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Volumn 194, Issue 13, 2012, Pages 3495-3501

Flagellar hook flexibility is essential for bundle formation in swimming Escherichia coli cells

Author keywords

[No Author keywords available]

Indexed keywords

MONOMER; STREPTAVIDIN;

EID: 84864003621     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00209-12     Document Type: Article
Times cited : (71)

References (35)
  • 1
    • 33746736246 scopus 로고    scopus 로고
    • Membrane lateral diffusion and capture of CFTR within transient confinement zones
    • Bates IR, et al. 2006. Membrane lateral diffusion and capture of CFTR within transient confinement zones. Biophys. J. 91:1046 -1058.
    • (2006) Biophys. J. , vol.91 , pp. 1046-1058
    • Bates, I.R.1
  • 2
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett D, Kovaleva E, Schatz PJ. 1999. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci. 8:921- 929.
    • (1999) Protein Sci , vol.8 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 3
    • 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
  • 4
    • 0015897650 scopus 로고
    • Bacteria swim by rotating their flagellar filaments
    • Berg HC, Anderson RA. 1973. Bacteria swim by rotating their flagellar filaments. Nature 245:380 -382.
    • (1973) Nature , vol.245 , pp. 380-382
    • Berg, H.C.1    Anderson, R.A.2
  • 5
    • 0024514118 scopus 로고
    • Compliance of bacterial flagella measured with optical tweezers
    • Block SM, Blair DF, Berg HC. 1989. Compliance of bacterial flagella measured with optical tweezers. Nature 338:514 -518.
    • (1989) Nature , vol.338 , pp. 514-518
    • Block, S.M.1    Blair, D.F.2    Berg, H.C.3
  • 6
    • 0025819598 scopus 로고
    • Compliance of bacterial polyhooks measured with optical tweezers
    • Block SM, Blair DF, Berg HC. 1991. Compliance of bacterial polyhooks measured with optical tweezers. Cytometry 12:492- 496.
    • (1991) Cytometry , vol.12 , pp. 492-496
    • Block, S.M.1    Blair, D.F.2    Berg, H.C.3
  • 8
    • 43849098574 scopus 로고    scopus 로고
    • Coordinating assembly of a bacterial macromolecular machine
    • Chevance FFV, Hughes KT. 2008. Coordinating assembly of a bacterial macromolecular machine. Nat. Rev. Microbiol. 6:455- 465.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 455-465
    • Chevance, F.F.V.1    Hughes, K.T.2
  • 9
    • 77952243925 scopus 로고    scopus 로고
    • A streptavidin variant with slower biotin dissociation and increased mechanostability
    • Chivers CE, et al. 2010. A streptavidin variant with slower biotin dissociation and increased mechanostability. Nat. Methods 7:391-393.
    • (2010) Nat. Methods , vol.7 , pp. 391-393
    • Chivers, C.E.1
  • 10
  • 11
    • 77954921897 scopus 로고    scopus 로고
    • Signal-dependent turnover of the bacterial flagellar switch protein FliM
    • Delalez NJ, et al. 2010. Signal-dependent turnover of the bacterial flagellar switch protein FliM. Proc. Natl. Acad. Sci. U. S. A. 107:11347-11351.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 11347-11351
    • Delalez, N.J.1
  • 12
    • 0014976040 scopus 로고
    • Fine structure and isolation of the hookbasal body complex of flagella from Escherichia coli and Bacillus subtilis
    • DePamphilis M, Adler J. 1971. Fine structure and isolation of the hookbasal body complex of flagella from Escherichia coli and Bacillus subtilis. J. Bacteriol. 105:384 -395.
    • (1971) J. Bacteriol. , vol.105 , pp. 384-395
