메뉴 건너뛰기




Volumn 5, Issue 9, 2016, Pages 989-1001

Engineering Hybrid Chemotaxis Receptors in Bacteria

Author keywords

chemotaxis; extracellular sensory domain; histidine kinase; hybrid chemoreceptors; ligand; methyl accepting chemotaxis protein

Indexed keywords

BACTERIAL PROTEIN; PROTEIN HISTIDINE KINASE; RECEPTOR; TAR RECEPTOR; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; HYBRID PROTEIN; LIGAND;

EID: 84987918369     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/acssynbio.6b00053     Document Type: Article
Times cited : (50)

References (58)
  • 1
    • 84861836686 scopus 로고    scopus 로고
    • Responding to chemical gradients: Bacterial chemotaxis
    • Sourjik, V. and Wingreen, N. S. (2012) Responding to chemical gradients: bacterial chemotaxis Curr. Opin. Cell Biol. 24, 262-268 10.1016/j.ceb.2011.11.008
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 262-268
    • Sourjik, V.1    Wingreen, N.S.2
  • 2
    • 67651219110 scopus 로고    scopus 로고
    • Engineering bacterial signals and sensors
    • Salis, H., Tamsir, A., and Voigt, C. (2009) Engineering bacterial signals and sensors Contrib. Microbiol. 16, 194-225 10.1159/000219381
    • (2009) Contrib. Microbiol. , vol.16 , pp. 194-225
    • Salis, H.1    Tamsir, A.2    Voigt, C.3
  • 3
    • 10044252242 scopus 로고    scopus 로고
    • Making sense of it all: Bacterial chemotaxis
    • Wadhams, G. H. and Armitage, J. P. (2004) Making sense of it all: bacterial chemotaxis Nat. Rev. Mol. Cell Biol. 5, 1024-1037 10.1038/nrm1524
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 1024-1037
    • Wadhams, G.H.1    Armitage, J.P.2
  • 4
    • 2942584862 scopus 로고    scopus 로고
    • Diversity in chemotaxis mechanisms among the bacteria and archaea
    • Szurmant, H. and Ordal, G. W. (2004) Diversity in chemotaxis mechanisms among the bacteria and archaea Microbiol. Mol. Biol. Rev. 68, 301-319 10.1128/MMBR.68.2.301-319.2004
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 301-319
    • Szurmant, H.1    Ordal, G.W.2
  • 5
    • 84872236877 scopus 로고    scopus 로고
    • Bacterial chemotaxis: The early years of molecular studies
    • Hazelbauer, G. L. (2012) Bacterial chemotaxis: the early years of molecular studies Annu. Rev. Microbiol. 66, 285-303 10.1146/annurev-micro-092611-150120
    • (2012) Annu. Rev. Microbiol. , vol.66 , pp. 285-303
    • Hazelbauer, G.L.1
  • 7
    • 78751525262 scopus 로고    scopus 로고
    • Chemotaxis to the quorum-sensing signal AI-2 requires the Tsr chemoreceptor and the periplasmic LsrB AI-2-binding protein
    • Hegde, M., Englert, D. L., Schrock, S., Cohn, W. B., Vogt, C., Wood, T. K., Manson, M. D., and Jayaraman, A. (2011) Chemotaxis to the quorum-sensing signal AI-2 requires the Tsr chemoreceptor and the periplasmic LsrB AI-2-binding protein J. Bacteriol. 193, 768-773 10.1128/JB.01196-10
    • (2011) J. Bacteriol. , vol.193 , pp. 768-773
    • Hegde, M.1    Englert, D.L.2    Schrock, S.3    Cohn, W.B.4    Vogt, C.5    Wood, T.K.6    Manson, M.D.7    Jayaraman, A.8
  • 8
    • 84927704178 scopus 로고    scopus 로고
    • Bacterial chemotaxis to xenobiotic chemicals and naturally-occurring analogs
    • Parales, R. E., Luu, R. A., Hughes, J. G., and Ditty, J. L. (2015) Bacterial chemotaxis to xenobiotic chemicals and naturally-occurring analogs Curr. Opin. Biotechnol. 33, 318-326 10.1016/j.copbio.2015.03.017
    • (2015) Curr. Opin. Biotechnol. , vol.33 , pp. 318-326
    • Parales, R.E.1    Luu, R.A.2    Hughes, J.G.3    Ditty, J.L.4
  • 9
    • 73949084950 scopus 로고    scopus 로고
    • Leptospira and leptospirosis.
