메뉴 건너뛰기




Volumn 5, Issue 12, 2004, Pages 1024-1037

Making sense of it all: Bacterial chemotaxis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHEA KINASE; CHEY PROTEIN; CHEZ PROTEIN; PROTEIN HISTIDINE KINASE; UNCLASSIFIED DRUG;

EID: 10044252242     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1524     Document Type: Review
Times cited : (1100)

References (144)
  • 1
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signaling systems
    • West, A. H. & Stock, A. M. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 26, 369-376 (2001). A good review of the biochemical and structural aspects of chemotaxis and other two-component signalling systems.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 369-376
    • West, A.H.1    Stock, A.M.2
  • 2
    • 0028228109 scopus 로고
    • A two-component system that regulates an osmosensing MAP kinase cascade in yeast
    • Maeda, T., Wurglermurphy, S. M. & Saito, H. A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature 369, 242-245 (1994).
    • (1994) Nature , vol.369 , pp. 242-245
    • Maeda, T.1    Wurglermurphy, S.M.2    Saito, H.3
  • 3
    • 0031937062 scopus 로고    scopus 로고
    • Isolation of CaSLN1 and CaNIK1, the genes for osmosensing histidine kinase homologues, from the pathogenic fungus Candida albicans
    • Nagahashi, S. et al. Isolation of CaSLN1 and CaNIK1, the genes for osmosensing histidine kinase homologues, from the pathogenic fungus Candida albicans. Microbiology 144, 425-432 (1998).
    • (1998) Microbiology , vol.144 , pp. 425-432
    • Nagahashi, S.1
  • 4
    • 0029783214 scopus 로고    scopus 로고
    • The hybrid histidine kinase DokA is part of the osmotic response system of Dictyostelium
    • Schuster, S. C., Noegel, A. A., Oehme, F., Gerisch, G. & Simon, M. I. The hybrid histidine kinase DokA is part of the osmotic response system of Dictyostelium. EMBO J. 15, 3880-3889 (1996).
    • (1996) EMBO J. , vol.15 , pp. 3880-3889
    • Schuster, S.C.1    Noegel, A.A.2    Oehme, F.3    Gerisch, G.4    Simon, M.I.5
  • 5
    • 0029561719 scopus 로고
    • An ethylene-inducible component of signal transduction encoded by never-ripe
    • Wilkinson, J. Q., Lanahan, M. B., Yen, H. C., Giovannoni, J. J. & Klee, H. J. An ethylene-inducible component of signal transduction encoded by never-ripe. Science 270, 1807-1809 (1995).
    • (1995) Science , vol.270 , pp. 1807-1809
    • Wilkinson, J.Q.1    Lanahan, M.B.2    Yen, H.C.3    Giovannoni, J.J.4    Klee, H.J.5
  • 6
    • 1342279429 scopus 로고    scopus 로고
    • Survey of the number of two-component response regulator genes in the complete and annotated genome sequences of prokaryotes
    • Ashby, M. K. Survey of the number of two-component response regulator genes in the complete and annotated genome sequences of prokaryotes. FEMS Microbiol. Lett. 231, 277-281 (2004).
    • (2004) FEMS Microbiol. Lett. , vol.231 , pp. 277-281
    • Ashby, M.K.1
  • 9
    • 0036296323 scopus 로고    scopus 로고
    • Expression, purification and characterisation of full-length histidine protein kinase RegB from Rhodobacter sphaeroides
    • Potter, C. A. et al. Expression, purification and characterisation of full-length histidine protein kinase RegB from Rhodobacter sphaeroides. J. Mol. Biol. 320, 201-213 (2002).
    • (2002) J. Mol. Biol. , vol.320 , pp. 201-213
    • Potter, C.A.1
  • 10
    • 0033277365 scopus 로고    scopus 로고
    • Bacterial tactic responses
    • Armitage, J. P. Bacterial tactic responses. Adv. Microb. Physiol. 41, 229-289 (1999).
    • (1999) Adv. Microb. Physiol. , vol.41 , pp. 229-289
    • Armitage, J.P.1
  • 11
    • 0034460297 scopus 로고    scopus 로고
    • How signals are heard during bacterial chemotaxis: Protein-protein interactions in sensory signal propagation
    • Bren, A. & Eisenbach, M. How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation. J. Bacteriol. 182, 6865-6873 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 6865-6873
    • Bren, A.1    Eisenbach, M.2
  • 12
    • 0033040340 scopus 로고    scopus 로고
    • A twisted tale: The origin and evolution of motility and chemotaxis in prokaryotes
    • Faguy, D. M. & Jarrell, K. F. A twisted tale: the origin and evolution of motility and chemotaxis in prokaryotes. Microbiology 145, 279-281 (1999).
    • (1999) Microbiology , vol.145 , pp. 279-281
    • Faguy, D.M.1    Jarrell, K.F.2
  • 14
    • 0037948805 scopus 로고    scopus 로고
    • Bacteria are not too small for spatial sensing of chemical gradients: An experimental evidence
    • Thar, R. & Kühl, M. Bacteria are not too small for spatial sensing of chemical gradients: an experimental evidence. Proc. Natl Acad. Sci. USA 100, 5748-5753 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5748-5753
    • Thar, R.1    Kühl, M.2
  • 15
    • 0034015656 scopus 로고    scopus 로고
    • Real-time imaging of fluorescent flagellar filaments
    • Tumer, L., Ryu, W. S. & Berg, H. C. Real-time imaging of fluorescent flagellar filaments. J. Bacteriol. 182, 2793-2801 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 2793-2801
    • Tumer, L.1    Ryu, W.S.2    Berg, H.C.3
  • 16
    • 0031437603 scopus 로고    scopus 로고
    • Bacterial chemotaxis: Rhodobacter sphaeroides and Sinorhizobium meliloti - Variations on a theme?
    • Armitage, J. P. & Schmitt, R. Bacterial chemotaxis: Rhodobacter sphaeroides and Sinorhizobium meliloti - variations on a theme? Microbiology 143, 3671-3682 (1997).
    • (1997) Microbiology , vol.143 , pp. 3671-3682
    • Armitage, J.P.1    Schmitt, R.2
  • 17
    • 0014692237 scopus 로고
    • Chemoreceptors in bacteria
    • Adler, J. Chemoreceptors in bacteria. Science 166, 1588-1597 (1969).
    • (1969) Science , vol.166 , pp. 1588-1597
    • Adler, J.1
  • 19
    • 0033552946 scopus 로고    scopus 로고
    • Robustness in bacterial chemotaxis
    • Alon, U., Surette, M. G., Barkai, N. & Leibler, S. Robustness in bacterial chemotaxis. Nature 397, 168-171 (1999). A mathematical consideration of the processes of adaptation and robustness in the bacterial chemotaxis pathway.
    • (1999) Nature , vol.397 , pp. 168-171
    • Alon, U.1    Surette, M.G.2    Barkai, N.3    Leibler, S.4
  • 20
    • 0037015003 scopus 로고    scopus 로고
    • Dynamic and clustering model of bacterial chemotaxis receptors: Structural basis for signaling and high sensitivity
    • Kim, S. H., Wang, W. R. & Kim, K. K. Dynamic and clustering model of bacterial chemotaxis receptors: structural basis for signaling and high sensitivity. Proc. Natl Acad. Sci. USA 99, 11611-11615 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11611-11615
    • Kim, S.H.1    Wang, W.R.2    Kim, K.K.3
  • 21
    • 1842473065 scopus 로고    scopus 로고
    • Functional interactions between receptors in bacterial chemotaxis
    • Sourjik, V. & Berg, H. C. Functional interactions between receptors in bacterial chemotaxis. Nature 428, 437-441 (2004).
