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Volumn 86, Issue 6, 2004, Pages 4049-4058

The fast tumble signal in bacterial chemotaxis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHEYP PROTEIN; LEUCINE; PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 2942655501     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.103.033043     Document Type: Article
Times cited : (21)

References (42)
  • 1
    • 0028097182 scopus 로고
    • Constitutively signaling fragments of Tsr, the Escherichia coli serine chemoreceptor
    • Ames, P., and J. S. Parkinson. 1994. Constitutively signaling fragments of Tsr, the Escherichia coli serine chemoreceptor. J. Bacteriol. 176:6340-6348.
    • (1994) J. Bacteriol. , vol.176 , pp. 6340-6348
    • Ames, P.1    Parkinson, J.S.2
  • 2
    • 0037076332 scopus 로고    scopus 로고
    • Collaborative signaling by mixed chemoreceptor teams in Escherichia coli
    • Ames, P., C. A. Studdert, R. H. Reiser, and J. S. Parkinson. 2002. Collaborative signaling by mixed chemoreceptor teams in Escherichia coli. Proc. Natl. Acad. Sci. USA. 99:7060-7065.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7060-7065
    • Ames, P.1    Studdert, C.A.2    Reiser, R.H.3    Parkinson, J.S.4
  • 3
    • 0015526205 scopus 로고
    • Chemotaxis in Escherichia coli analysed by three-dimensional tracking
    • Berg, H. C., and D. A. Brown. 1972. Chemotaxis in Escherichia coli analysed by three-dimensional tracking. Nature. 239:500-504.
    • (1972) Nature , vol.239 , pp. 500-504
    • Berg, H.C.1    Brown, D.A.2
  • 4
    • 0001180444 scopus 로고
    • Transient response to chemotactic stimuli in Escherichia coli
    • Berg, H. C., and P. M. Tedesco. 1975. Transient response to chemotactic stimuli in Escherichia coli. Proc. Natl. Acad. Sci. USA. 72:3235-3239.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 3235-3239
    • Berg, H.C.1    Tedesco, P.M.2
  • 5
    • 0031460634 scopus 로고    scopus 로고
    • Absence of a barrier to backwards rotation of the bacterial flagellar motor demonstrated with optical tweezers
    • Berry, R. M., and H. C. Berg. 1997. Absence of a barrier to backwards rotation of the bacterial flagellar motor demonstrated with optical tweezers. Proc. Natl. Acad. Sci. USA. 94:14433-14437.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14433-14437
    • Berry, R.M.1    Berg, H.C.2
  • 6
    • 0020398978 scopus 로고
    • Impulse responses in bacterial chemotaxis
    • Block, S. M., J. E. Segall, and H. C. Berg. 1982. Impulse responses in bacterial chemotaxis. Cell. 31:215-226.
    • (1982) Cell , vol.31 , pp. 215-226
    • Block, S.M.1    Segall, J.E.2    Berg, H.C.3
  • 7
    • 0024514118 scopus 로고
    • Compliance of bacterial flagella measured with optical tweezers
    • Block, S. M., D. F. Blair, and H. C. Berg. 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
  • 8
    • 0037424604 scopus 로고    scopus 로고
    • Quantitative analysis of aspartate receptor signaling complex reveals that the homogeneous two-state model is inadequate: Development of a heterogeneous two-state model
    • Bomhorst, J. A., and J. J. Falke. 2003. Quantitative analysis of aspartate receptor signaling complex reveals that the homogeneous two-state model is inadequate: development of a heterogeneous two-state model. J. Mol. Biol. 326:1597-1614.
    • (2003) J. Mol. Biol. , vol.326 , pp. 1597-1614
    • Bomhorst, J.A.1    Falke, J.J.2
  • 9
    • 0034460297 scopus 로고    scopus 로고
    • How signals are heard during bacterial chemotaxis: Protein-protein interactions in sensory signal propagation
    • Bren, A., and M. Eisenbach. 2000. How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation. J. Bacteriol. 182:6865-6873.