    • DePamphilis, M.1    Adler, J.2
  • 13
    • 0014979468 scopus 로고
    • Purification of intact flagella from Escherichia coli and Bacillus subtilis
    • DePamphilis M, Adler J. 1971. Purification of intact flagella from Escherichia coli and Bacillus subtilis. J. Bacteriol. 105:376 -383.
    • (1971) J. Bacteriol. , vol.105 , pp. 376-383
    • DePamphilis, M.1    Adler, J.2
  • 14
    • 48949120507 scopus 로고    scopus 로고
    • Differential dissociation of G protein heterotrimers
    • Digby GJ, Sethi PR, Lambert NA. 2008. Differential dissociation of G protein heterotrimers. J. Physiol. 586:3325-3335.
    • (2008) J. Physiol. , vol.586 , pp. 3325-3335
    • Digby, G.J.1    Sethi, P.R.2    Lambert, N.A.3
  • 16
    • 32144441831 scopus 로고    scopus 로고
    • A numerical algorithm for investigating the role of the motor-cargo linkage in molecular motor-driven transport
    • Fricks J, Wang H, Elston TC. 2006. A numerical algorithm for investigating the role of the motor-cargo linkage in molecular motor-driven transport. J. Theor. Biol. 239:33- 48.
    • (2006) J. Theor. Biol. , vol.239 , pp. 33-48
    • Fricks, J.1    Wang, H.2    Elston, T.C.3
  • 17
    • 70350719099 scopus 로고    scopus 로고
    • Specific arrangement of a-helical coiled coils in the core domain of the bacterial flagellar hook for the universal joint function
    • Fujii T, Kato T, Namba K. 2009. Specific arrangement of a-helical coiled coils in the core domain of the bacterial flagellar hook for the universal joint function. Structure 17:1485-1493.
    • (2009) Structure , vol.17 , pp. 1485-1493
    • Fujii, T.1    Kato, T.2    Namba, K.3
  • 19
    • 0028093390 scopus 로고
    • Roles of FliK and FlhB in determination of flagellar hook length in Salmonella typhimurium
    • Hirano T, Yamaguchi S, Oosawa K, Aizawa S. 1994. Roles of FliK and FlhB in determination of flagellar hook length in Salmonella typhimurium. J. Bacteriol. 176:5439 -5449.
    • (1994) J. Bacteriol. , vol.176 , pp. 5439-5449
    • Hirano, T.1    Yamaguchi, S.2    Oosawa, K.3    Aizawa, S.4
  • 20
    • 33645283107 scopus 로고    scopus 로고
    • A monovalent streptavidin with a single femtomolar biotin binding site
    • Howarth M, et al. 2006. A monovalent streptavidin with a single femtomolar biotin binding site. Nat. Methods 3:267-273.
    • (2006) Nat. Methods 3 , pp. 267-273
    • Howarth, M.1
  • 21
    • 40649128835 scopus 로고    scopus 로고
    • Imaging proteins in live mammalian cells with biotin ligase and monovalent streptavidin
    • Howarth M, Ting AY. 2008. Imaging proteins in live mammalian cells with biotin ligase and monovalent streptavidin. Nat. Protoc. 3:534 -545.
    • (2008) Nat. Protoc. , vol.3 , pp. 534-545
    • Howarth, M.1    Ting, A.Y.2
  • 22
    • 33748926752 scopus 로고    scopus 로고
    • Stoichiometry and turnover in single, functioning membrane protein complexes
    • Leake MC, et al. 2006. Stoichiometry and turnover in single, functioning membrane protein complexes. Nature 443:355-358.
    • (2006) Nature 443 , pp. 355-358
    • Leake, M.C.1
  • 23
    • 0030796260 scopus 로고    scopus 로고
    • Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization
    • Link AJ, Phillips D, Church GM. 1997. Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization. J. Bacteriol. 179:6228- 6237.
    • (1997) J. Bacteriol. , vol.179 , pp. 6228-6237
    • Link, A.J.1    Phillips, D.2    Church, G.M.3
  • 24
    • 80052472175 scopus 로고    scopus 로고