    • (2004) Nature , vol.428 , pp. 437-441
    • Sourjik, V.1    Berg, H.C.2
  • 22
    • 0037039384 scopus 로고    scopus 로고
    • Receptor sensitivity in bacterial chemotaxis
    • Sourjik, V. & Berg, H. C. Receptor sensitivity in bacterial chemotaxis. Proc. Natl Acad. Sci. USA 99, 123-127 (2002). References 21 and 22 use fluorescence resonance energy transfer to assay the interactions between chemoreceptors in E. coli and between CheY-P and CheZ to explain sensitivity and gain in the chemotaxis pathway.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 123-127
    • Sourjik, V.1    Berg, H.C.2
  • 23
    • 0035896025 scopus 로고    scopus 로고
    • Determinants of chemotactic signal amplification in Escherichia coli
    • Kim, C., Jackson, M., Lux, R. & Khan, S. Determinants of chemotactic signal amplification in Escherichia coli. J. Mol. Biol. 307, 119-135 (2001).
    • (2001) J. Mol. Biol. , vol.307 , pp. 119-135
    • Kim, C.1    Jackson, M.2    Lux, R.3    Khan, S.4
  • 24
    • 0024281410 scopus 로고
    • Phosphorylation of three proteins in the signalling pathway of bacterial chemotaxis
    • Hess, J. F., Oosawa, K., Kaplan, N. & Simon, M. I. Phosphorylation of three proteins in the signalling pathway of bacterial chemotaxis. Cell 53, 79-87 (1988). An early report showing that the phosphorylation of chemotaxis proteins is a mechanism for signal transaction.
    • (1988) Cell , vol.53 , pp. 79-87
    • Hess, J.F.1    Oosawa, K.2    Kaplan, N.3    Simon, M.I.4
  • 25
    • 0032491213 scopus 로고    scopus 로고
    • Activation of methylesterase CheB: Evidence of a dual role for the regulatory domain
    • Anand, G. S., Goudreau, P. N. & Stock, A. M. Activation of methylesterase CheB: evidence of a dual role for the regulatory domain. Biochemistry 37, 14038-14047 (1998).
    • (1998) Biochemistry , vol.37 , pp. 14038-14047
    • Anand, G.S.1    Goudreau, P.N.2    Stock, A.M.3
  • 26
    • 0027517812 scopus 로고
    • Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria
    • Welch, M., Oosawa, K., Aizawa, S.-I. & Eisenbach, M. Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. Proc. Natl Acad. Sci. USA 90, 8787-8791 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8787-8791
    • Welch, M.1    Oosawa, K.2    Aizawa, S.-I.3    Eisenbach, M.4
  • 27
    • 0031592943 scopus 로고    scopus 로고
    • Distinct regions of bacterial flagellar switch protein FliM interact with FliG, FliN and CheY
    • Token A. S. & Macnab, R. M. Distinct regions of bacterial flagellar switch protein FliM interact with FliG, FliN and CheY. J. Mol. Biol. 273, 623-634 (1997).
    • (1997) J. Mol. Biol. , vol.273 , pp. 623-634
    • Token, A.S.1    Macnab, R.M.2
  • 28
    • 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, M. M., Bren, A., Eisenbach, M. & Dahlquist, F. W. 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 (1999).
    • (1999) J. Mol. Biol. , vol.289 , pp. 1423-1433
    • McEvoy, M.M.1    Bren, A.2    Eisenbach, M.3    Dahlquist, F.W.4
  • 29
    • 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. & Berg, H. C. 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).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12669-12674
    • Sourjik, V.1    Berg, H.C.2
  • 30
    • 0027391963 scopus 로고
    • Proteins antigenically related to methyl-accepting chemotaxis proteins of Escherichia coli detected in a wide range of bacterial species
    • Morgan, D. G., Baumgartner, J. B. & Hazelbauer, G. L. Proteins antigenically related to methyl-accepting chemotaxis proteins of Escherichia coli detected in a wide range of bacterial species. J. Bacteriol. 175, 133-140 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 133-140
    • Morgan, D.G.1    Baumgartner, J.B.2    Hazelbauer, G.L.3
  • 31
    • 0035312774 scopus 로고    scopus 로고
    • Transmembrane signaling in bacterial chemoreceptors
    • Falke, J. J. & Hazelbauer, G. L. Transmembrane signaling in bacterial chemoreceptors. Trends Biochem. Sci. 26, 257-265 (2001).
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 257-265
    • Falke, J.J.1    Hazelbauer, G.L.2
  • 32
    • 0030595334 scopus 로고    scopus 로고
    • High resolution structures of the ligand binding domain of the wild type aspartate receptor
    • Yeh, J. I. et al. High resolution structures of the ligand binding domain of the wild type aspartate receptor. J. Mol. Biol. 262, 186-201 (1996).
    • (1996) J. Mol. Biol. , vol.262 , pp. 186-201
    • Yeh, J.I.1
  • 33
    • 0001690764 scopus 로고    scopus 로고
    • Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor
    • Kim, K. K., Yokota, H. & Kim, S. H. Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor. Nature 400, 787-792 (1999).
    • (1999) Nature , vol.400 , pp. 787-792
    • Kim, K.K.1    Yokota, H.2    Kim, S.H.3
  • 34
    • 10044296990 scopus 로고
    • Structural changes in a transmembrane receptor - Crystal structures of the ligand domain of aspartate chemotaxis receptor with and without aspartate
    • Milbum, M. V. et al. Structural changes in a transmembrane receptor - crystal structures of the ligand domain of aspartate chemotaxis receptor with and without aspartate. Biochemistry 31, 2192 (1992).
    • (1992) Biochemistry , vol.31 , pp. 2192
    • Milbum, M.V.1
  • 35
    • 0023658327 scopus 로고
    • Additive and independent responses to a single receptor: Aspartate and maltose stimuli on the Tar protein
    • Mowbray, S. L. & Koshland, D. E. Jr. Additive and independent responses to a single receptor: aspartate and maltose stimuli on the Tar protein. Cell 50, 171-180 (1987).
    • (1987) Cell , vol.50 , pp. 171-180
    • Mowbray, S.L.1    Koshland Jr., D.E.2
  • 36
    • 0035155805 scopus 로고    scopus 로고
    • Substitutions in the periplasmic domain of low-abundance chemoreceptor Trg that induce or reduce transmembrane signaling: Kinase activation and context effects
    • Beel, B. D. & Hazelbauer, G. L. Substitutions in the periplasmic domain of low-abundance chemoreceptor Trg that induce or reduce transmembrane signaling: kinase activation and context effects. J. Bacteriol. 183, 671-679 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 671-679
    • Beel, B.D.1    Hazelbauer, G.L.2
  • 37
    • 0037022825 scopus 로고    scopus 로고
    • Site-directed rotational resonance solid-state NMR distance measurements probe structure and mechanism in the transmembrane domain of the serine bacterial chemoreceptor
    • Isaac, B., Gallagher, G. J., Balazs, Y. S. & Thompson, L. K. Site-directed rotational resonance solid-state NMR distance measurements probe structure and mechanism in the transmembrane domain of the serine bacterial chemoreceptor. Biochemistry 41, 3025-3036 (2002).
    • (2002) Biochemistry , vol.41 , pp. 3025-3036
    • Isaac, B.1    Gallagher, G.J.2    Balazs, Y.S.3    Thompson, L.K.4
  • 38
    • 0035814825 scopus 로고    scopus 로고
    • Site-directed solid-state NMR measurement of a ligand-induced conformational change in the serine bacterial chemoreceptor
    • Murphy, O. J., Kovacs, F. A., Sicard, E. L. & Thompson, L. K. Site-directed solid-state NMR measurement of a ligand-induced conformational change in the serine bacterial chemoreceptor. Biochemistry 40, 1358-1366 (2001).