    • (2000) J. Bacteriol. , vol.182 , pp. 6865-6873
    • Bren, A.1    Eisenbach, M.2
  • 10
    • 0018712142 scopus 로고
    • Membrane receptors for aspartate and serine in bacterial chemotaxis
    • Clarke, S., and D. E. Koshland, Jr. 1979. Membrane receptors for aspartate and serine in bacterial chemotaxis. J. Biol. Chem. 254:9695-9702.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9695-9702
    • Clarke, S.1    Koshland Jr., D.E.2
  • 11
    • 0034009901 scopus 로고    scopus 로고
    • An ultrasensitive bacterial motor revealed by monitoring signaling proteins in single cells
    • Cluzel, P., M. Surette, and S. Leibler. 2000. An ultrasensitive bacterial motor revealed by monitoring signaling proteins in single cells. Science. 287:1652-1655.
    • (2000) Science , vol.287 , pp. 1652-1655
    • Cluzel, P.1    Surette, M.2    Leibler, S.3
  • 12
    • 0035804929 scopus 로고    scopus 로고
    • Conformational spread in a ring of proteins: A stochastic approach to allostery
    • Duke, T. A., N. L. Novere, and D. Bray. 2001. Conformational spread in a ring of proteins: a stochastic approach to allostery. J. Mol. Biol. 308:541-553.
    • (2001) J. Mol. Biol. , vol.308 , pp. 541-553
    • Duke, T.A.1    Novere, N.L.2    Bray, D.3
  • 13
    • 0025181297 scopus 로고
    • Repellents for Escherichia coli operate neither by changing membrane fluidity nor by being sensed by periplasmic receptors during chemotaxis
    • Eisenbach, M., C. Constantinou, H. Aloni, and M. Shinitzky. 1990. Repellents for Escherichia coli operate neither by changing membrane fluidity nor by being sensed by periplasmic receptors during chemotaxis. J. Bacteriol. 172:5218-5224.
    • (1990) J. Bacteriol. , vol.172 , pp. 5218-5224
    • Eisenbach, M.1    Constantinou, C.2    Aloni, H.3    Shinitzky, M.4
  • 14
    • 0038112089 scopus 로고    scopus 로고
    • Biomechanics: Bacterial flagellar switching under load
    • Fahmer, K. A., W. S. Ryu, and H. C. Berg. 2003. Biomechanics: bacterial flagellar switching under load. Nature. 424:938.
    • (2003) Nature , vol.424 , pp. 938
    • Fahmer, K.A.1    Ryu, W.S.2    Berg, H.C.3
  • 15
    • 0031455398 scopus 로고    scopus 로고
    • The two-component signaling pathway of bacterial chemotaxis: A molecular view of signal transduction by receptors, kinases, and adaptation enzymes
    • Falke, J. J., R. B. Bass, S. L. Butler, S. A. Chervitz, and M. A. Danielson. 1997. The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes. Annu. Rev. Cell Dev. Biol. 13:457-512.
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 457-512
    • Falke, J.J.1    Bass, R.B.2    Butler, S.L.3    Chervitz, S.A.4    Danielson, M.A.5
  • 16
    • 0030660403 scopus 로고    scopus 로고
    • High- and low-abundance chemoreceptors in Escherichia coli: Differential activities associated with closely related cytoplasmic domains
    • Feng, X., J. W. Baumgartner, and G. L. Hazelbauer. 1997. High- and low-abundance chemoreceptors in Escherichia coli: differential activities associated with closely related cytoplasmic domains. J. Bacteriol. 179:6714-6720.
    • (1997) J. Bacteriol. , vol.179 , pp. 6714-6720
    • Feng, X.1    Baumgartner, J.W.2    Hazelbauer, G.L.3
  • 17
    • 0037184114 scopus 로고    scopus 로고
    • Subunit organization in a soluble complex of Tar, CheW, and CheA by electron microscopy
    • Francis, N. R., M. N. Levit, T. R. Shaikh, L. A. Melanson, J. B. Stock, and D. J. DeRosier. 2002. Subunit organization in a soluble complex of Tar, CheW, and CheA by electron microscopy. J. Biol. Chem. 277:36755-36759.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36755-36759
    • Francis, N.R.1    Levit, M.N.2    Shaikh, T.R.3    Melanson, L.A.4    Stock, J.B.5    DeRosier, D.J.6
  • 18
    • 0019526265 scopus 로고
    • Hydrodynamic properties of complex, rigid, biological macromolecules: Theory and applications
    • Garcia de la Torre, J. G., and V. A. Bloomfield. 1981. Hydrodynamic properties of complex, rigid, biological macromolecules: theory and applications. Q. Rev. Biophys. 14:81-139.
