherichia coli
    • Li H, Sourjik V. 2011. Assembly and stability of flagellar motor in Escherichia coli. Mol. Microbiol. 80:886-899. http://dx.doi.org/10.1111/j.1365-2958.2011.07557.x.
    • (2011) Mol. Microbiol , vol.80 , pp. 886-899
    • Li, H.1    Sourjik, V.2
  • 24
    • 0018189924 scopus 로고
    • Complementation analysis and deletion mapping of Escherichia coli mutants defective in chemotaxis
    • Parkinson JS. 1978. Complementation analysis and deletion mapping of Escherichia coli mutants defective in chemotaxis. J. Bacteriol. 135:45-53.
    • (1978) J. Bacteriol , vol.135 , pp. 45-53
    • Parkinson, J.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.