    • (2001) Biochemistry , vol.40 , pp. 1358-1366
    • Murphy, O.J.1    Kovacs, F.A.2    Sicard, E.L.3    Thompson, L.K.4
  • 39
    • 0033543590 scopus 로고    scopus 로고
    • A piston model for transmembrane signaling of the aspartate receptor
    • Ottsmann, K. M., Xiao, W., Shin, Y. K. & Koshland, D. E. Jr. A piston model for transmembrane signaling of the aspartate receptor. Science 285, 1751-1754 (1999).
    • (1999) Science , vol.285 , pp. 1751-1754
    • Ottsmann, K.M.1    Xiao, W.2    Shin, Y.K.3    Koshland Jr., D.E.4
  • 40
    • 0024276608 scopus 로고
    • Transmembrane signaling by bacterial chemoreceptors: E. coli transducers with locked signal output
    • Ames, P. & Parkinson, J. S. Transmembrane signaling by bacterial chemoreceptors: E. coli transducers with locked signal output. Cell 55, 817-826 (1988).
    • (1988) Cell , vol.55 , pp. 817-826
    • Ames, P.1    Parkinson, J.S.2
  • 41
    • 0029893940 scopus 로고    scopus 로고
    • Role of α-helical coiled-coil interactions in receptor dimerization, signaling, and adaptation during bacterial chemotaxis
    • Surette, M. G. & Stock, J. B. Role of α-helical coiled-coil interactions in receptor dimerization, signaling, and adaptation during bacterial chemotaxis. J. Biol. Chem. 271, 17966-17973 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 17966-17973
    • Surette, M.G.1    Stock, J.B.2
  • 42
    • 0033104510 scopus 로고    scopus 로고
    • Car: A cytoplasmic sensor responsible for arginine chemotaxis in the archaeon Halobacterium salinarum
    • Storch, K. F., Rudolph, J. & Oesterhelt, D. Car: a cytoplasmic sensor responsible for arginine chemotaxis in the archaeon Halobacterium salinarum. EMBO J. 18, 1146-1158 (1999).
    • (1999) EMBO J. , vol.18 , pp. 1146-1158
    • Storch, K.F.1    Rudolph, J.2    Oesterhelt, D.3
  • 43
    • 0036885987 scopus 로고    scopus 로고
    • TlpC, a novel chemotaxis protein in Rhodobacter sphaeroides, localizes to a discrete region in the cytoplasm
    • Wadhams, G. H. et al. TlpC, a novel chemotaxis protein in Rhodobacter sphaeroides, localizes to a discrete region in the cytoplasm. Mol. Microbiol. 46, 1211-1221 (2002).
    • (2002) Mol. Microbiol. , vol.46 , pp. 1211-1221
    • Wadhams, G.H.1
  • 44
    • 0033548704 scopus 로고    scopus 로고
    • Inversion of thermosensing property of the bacterial receptor Tar by mutations in the second transmembrane region
    • Nishiyama, S., Maruyama, I. N., Homma, M. & Kawagishi, I. Inversion of thermosensing property of the bacterial receptor Tar by mutations in the second transmembrane region. J. Mol. Biol 286, 1275-1284 (1999).
    • (1999) J. Mol. Biol. , vol.286 , pp. 1275-1284
    • Nishiyama, S.1    Maruyama, I.N.2    Homma, M.3    Kawagishi, I.4
  • 45
    • 0042561788 scopus 로고    scopus 로고
    • Probing conservation of HAMP linker structure and signal transduction mechanism through analysis of hybrid sensor kinases
    • Appleman, J. A., Chen, L.L. & Stewart, V. Probing conservation of HAMP linker structure and signal transduction mechanism through analysis of hybrid sensor kinases. J. Bacteriol. 185, 4872-4882 (2003).
    • (2003) J. Bacteriol. , vol.185 , pp. 4872-4882
    • Appleman, J.A.1    Chen, L.L.2    Stewart, V.3
  • 46
    • 0032766134 scopus 로고    scopus 로고
    • The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins
    • Aravind, L. & Ponting, C. P. The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins. FEMS Microbiol. Lett. 176, 111-116 (1999).
    • (1999) FEMS Microbiol. Lett. , vol.176 , pp. 111-116
    • Aravind, L.1    Ponting, C.P.2
  • 47
    • 0023797198 scopus 로고
    • Reversible receptor methylation is essential for normal chemotaxis of Escherichia coli in gradients of aspartic acid
    • Weis, R. M. & Koshland, D. E. Jr. Reversible receptor methylation is essential for normal chemotaxis of Escherichia coli in gradients of aspartic acid. Proc. Natl Acad. Sci. USA 85, 83-67 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 83-67
    • Weis, R.M.1    Koshland Jr., D.E.2
  • 48
    • 0020770030 scopus 로고
    • Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product
    • Kehry, M. R., Bond, M. W., Hunkapiller, M. W. & Dahlquist, F. W. Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product. Proc. Natl Acad. Sci. USA 80, 3599-3603 (1983).
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 3599-3603
    • Kehry, M.R.1    Bond, M.W.2    Hunkapiller, M.W.3    Dahlquist, F.W.4
  • 49
    • 0029979271 scopus 로고    scopus 로고
    • The receptor binding site for the methyltransferase of bacterial chemotaxis is distinct from the sites of methylation
    • Wu, J. G., Li, J. Y., Li, G. Y., Long, D. G. & Weis, R. M. The receptor binding site for the methyltransferase of bacterial chemotaxis is distinct from the sites of methylation. Biochemistry 35, 4984-4993 (1996).
    • (1996) Biochemistry , vol.35 , pp. 4984-4993
    • Wu, J.G.1    Li, J.Y.2    Li, G.Y.3    Long, D.G.4    Weis, R.M.5
  • 50
    • 0032444115 scopus 로고    scopus 로고
    • Comparison in vitro of a high- and a low-abundance chemoreceptor of Escherichia coli: Similar kinase activation but different methyl-accepting activities
    • Barnakov, A. N., Barnakova, L. A. & Hazelbauer, G. L. Comparison in vitro of a high- and a low-abundance chemoreceptor of Escherichia coli: similar kinase activation but different methyl-accepting activities. J. Bacteriol. 180, 6713-6718 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 6713-6718
    • Barnakov, A.N.1    Barnakova, L.A.2    Hazelbauer, G.L.3
  • 51
    • 0030736078 scopus 로고    scopus 로고
    • Methylation of the Escherichia coli chemotaxis receptors: Intra- and interdimer mechanisms
    • Le Moual, H., Quang, T. & Koshland, D. E. Jr. Methylation of the Escherichia coli chemotaxis receptors: intra- and interdimer mechanisms. Biochemistry 36, 13441-13448 (1997).
    • (1997) Biochemistry , vol.36 , pp. 13441-13448
    • Le Moual, H.1    Quang, T.2    Koshland Jr., D.E.3
  • 52
    • 0027476771 scopus 로고
    • Polar location of the chemoreceptor complex in the Escherichia coli cell
    • Maddock, J. R. & Shapiro, L. Polar location of the chemoreceptor complex in the Escherichia coli cell. Science 259, 1717-1723 (1993). The use of immunogold electron microscopy to show for the first time that chemoreceptors cluster at the poles of bacterial cells.
    • (1993) Science , vol.259 , pp. 1717-1723
    • Maddock, J.R.1    Shapiro, L.2
  • 53
    • 0033948223 scopus 로고    scopus 로고
    • Identification and localization of a methyl-accepting chemotaxis protein in Rhodobacter sphaeroides
    • Wadhams, G. H., Martin, A. C. & Armitage, J. P. Identification and localization of a methyl-accepting chemotaxis protein in Rhodobacter sphaeroides. Mol. Microbiol. 36, 1222-1233 (2000).
    • (2000) Mol. Microbiol. , vol.36 , pp. 1222-1233
    • Wadhams, G.H.1    Martin, A.C.2    Armitage, J.P.3
  • 54
    • 0037019023 scopus 로고    scopus 로고
    • Signal transduction: Receptor clusters as information processing arrays
    • Thomason, P. A., Wolanin, P. M. & Stock, J. B. Signal transduction: receptor clusters as information processing arrays. Curr. Biol. 12, R399-R401 (2002).