    • Adler, B. and de la Pena Moctezuma, A. (2010) Leptospira and leptospirosis. Vet. Microbiol. 140, 287-296 10.1016/j.vetmic.2009.03.012
    • (2010) Vet. Microbiol. , vol.140 , pp. 287-296
    • Adler, B.1    De La Pena Moctezuma, A.2
  • 10
    • 84937635648 scopus 로고    scopus 로고
    • Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update
    • Parkinson, J. S., Hazelbauer, G. L., and Falke, J. J. (2015) Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update Trends Microbiol. 23, 257-266 10.1016/j.tim.2015.03.003
    • (2015) Trends Microbiol. , vol.23 , pp. 257-266
    • Parkinson, J.S.1    Hazelbauer, G.L.2    Falke, J.J.3
  • 11
    • 77949917744 scopus 로고    scopus 로고
    • Bacterial chemoreceptors: Providing enhanced features to two-component signaling
    • Hazelbauer, G. L. and Lai, W. C. (2010) Bacterial chemoreceptors: providing enhanced features to two-component signaling Curr. Opin. Microbiol. 13, 124-132 10.1016/j.mib.2009.12.014
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 124-132
    • Hazelbauer, G.L.1    Lai, W.C.2
  • 12
    • 37749029507 scopus 로고    scopus 로고
    • Bacterial chemoreceptors: High-performance signaling in networked arrays
    • Hazelbauer, G. L., Falke, J. J., and Parkinson, J. S. (2008) Bacterial chemoreceptors: high-performance signaling in networked arrays Trends Biochem. Sci. 33, 9-19 10.1016/j.tibs.2007.09.014
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 9-19
    • Hazelbauer, G.L.1    Falke, J.J.2    Parkinson, J.S.3
  • 13
    • 78249236863 scopus 로고    scopus 로고
    • Sensing of environmental signals: Classification of chemoreceptors according to the size of their ligand binding regions
    • Lacal, J., Garcia-Fontana, C., Munoz-Martinez, F., Ramos, J. L., and Krell, T. (2010) Sensing of environmental signals: classification of chemoreceptors according to the size of their ligand binding regions Environ. Microbiol. 12, 2873-2884 10.1111/j.1462-2920.2010.02325.x
    • (2010) Environ. Microbiol. , vol.12 , pp. 2873-2884
    • Lacal, J.1    Garcia-Fontana, C.2    Munoz-Martinez, F.3    Ramos, J.L.4    Krell, T.5
  • 14
    • 28944454614 scopus 로고    scopus 로고
    • Four-helix bundle: A ubiquitous sensory module in prokaryotic signal transduction
    • Ulrich, L. E. and Zhulin, I. B. (2005) Four-helix bundle: a ubiquitous sensory module in prokaryotic signal transduction Bioinformatics 21 (Suppl 3) iii45-48 10.1093/bioinformatics/bti1204
    • (2005) Bioinformatics , vol.21 , pp. iii45-48
    • Ulrich, L.E.1    Zhulin, I.B.2
  • 15
    • 77949918665 scopus 로고    scopus 로고
    • Sensor domains of two-component regulatory systems
    • Cheung, J. and Hendrickson, W. A. (2010) Sensor domains of two-component regulatory systems Curr. Opin. Microbiol. 13, 116-123 10.1016/j.mib.2010.01.016
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 116-123
    • Cheung, J.1    Hendrickson, W.A.2
  • 16
    • 84900460731 scopus 로고    scopus 로고
    • The HBM domain: Introducing bimodularity to bacterial sensing
    • Ortega, A. and Krell, T. (2014) The HBM domain: introducing bimodularity to bacterial sensing Protein Sci. 23, 332-336 10.1002/pro.2410
    • (2014) Protein Sci. , vol.23 , pp. 332-336
    • Ortega, A.1    Krell, T.2
  • 17
    • 0037333759 scopus 로고    scopus 로고
    • The NIT domain: A predicted nitrate-responsive module in bacterial sensory receptors