    • (1981) Q. Rev. Biophys. , vol.14 , pp. 81-139
    • Garcia De La Torre, J.G.1    Bloomfield, V.A.2
  • 19
    • 0033014470 scopus 로고    scopus 로고
    • Chemotactic responses of Escherichia coli to small jumps of photo-released L-aspartate
    • Jasuja, R., J. Keyoung, G. P. Reid, D. R. Trentham, and S. Khan. 1999a. Chemotactic responses of Escherichia coli to small jumps of photo-released L-aspartate. Biophys. J. 76:1706-1719.
    • (1999) Biophys. J. , vol.76 , pp. 1706-1719
    • Jasuja, R.1    Keyoung, J.2    Reid, G.P.3    Trentham, D.R.4    Khan, S.5
  • 21
    • 0034031421 scopus 로고    scopus 로고
    • On bacterial tactic response times and latencies
    • Khan, S. 2000. On bacterial tactic response times and latencies. Biophys. J. 78:2186-2187.
    • (2000) Biophys. J. , vol.78 , pp. 2186-2187
    • Khan, S.1
  • 23
    • 0019325206 scopus 로고
    • The steady-state counterclockwise/clockwise ratio of bacterial flagellar motors is regulated by protonmotive force
    • Khan, S., and R. M. Macnab. 1980. The steady-state counterclockwise/ clockwise ratio of bacterial flagellar motors is regulated by protonmotive force. J. Mol. Biol. 138:563-597.
    • (1980) J. Mol. Biol. , vol.138 , pp. 563-597
    • Khan, S.1    Macnab, R.M.2
  • 25
    • 0347285391 scopus 로고    scopus 로고
    • Biphasic chemotactic excitation in Escherichia coli to L-leucine
    • Khan, S., and D. R. Trentham. 2004. Biphasic chemotactic excitation in Escherichia coli to L-leucine. J. Bacteriol. 186:588-592.
    • (2004) J. Bacteriol. , vol.186 , pp. 588-592
    • Khan, S.1    Trentham, D.R.2
  • 26
    • 0019395341 scopus 로고
    • Cytoplasmic pH mediates pH taxis and weak-acid repellent taxis of bacteria
    • Kihara, M., and R. M. Macnab. 1981. Cytoplasmic pH mediates pH taxis and weak-acid repellent taxis of bacteria. J. Bacteriol. 145:1209-1221.
    • (1981) J. Bacteriol. , vol.145 , pp. 1209-1221
    • Kihara, M.1    Macnab, R.M.2
  • 27
    • 0035896025 scopus 로고    scopus 로고
    • Determinants of chemotactic signal amplification in Escherichia coli
    • Kim, C., M. Jackson, R. Lux, and S. Khan. 2001. Determinants of chemotactic signal amplification in Escherichia coli. J. Mol. Biol. 307:119-135.
    • (2001) J. Mol. Biol. , vol.307 , pp. 119-135
    • Kim, C.1    Jackson, M.2    Lux, R.3    Khan, S.4
  • 28
    • 0037015003 scopus 로고    scopus 로고
    • Dynamic and clustering model of bacterial chemotaxis receptors: Structural basis for signaling and high sensitivity
    • Kim, S. H., W. Wang, and K. K. Kim. 2002. Dynamic and clustering model of bacterial chemotaxis receptors: structural basis for signaling and high sensitivity. Proc. Natl. Acad. Sci. USA. 99:11611-11615.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11611-11615
    • Kim, S.H.1    Wang, W.2    Kim, K.K.3
  • 29
    • 0033580642 scopus 로고    scopus 로고
    • Mechanism of CheA protein kinase activation in receptor signaling complexes
    • Levit, M. N., Y. Liu, and J. B. Stock. 1999. Mechanism of CheA protein kinase activation in receptor signaling complexes. Biochemistry. 38:6651-6658.
    • (1999) Biochemistry , vol.38 , pp. 6651-6658
    • Levit, M.N.1    Liu, Y.2    Stock, J.B.3
  • 30
    • 0034603209 scopus 로고    scopus 로고
    • Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli
    • Li, G., and R. M. Weis. 2000. Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli. Cell. 100:357-365.