    • (2002) Curr. Biol. , vol.12
    • Thomason, P.A.1    Wolanin, P.M.2    Stock, J.B.3
  • 55
    • 0033865904 scopus 로고    scopus 로고
    • Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions
    • Sourjik, V. & Berg, H. C. Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions. Mol. Microbiol. 37, 740-751 (2000).
    • (2000) Mol. Microbiol. , vol.37 , pp. 740-751
    • Sourjik, V.1    Berg, H.C.2
  • 56
    • 0034940062 scopus 로고    scopus 로고
    • The roles of the multiple CheW and CheA homologues in chemotaxis and in chemoreceptor localization in Rhodobacter sphaeroides
    • Martin, A. C., Wadhams, G. H. & Armitage, J. P. The roles of the multiple CheW and CheA homologues in chemotaxis and in chemoreceptor localization in Rhodobacter sphaeroides. Mol. Microbiol. 40, 1261-1272 (2001).
    • (2001) Mol. Microbiol. , vol.40 , pp. 1261-1272
    • Martin, A.C.1    Wadhams, G.H.2    Armitage, J.P.3
  • 57
    • 1542618323 scopus 로고    scopus 로고
    • Attractant binding alters arrangement of chemoreceptor dimers within its cluster at a cell pole
    • Homma, M., Shiomi, D., Homma, M. & Kawagishi, I. Attractant binding alters arrangement of chemoreceptor dimers within its cluster at a cell pole. Proc. Natl Acad. Sci. USA 101, 3462-3467 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 3462-3467
    • Homma, M.1    Shiomi, D.2    Homma, M.3    Kawagishi, I.4
  • 58
    • 1242274351 scopus 로고    scopus 로고
    • Crosslinking snapshots of bacterial chemoreceptor squads
    • Studdert, C. A. & Parkinson, J. S. Crosslinking snapshots of bacterial chemoreceptor squads. Proc. Natl Acad. Sci. USA 101, 2117-2122 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 2117-2122
    • Studdert, C.A.1    Parkinson, J.S.2
  • 59
    • 2942748593 scopus 로고    scopus 로고
    • Bacterial chemosensing: Cooperative molecular logic
    • Wolanin, P. M. & Stock, J. B. Bacterial chemosensing: cooperative molecular logic. Curr. Biol. 14, R486-R487 (2004).
    • (2004) Curr. Biol. , vol.14
    • Wolanin, P.M.1    Stock, J.B.2
  • 60
    • 0032492852 scopus 로고    scopus 로고
    • Receptor clustering as a cellular mechanism to control sensitivity
    • Bray, D., Levin, M, D. & Morton, F. C. Receptor clustering as a cellular mechanism to control sensitivity. Nature 393, 85-88 (1998). One of the first papers to propose that chemoreceptor clustering could explain the sensitivity and gain in the chemotaxis pathway.
    • (1998) Nature , vol.393 , pp. 85-88
    • Bray, D.1    Levin, M.2    Morton, F.C.3
  • 61
    • 0037184003 scopus 로고    scopus 로고
    • Organization of the receptor-kinase signaling array that regulates Escherichia coli chemotaxis
    • Levit, M. N., Grebe, T. W. & Stock, J. B. Organization of the receptor-kinase signaling array that regulates Escherichia coli chemotaxis. J. Biol. Chem. 277, 36748-36754 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 36748-36754
    • Levit, M.N.1    Grebe, T.W.2    Stock, J.B.3
  • 62
    • 0036724360 scopus 로고    scopus 로고
    • Conserved amplification of chemotactic responses through chemoreceptor interactions
    • Lamanna, A. C. et al. Conserved amplification of chemotactic responses through chemoreceptor interactions. J. Bacteriol. 184,4981-4987 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 4981-4987
    • Lamanna, A.C.1
  • 63
    • 0037076332 scopus 로고    scopus 로고
    • Collaborative signaling by mixed chemoreceptor teams in Escherichia coli
    • Ames, P., Studdert, C. A., Reiser, R. H. & Parkinson, J. S. Collaborative signaling by mixed chemoreceptor teams in Escherichia coli. Proc. Natl Acad. Sci. USA 99, 7060-7065 (2002).
    • (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
  • 64
    • 2942610579 scopus 로고    scopus 로고
    • Cellular stoichiometries of the components of the chemotaxis signaling complex
    • Li, M. & Hazelbauer, G. L. Cellular stoichiometries of the components of the chemotaxis signaling complex. J. Bacteriol. 186, 3687-3694 (2004). A quantitative western-blot analysis of chemotaxis proteins in cells that were grown under different growth conditions, which showed that although the absolute numbers of the signalling components vary, the stoichiometry between them remains relatively constant.
    • (2004) J. Bacteriol. , vol.186 , pp. 3687-3694
    • Li, M.1    Hazelbauer, G.L.2
  • 65
    • 0033778277 scopus 로고    scopus 로고
    • Molecular model of a lattice of signalling proteins involved in bacterial chemotaxis
    • Shimizu, T. S. et al. Molecular model of a lattice of signalling proteins involved in bacterial chemotaxis. Nature Cell Biol. 2, 792-796 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 792-796
    • Shimizu, T.S.1
  • 66
    • 0030883388 scopus 로고    scopus 로고
    • The Aer protein and the serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior
    • Rebbapragada, A. et al. The Aer protein and the serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior. Proc. Natl Acad. Sci. USA 94, 10541-10546 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10541-10546
    • Rebbapragada, A.1
  • 67
    • 0034705035 scopus 로고    scopus 로고
    • Domain organization and flavin adenine dinucleotide-binding determinants in the aerotaxis signal transducer Aer of Escherichia coli
    • Bibikov, S. I., Barnes, L. A., Gitin, Y. & Parkinson, J. S. Domain organization and flavin adenine dinucleotide-binding determinants in the aerotaxis signal transducer Aer of Escherichia coli. Proc. Natl Acad. Sci. USA 97, 5830-5835 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5830-5835
    • Bibikov, S.I.1    Barnes, L.A.2    Gitin, Y.3    Parkinson, J.S.4
  • 68
    • 0028012225 scopus 로고
    • DcrA, a c-type heme-containing methyl-accepting chemotaxis protein from Desulfovibrio vulgaris Hildenborough, senses the oxygen concentration or redox potential of the environment
    • Fu, R., Wall, J. D. & Voordouw, G. DcrA, a c-type heme-containing methyl-accepting chemotaxis protein from Desulfovibrio vulgaris Hildenborough, senses the oxygen concentration or redox potential of the environment. J. Bacteriol. 176, 344-350 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 344-350
    • Fu, R.1    Wall, J.D.2    Voordouw, G.3
  • 69
    • 0034598826 scopus 로고    scopus 로고
    • Myoglobin-like aerotaxis transducers in Archaea and bacteria
    • Hou, S. et al. Myoglobin-like aerotaxis transducers in Archaea and bacteria. Nature 403, 540-544 (2000).