    • Shu, C. J., Ulrich, L. E., and Zhulin, I. B. (2003) The NIT domain: a predicted nitrate-responsive module in bacterial sensory receptors Trends Biochem. Sci. 28, 121-124 10.1016/S0968-0004(03)00032-X
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 121-124
    • Shu, C.J.1    Ulrich, L.E.2    Zhulin, I.B.3
  • 18
    • 84925492168 scopus 로고    scopus 로고
    • Bacterial chemoreceptors and chemoeffectors
    • Bi, S. and Lai, L. (2015) Bacterial chemoreceptors and chemoeffectors Cell. Mol. Life Sci. 72, 691-708 10.1007/s00018-014-1770-5
    • (2015) Cell. Mol. Life Sci. , vol.72 , pp. 691-708
    • Bi, S.1    Lai, L.2
  • 20
    • 29444451565 scopus 로고    scopus 로고
    • Changing the specificity of a bacterial chemoreceptor
    • Derr, P., Boder, E., and Goulian, M. (2006) Changing the specificity of a bacterial chemoreceptor J. Mol. Biol. 355, 923-932 10.1016/j.jmb.2005.11.025
    • (2006) J. Mol. Biol. , vol.355 , pp. 923-932
    • Derr, P.1    Boder, E.2    Goulian, M.3
  • 21
    • 84871012696 scopus 로고    scopus 로고
    • Opposite responses by different chemoreceptors set a tunable preference point in Escherichia coli pH taxis
    • Yang, Y. and Sourjik, V. (2012) Opposite responses by different chemoreceptors set a tunable preference point in Escherichia coli pH taxis Mol. Microbiol. 86, 1482-1489 10.1111/mmi.12070
    • (2012) Mol. Microbiol. , vol.86 , pp. 1482-1489
    • Yang, Y.1    Sourjik, V.2
  • 22
    • 0030660403 scopus 로고    scopus 로고
    • High- and low-abundance chemoreceptors in Escherichia coli: Differential activities associated with closely related cytoplasmic domains
    • Feng, X., Baumgartner, J. W., and Hazelbauer, G. L. (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
  • 23
    • 0031931506 scopus 로고    scopus 로고
    • Chimeric chemoreceptors in Escherichia coli: Signaling properties of Tar-Tap and Tap-Tar hybrids
    • Weerasuriya, S., Schneider, B. M., and Manson, M. D. (1998) Chimeric chemoreceptors in Escherichia coli: signaling properties of Tar-Tap and Tap-Tar hybrids J. Bacteriol. 180, 914-920
    • (1998) J. Bacteriol. , vol.180 , pp. 914-920
    • Weerasuriya, S.1    Schneider, B.M.2    Manson, M.D.3
  • 24
    • 0037340214 scopus 로고    scopus 로고
    • The conserved cytoplasmic module of the transmembrane chemoreceptor McpC mediates carbohydrate chemotaxis in Bacillus subtilis
    • Kristich, C. J., Glekas, G. D., and Ordal, G. W. (2003) The conserved cytoplasmic module of the transmembrane chemoreceptor McpC mediates carbohydrate chemotaxis in Bacillus subtilis Mol. Microbiol. 47, 1353-1366 10.1046/j.1365-2958.2003.03375.x
    • (2003) Mol. Microbiol. , vol.47 , pp. 1353-1366
    • Kristich, C.J.1    Glekas, G.D.2    Ordal, G.W.3
  • 25
    • 84928435692 scopus 로고    scopus 로고
    • Correlation between signal input and output in PctA and PctB amino acid chemoreceptor of Pseudomonas aeruginosa
    • Reyes-Darias, J. A., Yang, Y., Sourjik, V., and Krell, T. (2015) Correlation between signal input and output in PctA and PctB amino acid chemoreceptor of Pseudomonas aeruginosa Mol. Microbiol. 96, 513-525 10.1111/mmi.12953
    • (2015) Mol. Microbiol. , vol.96 , pp. 513-525
    • Reyes-Darias, J.A.1    Yang, Y.2    Sourjik, V.3    Krell, T.4
  • 27
    • 0036091152 scopus 로고    scopus 로고
    • A NarX-Tar chimera mediates repellent chemotaxis to nitrate and nitrite
    • Ward, S. M., Delgado, A., Gunsalus, R. P., and Manson, M. D. (2002) A NarX-Tar chimera mediates repellent chemotaxis to nitrate and nitrite Mol. Microbiol. 44, 709-719 10.1046/j.1365-2958.2002.02902.x