    • Steps and bumps: precision extraction of discrete states of molecular machines
    • Little MA, et al. 2011. Steps and bumps: precision extraction of discrete states of molecular machines. Biophys. J. 101:477- 485.
    • (2011) Biophys. J. , vol.101 , pp. 477-485
    • Little, M.A.1
  • 26
    • 0036932207 scopus 로고    scopus 로고
    • The motion of a single molecule, the l-receptor, in the bacterial outer membrane
    • Oddershede L, Dreyer JK, Grego S, Brown S, Berg-Sørensen K. 2002. The motion of a single molecule, the l-receptor, in the bacterial outer membrane. Biophys. J. 83:3152-3161.
    • (2002) Biophys. J. , vol.83 , pp. 3152-3161
    • Oddershede, L.1    Dreyer, J.K.2    Grego, S.3    Brown, S.4    Berg-Sørensen, K.5
  • 27
    • 1942487190 scopus 로고    scopus 로고
    • Improvement of pCVD442, a suicide plasmid for gene allele exchange in bacteria
    • Philippe N, Alcaraz JP, Coursange E, Geiselmann J, Schneider D. 2004. Improvement of pCVD442, a suicide plasmid for gene allele exchange in bacteria. Plasmid 51:246 -255.
    • (2004) Plasmid , vol.51 , pp. 246-255
    • Philippe, N.1    Alcaraz, J.P.2    Coursange, E.3    Geiselmann, J.4    Schneider, D.5
  • 28
    • 67650908932 scopus 로고    scopus 로고
    • A molecular brake, not a clutch, stops the Rhodobacter sphaeroides flagellar motor
    • Pilizota T, et al. 2009. A molecular brake, not a clutch, stops the Rhodobacter sphaeroides flagellar motor. Proc. Natl. Acad. Sci. U. S. A. 106: 11582-11587.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 11582-11587
    • Pilizota, T.1
  • 29
    • 84890506631 scopus 로고
    • Life at low Reynolds number
    • Purcell EM. 1977. Life at low Reynolds number. Am. J. Phys. 45:3-11.
    • (1977) Am. J. Phys. , vol.45 , pp. 3-11
    • Purcell, E.M.1
  • 30
    • 7744246770 scopus 로고    scopus 로고
    • Structure of the bacterial flagellar hook and implication for the molecular universal joint mechanism
    • Samatey FA, et al. 2004. Structure of the bacterial flagellar hook and implication for the molecular universal joint mechanism. Nature 431: 1062-1068.
    • (2004) Nature , vol.431 , pp. 1062-1068
    • Samatey, F.A.1
  • 31
    • 12844288625 scopus 로고    scopus 로고
    • A partial atomic structure for the flagellar hook of Salmonella typhimurium
    • Shaikh TR, et al. 2005. A partial atomic structure for the flagellar hook of Salmonella typhimurium. Proc. Natl. Acad. Sci. U. S. A. 102:1023-1028.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 1023-1028
    • Shaikh, T.R.1
  • 32
    • 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
  • 33
    • 0020410957 scopus 로고
    • Flagellar hook structures of Caulobacter and Salmonella and their relationship to filament structure
    • Wagenknecht T, DeRosier DJ. 1982. Flagellar hook structures of Caulobacter and Salmonella and their relationship to filament structure. J. Mol. Biol. 162:69-87.
    • (1982) J. Mol. Biol. , vol.162 , pp. 69-87
    • Wagenknecht, T.1    DeRosier, D.J.2
  • 35
    • 34547261744 scopus 로고    scopus 로고
    • Bifunctional nanotube scaffolds for diverse ligands are purified simply from Escherichia coli strains coexpressing two functionalized flagellar genes
    • Woods RD, et al. 2007. Bifunctional nanotube scaffolds for diverse ligands are purified simply from Escherichia coli strains coexpressing two functionalized flagellar genes. Nano Lett. 7:1809 -1816.
    • (2007) Nano Lett , vol.7 , pp. 1809-1816
    • Woods, R.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.