    • (2000) Nature , vol.403 , pp. 540-544
    • Hou, S.1
  • 70
    • 0032939921 scopus 로고    scopus 로고
    • Elucidation of a PTS-carbohydrate chemotactic signal pathway in Escherichia coli using a time-resolved behavioral assay
    • Lux, R. et al. Elucidation of a PTS-carbohydrate chemotactic signal pathway in Escherichia coli using a time-resolved behavioral assay. Mol. Biol. Cell 10, 1133-1146 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1133-1146
    • Lux, R.1
  • 71
    • 0037189482 scopus 로고    scopus 로고
    • CheA kinase and chemoreceptor interaction surfaces on CheW
    • Boukhvalova, M., VanBruggen, R. & Stewart, R. C. CheA kinase and chemoreceptor interaction surfaces on CheW. J. Biol. Chem. 277, 23596-23603 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 23596-23603
    • Boukhvalova, M.1    VanBruggen, R.2    Stewart, R.C.3
  • 72
    • 0036166306 scopus 로고    scopus 로고
    • The solution structure and interactions of CheW from Thermotoga maritima
    • Griswold, I. J. et al. The solution structure and interactions of CheW from Thermotoga maritima. Nature Struct. Biol. 9, 121-125 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 121-125
    • Griswold, I.J.1
  • 73
    • 0033977153 scopus 로고    scopus 로고
    • Identification of a fourth cheY gene in Rhodobacter sphaeroides and interspecies interaction within the bacterial chemotaxis signal transduction pathway
    • Shah, D. S. et al. Identification of a fourth cheY gene in Rhodobacter sphaeroides and interspecies interaction within the bacterial chemotaxis signal transduction pathway. Mol. Microbiol. 35, 101-112 (2000).
    • (2000) Mol. Microbiol. , vol.35 , pp. 101-112
    • Shah, D.S.1
  • 74
    • 0030889858 scopus 로고    scopus 로고
    • Characterization of the chemotaxis protein CheW from Rhodobacter sphaeroides and its effect on the behaviour of Escherichia coli
    • Hamblin, P. A., Bourne, N. A. & Armitage, J. P. Characterization of the chemotaxis protein CheW from Rhodobacter sphaeroides and its effect on the behaviour of Escherichia coli. Mol. Microbiol 24, 41-51 (1997).
    • (1997) Mol. Microbiol , vol.24 , pp. 41-51
    • Hamblin, P.A.1    Bourne, N.A.2    Armitage, J.P.3
  • 75
    • 0030886624 scopus 로고    scopus 로고
    • A fragment liberated from the Escherichia coli CheA kinase that blocks stimulatory, but not inhibitory, chemoreceptor signaling
    • Morrison, T. B. & Parkinson, J. S. A fragment liberated from the Escherichia coli CheA kinase that blocks stimulatory, but not inhibitory, chemoreceptor signaling. J. Bacteriol. 179, 5543-5550 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 5543-5550
    • Morrison, T.B.1    Parkinson, J.S.2
  • 76
    • 0035903179 scopus 로고    scopus 로고
    • Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis
    • Mourey, L. et al. Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis. J. Biol. Chem. 276, 31074-31082 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 31074-31082
    • Mourey, L.1
  • 77
    • 0033534368 scopus 로고    scopus 로고
    • Structure of CheA, a signal-transducing histidine kinase
    • Bilwes, A. M., Alex, L. A., Crane, B. R. & Simon, M. I. Structure of CheA, a signal-transducing histidine kinase. Cell 96, 131-141 (1999).
    • (1999) Cell , vol.96 , pp. 131-141
    • Bilwes, A.M.1    Alex, L.A.2    Crane, B.R.3    Simon, M.I.4
  • 78
    • 0027502587 scopus 로고
    • The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW
    • Bourret, R. B., Davagnino, J. & Simon, M. I. The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW. J. Bacteriol. 175, 2097-2101 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 2097-2101
    • Bourret, R.B.1    Davagnino, J.2    Simon, M.I.3
  • 79
    • 0033580642 scopus 로고    scopus 로고
    • Mechanism of CheA protein kinase activation in receptor signaling complexes
    • Levit, M. N., Liu, Y. & Stock, J. B. Mechanism of CheA protein kinase activation in receptor signaling complexes, Biochemistry 38, 6651-6658 (1999).
    • (1999) Biochemistry , vol.38 , pp. 6651-6658
    • Levit, M.N.1    Liu, Y.2    Stock, J.B.3
  • 80
    • 0028869205 scopus 로고
    • The response regulators CheB and CheY exhibit competitive binding to the kinase CheA
    • Li, J. Y., Swanson, R. V., Simon, M. I. & Weis, R. M. The response regulators CheB and CheY exhibit competitive binding to the kinase CheA. Biochemistry 34, 14628-14636 (1995).
    • (1995) Biochemistry , vol.34 , pp. 14628-14636
    • Li, J.Y.1    Swanson, R.V.2    Simon, M.I.3    Weis, R.M.4
  • 81
    • 0031975752 scopus 로고    scopus 로고
    • Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
    • Welch, M., Chinardet, N., Mourey, L., Birck, C. & Samama, J. P. Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY. Nature Struct. Biol. 5, 25-29 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 25-29
    • Welch, M.1    Chinardet, N.2    Mourey, L.3    Birck, C.4    Samama, J.P.5
  • 82
    • 0033792542 scopus 로고    scopus 로고
    • Rapid phosphotransfer to CheY from a CheA protein lacking the CheY-binding domain
    • Stewart, R. C., Jahreis, K. & Parkinson, J. S. Rapid phosphotransfer to CheY from a CheA protein lacking the CheY-binding domain. Biochemistry 39, 13157-13165 (2000).
    • (2000) Biochemistry , vol.39 , pp. 13157-13165
    • Stewart, R.C.1    Jahreis, K.2    Parkinson, J.S.3
  • 83
    • 0023723766 scopus 로고
    • Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis
    • Hess, J. F., Bourret, R. B. & Simon, M. I. Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis. Nature 336, 139-143 (1988).
    • (1988) Nature , vol.336 , pp. 139-143
    • Hess, J.F.1    Bourret, R.B.2    Simon, M.I.3
  • 84
    • 0034624879 scopus 로고    scopus 로고
    • The 1.9 Å resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY
    • Halkides, C. J. et al. The 1.9 Å resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY. Biochemistry 33, 5280-5286 (2000).
    • (2000) Biochemistry , vol.33 , pp. 5280-5286
    • Halkides, C.J.1
  • 85
    • 0035844214 scopus 로고    scopus 로고
    • Crystal structure of activated CheY - Comparison with other activated receiver domains
    • Lee, S. Y. et al. Crystal structure of activated CheY - comparison with other activated receiver domains. J. Biol. Chem. 276, 16425-16431 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 16425-16431
    • Lee, S.Y.1
  • 86
    • 0034737324 scopus 로고    scopus 로고
    • NMR structure of activated CheY
    • Cho, H. S. et al. NMR structure of activated CheY. J. Mol. Biol. 297, 543-551 (2000).
    • (2000) J. Mol. Biol. , vol.297 , pp. 543-551
    • Cho, H.S.1
  • 87
    • 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. 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 (1998).
    • (1998) J. Mol. Biol. , vol.278 , pp. 507-514
    • Bren, A.1    Eisenbach, M.2
  • 88
    • 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., Khan, S. & Eisenbach, M. 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). Showed that CheY-P binds to the switch component of the bacterial flagellar motor in a non-cooperative manner, which indicates that any amplification that occurs at the motor occurs after CheY-P binding.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25867-25871
    • Sagi, Y.1    Khan, S.2    Eisenbach, M.3
  • 89
    • 0035174242 scopus 로고    scopus 로고
    • Crystal structure of an activated response regulator bound to its target
    • Lee, S. Y. et al. Crystal structure of an activated response regulator bound to its target Nature Struct. Biol. 8, 52-56 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 52-56
    • Lee, S.Y.1
  • 90
    • 0032856980 scopus 로고    scopus 로고
    • Kinetics of CheY phosphorylation by small molecule phosphodonors
    • Da Re, S. S., Deville-Bonne, D., Tolstykh, T., Veron, M. & Stock, J. B. Kinetics of CheY phosphorylation by small molecule phosphodonors. FEBS Lett. 457, 323-326 (1999).
    • (1999) FEBS Lett. , vol.457 , pp. 323-326
    • Da Re, S.S.1    Deville-Bonne, D.2    Tolstykh, T.3    Veron, M.4    Stock, J.B.5
  • 91
    • 0034996629 scopus 로고    scopus 로고
    • Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis
    • Barak, R. & Eisenbach, M. Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis. Mol. Microbiol. 40, 731-743 (2001).