    • (2002) Mol. Microbiol. , vol.44 , pp. 709-719
    • Ward, S.M.1    Delgado, A.2    Gunsalus, R.P.3    Manson, M.D.4
  • 28
    • 36549084978 scopus 로고    scopus 로고
    • Chemotaxis mediated by NarX-FrzCD chimeras and nonadapting repellent responses in Myxococcus xanthus
    • Xu, Q., Black, W. P., Mauriello, E. M., Zusman, D. R., and Yang, Z. (2007) Chemotaxis mediated by NarX-FrzCD chimeras and nonadapting repellent responses in Myxococcus xanthus Mol. Microbiol. 66, 1370-1381 10.1111/j.1365-2958.2007.05996.x
    • (2007) Mol. Microbiol. , vol.66 , pp. 1370-1381
    • Xu, Q.1    Black, W.P.2    Mauriello, E.M.3    Zusman, D.R.4    Yang, Z.5
  • 29
    • 0026315513 scopus 로고
    • Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand
    • Milburn, M. V., Prive, G. G., Milligan, D. L., Scott, W. G., Yeh, J., Jancarik, J., Koshland, D. E., Jr., and Kim, S. H. (1991) Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand Science 254, 1342-1347 10.1126/science.1660187
    • (1991) Science , vol.254 , pp. 1342-1347
    • Milburn, M.V.1    Prive, G.G.2    Milligan, D.L.3    Scott, W.G.4    Yeh, J.5    Jancarik, J.6    Koshland, Jr.D.E.7    Kim, S.H.8
  • 30
    • 82755171841 scopus 로고    scopus 로고
    • Ligand specificity determined by differentially arranged common ligand-binding residues in bacterial amino acid chemoreceptors Tsr and Tar
    • Tajima, H., Imada, K., Sakuma, M., Hattori, F., Nara, T., Kamo, N., Homma, M., and Kawagishi, I. (2011) Ligand specificity determined by differentially arranged common ligand-binding residues in bacterial amino acid chemoreceptors Tsr and Tar J. Biol. Chem. 286, 42200-42210 10.1074/jbc.M111.221887
    • (2011) J. Biol. Chem. , vol.286 , pp. 42200-42210
    • Tajima, H.1    Imada, K.2    Sakuma, M.3    Hattori, F.4    Nara, T.5    Kamo, N.6    Homma, M.7    Kawagishi, I.8
  • 31
    • 84855403705 scopus 로고    scopus 로고
    • Phenol sensing by Escherichia coli chemoreceptors: A nonclassical mechanism
    • Pham, H. T. and Parkinson, J. S. (2011) Phenol sensing by Escherichia coli chemoreceptors: a nonclassical mechanism J. Bacteriol. 193, 6597-6604 10.1128/JB.05987-11
    • (2011) J. Bacteriol. , vol.193 , pp. 6597-6604
    • Pham, H.T.1    Parkinson, J.S.2
  • 33
    • 0037059759 scopus 로고    scopus 로고
    • Sensing of cytoplasmic pH by bacterial chemoreceptors involves the linker region that connects the membrane-spanning and the signal-modulating helices
    • Umemura, T., Matsumoto, Y., Ohnishi, K., Homma, M., and Kawagishi, I. (2002) Sensing of cytoplasmic pH by bacterial chemoreceptors involves the linker region that connects the membrane-spanning and the signal-modulating helices J. Biol. Chem. 277, 1593-1598 10.1074/jbc.M109930200
    • (2002) J. Biol. Chem. , vol.277 , pp. 1593-1598
    • Umemura, T.1    Matsumoto, Y.2    Ohnishi, K.3    Homma, M.4    Kawagishi, I.5
  • 34
    • 59649092359 scopus 로고    scopus 로고
    • Structural analysis of ligand stimulation of the histidine kinase NarX
    • Cheung, J. and Hendrickson, W. A. (2009) Structural analysis of ligand stimulation of the histidine kinase NarX Structure 17, 190-201 10.1016/j.str.2008.12.013
    • (2009) Structure , vol.17 , pp. 190-201
    • Cheung, J.1    Hendrickson, W.A.2
  • 35
    • 0029006481 scopus 로고
    • Nitrate repression of the Escherichia coli pfl operon is mediated by the dual sensors NarQ and NarX and the dual regulators NarL and NarP