    • (2000) Cell , vol.100 , pp. 357-365
    • Li, G.1    Weis, R.M.2
  • 31
    • 0017704180 scopus 로고
    • Normal-to-curly flagellar transitions and their role in bacterial tumbling. Stabilization of an alternative quaternary structure by mechanical force
    • Macnab, R. M., and M. K. Ornston. 1977. Normal-to-curly flagellar transitions and their role in bacterial tumbling. Stabilization of an alternative quaternary structure by mechanical force. J. Mol. Biol. 112:1-30.
    • (1977) J. Mol. Biol. , vol.112 , pp. 1-30
    • Macnab, R.M.1    Ornston, M.K.2
  • 32
    • 0038168479 scopus 로고    scopus 로고
    • Binding of the chemotaxis response regulator CheY to the isolated, intact switch complex of the bacterial flagellar motor: Lack of cooperativity
    • Sagi, Y., S. Khan, and M. Eisenbach. 2003. Binding of the chemotaxis response regulator CheY to the isolated, intact switch complex of the bacterial flagellar motor: lack of cooperativity. J. Biol. Chem. 278:25867-25871.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25867-25871
    • Sagi, Y.1    Khan, S.2    Eisenbach, M.3
  • 34
    • 0019953987 scopus 로고
    • Signal processing times in bacterial chemotaxis
    • Segall, J. E., M. D. Manson, and H. C. Berg. 1982. Signal processing times in bacterial chemotaxis. Nature. 296:855-857.
    • (1982) Nature , vol.296 , pp. 855-857
    • Segall, J.E.1    Manson, M.D.2    Berg, H.C.3
  • 35
    • 0037039384 scopus 로고    scopus 로고
    • Receptor sensitivity in bacterial chemotaxis
    • Sourjik, V., and H. C. Berg. 2002a. Receptor sensitivity in bacterial chemotaxis. Proc. Natl. Acad. Sci. USA. 99:123-127.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 123-127
    • Sourjik, V.1    Berg, H.C.2
  • 36
    • 0036790991 scopus 로고    scopus 로고
    • Binding of the Escherichia coli response regulator CheY to its target measured in vivo by fluorescence resonance energy transfer
    • Sourjik, V., and H. C. Berg. 2002b. Binding of the Escherichia coli response regulator CheY to its target measured in vivo by fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. USA. 99:12669-12674.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12669-12674
    • Sourjik, V.1    Berg, H.C.2
  • 37
    • 0018634153 scopus 로고
    • Protein methylation in behavioural control mechanisms and in signal transduction
    • Springer, M. S., M. F. Goy, and J. Adler. 1979. Protein methylation in behavioural control mechanisms and in signal transduction. Nature. 280:279-284.
    • (1979) Nature , vol.280 , pp. 279-284
    • Springer, M.S.1    Goy, M.F.2    Adler, J.3
  • 39
    • 0016258213 scopus 로고
    • Negative chemotaxis in Escherichia coli
    • Tso, W. W., and J. Adler. 1974. Negative chemotaxis in Escherichia coli. J. Bacteriol. 118:560-576.
    • (1974) J. Bacteriol. , vol.118 , pp. 560-576
    • Tso, W.W.1    Adler, J.2
  • 40
    • 0034015656 scopus 로고    scopus 로고
    • Real-time imaging of fluorescent flagellar filaments
    • Turner, L., W. S. Ryu, and H. C. Berg. 2000. Real-time imaging of fluorescent flagellar filaments. J. Bacteriol. 182:2793-2801.
    • (2000) J. Bacteriol. , vol.182 , pp. 2793-2801
    • Turner, L.1    Ryu, W.S.2    Berg, H.C.3
  • 41
    • 0033014680 scopus 로고    scopus 로고
    • Temperature dependence of switching of the bacterial flagellar motor by the protein CheY(13DK106YW)
    • Turner, L., A. D. Samuel, A. S. Stem, and H. C. Berg. 1999. Temperature dependence of switching of the bacterial flagellar motor by the protein CheY(13DK106YW). Biophys. J. 77:597-603.
    • (1999) Biophys. J. , vol.77 , pp. 597-603
    • Turner, L.1    Samuel, A.D.2    Stem, A.S.3    Berg, H.C.4
  • 42
    • 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


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