    • (2001) Mol. Microbiol. , vol.40 , pp. 731-743
    • Barak, R.1    Eisenbach, M.2
  • 92
    • 0030022637 scopus 로고    scopus 로고
    • Oligomerization of the phosphatase CheZ upon interaction with the phosphorylated form of CheY - The signal protein of bacterial chemotaxis
    • Blat, Y. & Eisenbach, M. Oligomerization of the phosphatase CheZ upon interaction with the phosphorylated form of CheY - the signal protein of bacterial chemotaxis, J. Biol. Chem. 271, 1226-1231 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 1226-1231
    • Blat, Y.1    Eisenbach, M.2
  • 93
    • 0030042082 scopus 로고    scopus 로고
    • Mutants with defective phosphatase activity show no phosphorylation- dependent oligomerization of CheZ. The phosphatase of bacterial chemotaxis
    • Blat, Y. & Eisenbach, M. Mutants with defective phosphatase activity show no phosphorylation-dependent oligomerization of CheZ. The phosphatase of bacterial chemotaxis. J. Biol. Chem. 271, 1232-1236 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 1232-1236
    • Blat, Y.1    Eisenbach, M.2
  • 94
    • 0036312369 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of the E.coli chemotaxis phosphatase CheZ
    • Zhao, R., Collins, E. J., Bourret, R. B. & Silversmith, R. E. Structure and catalytic mechanism of the E.coli chemotaxis phosphatase CheZ. Nature Struct. Biol. 9, 570-575 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 570-575
    • Zhao, R.1    Collins, E.J.2    Bourret, R.B.3    Silversmith, R.E.4
  • 95
    • 0032562236 scopus 로고    scopus 로고
    • Phosphotransfer between CheA, CheY1, and CheY2 in the chemotaxis signal transduction chain of Rhizobium meliloti
    • Sourjik, V. & Schmitt, R. Phosphotransfer between CheA, CheY1, and CheY2 in the chemotaxis signal transduction chain of Rhizobium meliloti. Biochemistry 37, 2327-2335 (1998). Identified an alternative signal-termination mechanism, which uses a phosphate sink in a bacterial species that lacks CheZ.
    • (1998) Biochemistry , vol.37 , pp. 2327-2335
    • Sourjik, V.1    Schmitt, R.2
  • 96
    • 0035941366 scopus 로고    scopus 로고
    • Phosphorylation of the response regulator CheV is required for adaptation to attractants during Bacillus subtilis chemotaxis
    • Karatan, E., Saulmon, M. M., Bunn, M. W. & Ordal, G. W. Phosphorylation of the response regulator CheV is required for adaptation to attractants during Bacillus subtilis chemotaxis. J. Biol. Chem. 276, 43618-43626 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 43618-43626
    • Karatan, E.1    Saulmon, M.M.2    Bunn, M.W.3    Ordal, G.W.4
  • 97
    • 0034802293 scopus 로고    scopus 로고
    • Chemotaxis in the human gastric pathogen Helicobacter pylori: Different roles for CheW and the three CheV paralogues, and evidence for CheV2 phosphorylation
    • Pittman, M. S., Goodwin, M. & Kelly, D. J. Chemotaxis in the human gastric pathogen Helicobacter pylori: different roles for CheW and the three CheV paralogues, and evidence for CheV2 phosphorylation. Microbiology 147, 2493-2504 (2001).
    • (2001) Microbiology , vol.147 , pp. 2493-2504
    • Pittman, M.S.1    Goodwin, M.2    Kelly, D.J.3
  • 98
    • 0030884924 scopus 로고    scopus 로고
    • Analysis of a chemotaxis operon from Rhodospirillum centenum
    • Jiang, Z. Y. & Bauer, C. E. Analysis of a chemotaxis operon from Rhodospirillum centenum. J. Bacteriol. 179, 5712-5719 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 5712-5719
    • Jiang, Z.Y.1    Bauer, C.E.2
  • 99
    • 0036435693 scopus 로고    scopus 로고
    • Phosphotransfer in Rhodobacter sphaeroides chemotaxis
    • Porter, S. L. & Armitage, J. P. Phosphotransfer in Rhodobacter sphaeroides chemotaxis. J. Mol. Biol. 324, 35-45 (2002). Showed that different CheA proteins from B. sphaeroides differentially phosphorylate specific RRs.
    • (2002) J. Mol. Biol. , vol.324 , pp. 35-45
    • Porter, S.L.1    Armitage, J.P.2
  • 100
    • 0017360486 scopus 로고
    • Identification of a protein methyltransferase as the cheR gene product in the bacterial sensing system
    • Springer, W. R. & Koshland, D. E. Jr. Identification of a protein methyltransferase as the cheR gene product in the bacterial sensing system. Proc. Natl Acad. Sci. USA 74, 533-537 (1977).
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 533-537
    • Springer, W.R.1    Koshland Jr., D.E.2
  • 101
    • 0020162182 scopus 로고
    • Adaptation in bacterial chemotaxis: CheB-dependent modification permits additional methylations of sensory transducing proteins
    • Kehry, M. R. & Dahlquist, F. W. Adaptation in bacterial chemotaxis: CheB-dependent modification permits additional methylations of sensory transducing proteins. Cell 29, 761-772 (1982).
    • (1982) Cell , vol.29 , pp. 761-772
    • Kehry, M.R.1    Dahlquist, F.W.2
  • 102
    • 0021972574 scopus 로고
    • Sensory adaptation in bacterial chemotaxis - Regulation of demethylation
    • Kehry, M. R., Doak, T. G. & Dahlquist, F. W. Sensory adaptation in bacterial chemotaxis - regulation of demethylation. J. Bacteriol. 163, 983-990 (1985).
    • (1985) J. Bacteriol. , vol.163 , pp. 983-990
    • Kehry, M.R.1    Doak, T.G.2    Dahlquist, F.W.3
  • 103
    • 0031749947 scopus 로고    scopus 로고
    • Chemotaxis receptor recognition by protein methyltransferase CheR
    • Djordjevic, S. & Stock, A. M. Chemotaxis receptor recognition by protein methyltransferase CheR. Nature Struct. Biol. 5, 446-450 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 446-450
    • Djordjevic, S.1    Stock, A.M.2
  • 104
    • 0031569882 scopus 로고    scopus 로고
    • Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine
    • Djordjevic, S. & Stock, A. M. Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine. Strucfure 5, 545-558 (1997).
    • (1997) Strucfure , vol.5 , pp. 545-558
    • Djordjevic, S.1    Stock, A.M.2
  • 105
    • 0036830605 scopus 로고    scopus 로고
    • Dual recognition of the bacterial chemoreceptor by chemotaxis-specific domains of the CheR methyltransferase
    • Shiomi, D., Zhulin, I. B., Homma, M. & Kawagishi, I. Dual recognition of the bacterial chemoreceptor by chemotaxis-specific domains of the CheR methyltransferase. J. Biol. Chem. 277, 42325-42333 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 42325-42333
    • Shiomi, D.1    Zhulin, I.B.2    Homma, M.3    Kawagishi, I.4
  • 106
    • 0032539671 scopus 로고    scopus 로고
    • Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain
    • Djordjevic, S., Goudreau, P. N., Xu, Q., Stock, A. M. & West, A. H. Structural basis for methylesterase CheB regulation by a phosphorylation- activated domain. Proc. Natl Acad. Sci. USA 95, 1381-1386 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 1381-1386
    • Djordjevic, S.1    Goudreau, P.N.2    Xu, Q.3    Stock, A.M.4    West, A.H.5
  • 107
    • 0037188414 scopus 로고    scopus 로고
    • Kinetic basis for the stimulatory effect of phosphorylation on the methylesterase activity of CheB
    • Anand, G. S. & Stock, A. M. Kinetic basis for the stimulatory effect of phosphorylation on the methylesterase activity of CheB. Biochemistry 41, 6752-6760 (2002).