    • Kaiser, M. and Sawers, G. (1995) Nitrate repression of the Escherichia coli pfl operon is mediated by the dual sensors NarQ and NarX and the dual regulators NarL and NarP J. Bacteriol. 177, 3647-3655
    • (1995) J. Bacteriol. , vol.177 , pp. 3647-3655
    • Kaiser, M.1    Sawers, G.2
  • 36
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22, 4673-4680 10.1093/nar/22.22.4673
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 37
    • 33646597727 scopus 로고    scopus 로고
    • Loss- and gain-of-function mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer
    • Buron-Barral, M. C., Gosink, K. K., and Parkinson, J. S. (2006) Loss- and gain-of-function mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer J. Bacteriol. 188, 3477-3486 10.1128/JB.188.10.3477-3486.2006
    • (2006) J. Bacteriol. , vol.188 , pp. 3477-3486
    • Buron-Barral, M.C.1    Gosink, K.K.2    Parkinson, J.S.3
  • 38
    • 0037039384 scopus 로고    scopus 로고
    • Receptor sensitivity in bacterial chemotaxis
    • Sourjik, V. and Berg, H. C. (2002) Receptor sensitivity in bacterial chemotaxis Proc. Natl. Acad. Sci. U. S. A. 99, 123-127 10.1073/pnas.011589998
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 123-127
    • Sourjik, V.1    Berg, H.C.2
  • 39
    • 1842473065 scopus 로고    scopus 로고
    • Functional interactions between receptors in bacterial chemotaxis
    • Sourjik, V. and Berg, H. C. (2004) Functional interactions between receptors in bacterial chemotaxis Nature 428, 437-441 10.1038/nature02406
    • (2004) Nature , vol.428 , pp. 437-441
    • Sourjik, V.1    Berg, H.C.2
  • 40
    • 77958500295 scopus 로고    scopus 로고
    • Differences in signalling by directly and indirectly binding ligands in bacterial chemotaxis
    • Neumann, S., Hansen, C. H., Wingreen, N. S., and Sourjik, V. (2010) Differences in signalling by directly and indirectly binding ligands in bacterial chemotaxis EMBO J. 29, 3484-3495 10.1038/emboj.2010.224
    • (2010) EMBO J. , vol.29 , pp. 3484-3495
    • Neumann, S.1    Hansen, C.H.2    Wingreen, N.S.3    Sourjik, V.4
  • 42
    • 77954933118 scopus 로고    scopus 로고
    • Identification of a chemoreceptor for tricarboxylic acid cycle intermediates: Differential chemotactic response towards receptor ligands
    • Lacal, J., Alfonso, C., Liu, X., Parales, R. E., Morel, B., Conejero-Lara, F., Rivas, G., Duque, E., Ramos, J. L., and Krell, T. (2010) Identification of a chemoreceptor for tricarboxylic acid cycle intermediates: differential chemotactic response towards receptor ligands J. Biol. Chem. 285, 23126-23136 10.1074/jbc.M110.110403
    • (2010) J. Biol. Chem. , vol.285 , pp. 23126-23136
    • Lacal, J.1    Alfonso, C.2    Liu, X.3    Parales, R.E.4    Morel, B.5    Conejero-Lara, F.6    Rivas, G.7    Duque, E.8    Ramos, J.L.9    Krell, T.10
  • 43
    • 0037076332 scopus 로고    scopus 로고
    • Collaborative signaling by mixed chemoreceptor teams in Escherichia coli
    • Ames, P., Studdert, C. A., Reiser, R. H., and Parkinson, J. S. (2002) Collaborative signaling by mixed chemoreceptor teams in Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 99, 7060-7065 10.1073/pnas.092071899
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 7060-7065
    • Ames, P.1    Studdert, C.A.2    Reiser, R.H.3    Parkinson, J.S.4
  • 44
    • 84864096708 scopus 로고    scopus 로고