    • (2002) Biochemistry , vol.41 , pp. 6752-6760
    • Anand, G.S.1    Stock, A.M.2
  • 108
    • 0031767491 scopus 로고    scopus 로고
    • Stimulus response coupling in bacterial chemotaxis: Receptor dimers in signalling arrays
    • Levit, M. N., Liu, Y. & Stock, J. B. Stimulus response coupling in bacterial chemotaxis: receptor dimers in signalling arrays. Mol. Microbiol. 30, 459-466 (1998).
    • (1998) Mol. Microbiol. , vol.30 , pp. 459-466
    • Levit, M.N.1    Liu, Y.2    Stock, J.B.3
  • 109
    • 2942584862 scopus 로고    scopus 로고
    • Diversity in chemotaxis mechanisms among the bacteria and Archaea
    • Szurmant, H. & Ordal, G. W. Diversity in chemotaxis mechanisms among the bacteria and Archaea. Microbiol. Mol. Biol. Rev. 68, 301-319 (2004).
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 301-319
    • Szurmant, H.1    Ordal, G.W.2
  • 110
    • 0027819003 scopus 로고
    • Purification and characterization of Bacillus subtilis CheY
    • Bischoff, D. S., Bourret, R. B., Kirsch, M. L. & Ordal, G. W. Purification and characterization of Bacillus subtilis CheY. Biochemistry 32, 9256-9261 (1993).
    • (1993) Biochemistry , vol.32 , pp. 9256-9261
    • Bischoff, D.S.1    Bourret, R.B.2    Kirsch, M.L.3    Ordal, G.W.4
  • 111
    • 0034637533 scopus 로고    scopus 로고
    • Selective methylation changes on the Bacillus subtilis chemotaxis receptor McpB promote adaptation
    • Zimmer, M. A., Tiu, J., Collins, M. A. & Ordal, G. W. Selective methylation changes on the Bacillus subtilis chemotaxis receptor McpB promote adaptation. J. Biol. Chemistry 275, 24264-24272 (2000).
    • (2000) J. Biol. Chemistry , vol.275 , pp. 24264-24272
    • Zimmer, M.A.1    Tiu, J.2    Collins, M.A.3    Ordal, G.W.4
  • 112
    • 0028286556 scopus 로고
    • Identification of volatile forms of methyl groups released by Halobacterium salinarium
    • Nordmann, B. et al. Identification of volatile forms of methyl groups released by Halobacterium salinarium. J. Biol. Chem. 269, 16449-16454 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 16449-16454
    • Nordmann, B.1
  • 113
    • 0024354885 scopus 로고
    • Novel methyl transfer during chemotaxis in Bacillus subtilis
    • Thoelke, M. S., Kirby, J. R. & Ordal, G. W. Novel methyl transfer during chemotaxis in Bacillus subtilis. Biochemistry 28, 5585-5589 (1989).
    • (1989) Biochemistry , vol.28 , pp. 5585-5589
    • Thoelke, M.S.1    Kirby, J.R.2    Ordal, G.W.3
  • 114
    • 0030905518 scopus 로고    scopus 로고
    • Methanol production during chemotaxis to amino acids in Bacillus subtilis
    • Kirby, J. R., Kristich, C. J., Feinberg, S. L. & Ordal, G. W. Methanol production during chemotaxis to amino acids in Bacillus subtilis. Mol. Microbiol. 24, 869-878 (1997).
    • (1997) Mol. Microbiol. , vol.24 , pp. 869-878
    • Kirby, J.R.1    Kristich, C.J.2    Feinberg, S.L.3    Ordal, G.W.4
  • 115
    • 0027194322 scopus 로고
    • Chemotactic methylesterase promotes adaptation to high concentrations of attractant in Bacillus subtilis
    • Kirsch, M. L., Peters, P. D., Hanlon, D. W., Kirby, J. R. & Ordal, G. W. Chemotactic methylesterase promotes adaptation to high concentrations of attractant in Bacillus subtilis. J. Biol. Chem. 268, 18610-18616 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 18610-18616
    • Kirsch, M.L.1    Peters, P.D.2    Hanlon, D.W.3    Kirby, J.R.4    Ordal, G.W.5
  • 116
    • 0029787821 scopus 로고    scopus 로고
    • CheC and CheD interact to regulate methylation of Bacillus subtilis methyl-accepting chemotaxis proteins
    • Rosario, M. M. & Ordal G. W. CheC and CheD interact to regulate methylation of Bacillus subtilis methyl-accepting chemotaxis proteins. Mol. Microbiol. 21, 511-518 (1996).
    • (1996) Mol. Microbiol. , vol.21 , pp. 511-518
    • Rosario, M.M.1    Ordal, G.W.2
  • 117
    • 2542460079 scopus 로고    scopus 로고
    • Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the Chemotactic signal transduction cascade
    • Szurmant, H., Muff, T. J. & Ordal, G. W. Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the Chemotactic signal transduction cascade. J. Biol. Chem. 279, 21787-21792 (2004). Identified roles for extra chemotaxis proteins in B. subtilis.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21787-21792
    • Szurmant, H.1    Muff, T.J.2    Ordal, G.W.3
  • 118
    • 0036433477 scopus 로고    scopus 로고
    • The third chemotaxis locus of Rhodobacter sphaeroides is essential for chemotaxis
    • Porter, S. L., Warren, A. V., Martin, A. C. & Armitage, J. P. The third chemotaxis locus of Rhodobacter sphaeroides is essential for chemotaxis. Mol. Microbiol. 46, 1081-1094 (2002).
    • (2002) Mol. Microbiol. , vol.46 , pp. 1081-1094
    • Porter, S.L.1    Warren, A.V.2    Martin, A.C.3    Armitage, J.P.4
  • 119
    • 0242606200 scopus 로고    scopus 로고
    • Targeting of two signal transduction pathways to different regions of the bacterial cell
    • Wadhams, G. H., Warren, A. V., Martin, A. C. & Armitage, J. P. Targeting of two signal transduction pathways to different regions of the bacterial cell. Mol. Microbiol. 50, 763-770 (2003). Showed for the first time that the components of two chemotaxis pathways are physically separated within a bacterial cell.
    • (2003) Mol. Microbiol. , vol.50 , pp. 763-770
    • Wadhams, G.H.1    Warren, A.V.2    Martin, A.C.3    Armitage, J.P.4
  • 120
    • 10044250926 scopus 로고    scopus 로고
    • Chemotaxis in Rhodobacter sphaeroides requires an atypical histidine protein kinase
    • 12 Oct (doi:10.1074/jbc.M 408855200)
    • Porter, S. L. & Armitage, J. P. Chemotaxis in Rhodobacter sphaeroides requires an atypical histidine protein kinase. J. Biol. Chem. 12 Oct 2004 (doi:10.1074/jbc.M408855200).
    • (2004) J. Biol. Chem.
    • Porter, S.L.1    Armitage, J.P.2
  • 121
    • 0032807472 scopus 로고    scopus 로고
    • The Chemotactic response of Vibrio anguillarum to fish intestinal mucus is mediated by a combination of multiple mucus components
    • O'Toole, R. et al. The Chemotactic response of Vibrio anguillarum to fish intestinal mucus is mediated by a combination of multiple mucus components. J. Bacteriol. 181, 4308-4317 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 4308-4317
    • O'Toole, R.1
  • 122
    • 0032005154 scopus 로고    scopus 로고
    • Opine catabolic loci from Agrobacterium plasmids confer chemotaxis to their cognate substrates
    • Kim, H. & Farrand, S. K. Opine catabolic loci from Agrobacterium plasmids confer chemotaxis to their cognate substrates. Mol. Plant Microbe Interact. 11, 131-143 (1998).
    • (1998) Mol. Plant Microbe Interact. , vol.11 , pp. 131-143
    • Kim, H.1    Farrand, S.K.2
  • 123
    • 0141989893 scopus 로고    scopus 로고
    • Quorum sensing-dependent biofilms enhance colonization in Vibrio cholerae
    • Zhu, J. Mekalanos, J. J. Quorum sensing-dependent biofilms enhance colonization in Vibrio cholerae. Dev. Cell 5, 647-656 (2003).
    • (2003) Dev. Cell , vol.5 , pp. 647-656
    • Zhu, J.1    Mekalanos, J.J.2
  • 124
    • 1842737591 scopus 로고    scopus 로고
    • Both chemotaxis and net motility greatly influence the infectivity of Vibrio cholerae
    • Butler, S. M. & Camilli, A. Both chemotaxis and net motility greatly influence the infectivity of Vibrio cholerae. Proc. Natl Acad. Sci. USA 101, 5018-5023 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 5018-5023
    • Butler, S.M.1    Camilli, A.2
  • 125
    • 0033002579 scopus 로고    scopus 로고
    • Chemotaxis of Rhizobium SP.S2 towards Cajanus cajan root exudate and its major components
    • Pandya, S., Iyer, P., Gaitonde, V., Parekh, T. & Desai, A. Chemotaxis of Rhizobium SP.S2 towards Cajanus cajan root exudate and its major components. Curr. Microbiol. 38, 205-209 (1999).
    • (1999) Curr. Microbiol. , vol.38 , pp. 205-209
    • Pandya, S.1    Iyer, P.2    Gaitonde, V.3    Parekh, T.4    Desai, A.5
  • 126
    • 0037610101 scopus 로고    scopus 로고
    • 54-dependent transcriptional activator in Vibrio fischeri, is required for motility and symbiotic light-organ colonization
    • 54-dependent transcriptional activator in Vibrio fischeri, is required for motility and symbiotic light-organ colonization. J. Bacteriol. 185, 3547-3557 (2003).
    • (2003) J. Bacteriol. , vol.185 , pp. 3547-3557
    • Millikan, D.S.1    Ruby, E.G.2
  • 128
    • 0036809197 scopus 로고    scopus 로고
    • Anaerobic biofilm infections in cystic fibrosis
    • Costerton, J. W. Anaerobic biofilm infections in cystic fibrosis. Mol. Cell 10, 699-700 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 699-700
    • Costerton, J.W.1
  • 129
    • 0345060796 scopus 로고    scopus 로고
    • Chemical communication among bacteria
    • Taga, M. E. & Bassler, B. L. Chemical communication among bacteria. Proc. Natl Acad. Sci. USA 100, 14549-14554 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 14549-14554
    • Taga, M.E.1    Bassler, B.L.2
  • 130
    • 0041673353 scopus 로고    scopus 로고
    • The rotary motor of bacterial flagella
    • Berg, H. C. The rotary motor of bacterial flagella. Annu. Rev. Biochem. 72, 19-54 (2003). A comprehensive review of the mechanism of rotation of the bacterial flagellar motor.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 19-54
    • Berg, H.C.1
  • 131
    • 0026614338 scopus 로고
    • Polar and ateral flagellar motors of marine Vibrio are driven by dffferent ion-motive forces
    • Atsumi, T., McCarter, L. & Imae, Y. Polar and ateral flagellar motors of marine Vibrio are driven by dffferent ion-motive forces. Nature 355, 182-184 (1992).
    • (1992) Nature , vol.355 , pp. 182-184
    • Atsumi, T.1    McCarter, L.2    Imae, Y.3
  • 132
    • 0036405357 scopus 로고    scopus 로고
    • Type IV pili and twitching motility
    • Mattick, J. S. Type IV pili and twitching motility. Annu. Rev. Microbiol. 56, 289-314 (2002).
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 289-314
    • Mattick, J.S.1
  • 133
    • 1142267977 scopus 로고    scopus 로고
    • Coupling cell movement to multicellular development in Myxobacteria
    • Kaiser, D. Coupling cell movement to multicellular development in Myxobacteria. Nature Rev. Microbiol. 1, 45-54 (2003).
    • (2003) Nature Rev. Microbiol. , vol.1 , pp. 45-54
    • Kaiser, D.1
  • 134
    • 0034769801 scopus 로고    scopus 로고
    • Bacterial gliding motility: Multiple mechanisms for cell movement over surfaces
    • McBride, M. J. Bacterial gliding motility: multiple mechanisms for cell movement over surfaces. Annu. Rev. Microbiol. 55, 49-75 (2001).
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 49-75
    • McBride, M.J.1
  • 136
    • 0032837788 scopus 로고    scopus 로고
    • Transformations in flagellar structure of Rhodobacter sphaeroides and possible relationship to changes in swimming speed
    • Armitage, J. P., Pitta, T. P., Vigeant, M. A., Packer, H. L. & Ford, R. M. Transformations in flagellar structure of Rhodobacter sphaeroides and possible relationship to changes in swimming speed. J. Bacteriol. 181, 4825-4833 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 4825-4833
    • Armitage, J.P.1    Pitta, T.P.2    Vigeant, M.A.3    Packer, H.L.4    Ford, R.M.5
  • 137
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab, R. M. How bacteria assemble flagella. Annu. Rev. Microbiol. 57, 77-100 (2003). A review of the process of bacterial flagella assembly.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 77-100
    • Macnab, R.M.1
  • 138
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • Hueck, C. J. Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol. Mol. Biol. Rev. 62, 379-433 (1998).
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 139
    • 0037333239 scopus 로고    scopus 로고
    • Rotary protein motors
    • Oster, G. & Wang, H. Rotary protein motors. Trends Cell Biol. 13, 114-121 (2003).
    • (2003) Trends Cell Biol. , vol.13 , pp. 114-121
    • Oster, G.1    Wang, H.2
  • 140
    • 0027203466 scopus 로고
    • Chemotaxis plays a role in the social behaviour of Myxococcus xanthus
    • Shi, W., Kohler, T. & Zusman, D. R. Chemotaxis plays a role in the social behaviour of Myxococcus xanthus. Mol. Microbiol. 9, 601-611 (1993).
    • (1993) Mol. Microbiol. , vol.9 , pp. 601-611
    • Shi, W.1    Kohler, T.2    Zusman, D.R.3
  • 141
    • 0034669386 scopus 로고    scopus 로고
    • Phenotypic analyses of frz and dif double mutants of Myxococcus xanthus
    • Shi, W. Y., Yang, Z. M., Sun, H., Lancero, H. & Tong, L. M. Phenotypic analyses of frz and dif double mutants of Myxococcus xanthus. FEMS Microbiol. Lett. 192, 211-215 (2000).
    • (2000) FEMS Microbiol. Lett. , vol.192 , pp. 211-215
    • Shi, W.Y.1    Yang, Z.M.2    Sun, H.3    Lancero, H.4    Tong, L.M.5
  • 142
    • 0037452669 scopus 로고    scopus 로고
    • Chemosensory regulation of developmental gene expression in Myxococcus xanthus
    • Kirby, J. R. & Zusman, D. R. Chemosensory regulation of developmental gene expression in Myxococcus xanthus. Proc. Natl Acad. Sci. USA 100, 2008-2013 (2003). Provides an example of an operon that encodes chemotaxis-protein homologues that are not involved in the regulation of bacterial motility.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2008-2013
    • Kirby, J.R.1    Zusman, D.R.2
  • 143
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. & Wuthrich, K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-61 (1996).
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-61
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 144
    • 0037458820 scopus 로고    scopus 로고
    • Genomics: Molecular prodigality
    • Bray, D. Genomics: molecular prodigality. Science 299, 1189-1190 (2003).
    • (2003) Science , vol.299 , pp. 1189-1190
    • Bray, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.