    • The structure of the NasR transcription antiterminator reveals a one-component system with a NIT nitrate receptor coupled to an ANTAR RNA-binding effector
    • Boudes, M., Lazar, N., Graille, M., Durand, D., Gaidenko, T. A., Stewart, V., and van Tilbeurgh, H. (2012) The structure of the NasR transcription antiterminator reveals a one-component system with a NIT nitrate receptor coupled to an ANTAR RNA-binding effector Mol. Microbiol. 85, 431-444 10.1111/j.1365-2958.2012.08111.x
    • (2012) Mol. Microbiol. , vol.85 , pp. 431-444
    • Boudes, M.1    Lazar, N.2    Graille, M.3    Durand, D.4    Gaidenko, T.A.5    Stewart, V.6    Van Tilbeurgh, H.7
  • 45
    • 84946060416 scopus 로고    scopus 로고
    • SMART: Recent updates, new developments and status in 2015
    • Letunic, I., Doerks, T., and Bork, P. (2015) SMART: recent updates, new developments and status in 2015 Nucleic Acids Res. 43, D257-260 10.1093/nar/gku949
    • (2015) Nucleic Acids Res. , vol.43 , pp. D257-260
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 46
    • 46649120154 scopus 로고    scopus 로고
    • Crystal structure of a functional dimer of the PhoQ sensor domain
    • Cheung, J., Bingman, C. A., Reyngold, M., Hendrickson, W. A., and Waldburger, C. D. (2008) Crystal structure of a functional dimer of the PhoQ sensor domain J. Biol. Chem. 283, 13762-13770 10.1074/jbc.M710592200
    • (2008) J. Biol. Chem. , vol.283 , pp. 13762-13770
    • Cheung, J.1    Bingman, C.A.2    Reyngold, M.3    Hendrickson, W.A.4    Waldburger, C.D.5
  • 47
    • 57649219430 scopus 로고    scopus 로고
    • Crystal structures of C4-dicarboxylate ligand complexes with sensor domains of histidine kinases DcuS and DctB
    • Cheung, J. and Hendrickson, W. A. (2008) Crystal structures of C4-dicarboxylate ligand complexes with sensor domains of histidine kinases DcuS and DctB J. Biol. Chem. 283, 30256-30265 10.1074/jbc.M805253200
    • (2008) J. Biol. Chem. , vol.283 , pp. 30256-30265
    • Cheung, J.1    Hendrickson, W.A.2
  • 49
    • 0036121376 scopus 로고    scopus 로고
    • The sensor kinase CitA (DpiB) of Escherichia coli functions as a high-affinity citrate receptor
    • Kaspar, S. and Bott, M. (2002) The sensor kinase CitA (DpiB) of Escherichia coli functions as a high-affinity citrate receptor Arch. Microbiol. 177, 313-321 10.1007/s00203-001-0393-z
    • (2002) Arch. Microbiol. , vol.177 , pp. 313-321
    • Kaspar, S.1    Bott, M.2
  • 50
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., Bryson, K., and Jones, D. T. (2000) The PSIPRED protein structure prediction server Bioinformatics 16, 404-405 10.1093/bioinformatics/16.4.404
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 51
    • 33646544356 scopus 로고    scopus 로고
    • Signaling interactions between the aerotaxis transducer Aer and heterologous chemoreceptors in Escherichia coli
    • Gosink, K. K., Buron-Barral, M. C., and Parkinson, J. S. (2006) Signaling interactions between the aerotaxis transducer Aer and heterologous chemoreceptors in Escherichia coli J. Bacteriol. 188, 3487-3493 10.1128/JB.188.10.3487-3493.2006
    • (2006) J. Bacteriol. , vol.188 , pp. 3487-3493
    • Gosink, K.K.1    Buron-Barral, M.C.2    Parkinson, J.S.3
  • 52
    • 77954384425 scopus 로고    scopus 로고
    • Structural characterization of the predominant family of histidine kinase sensor domains
    • Zhang, Z. and Hendrickson, W. A. (2010) Structural characterization of the predominant family of histidine kinase sensor domains J. Mol. Biol. 400, 335-353 10.1016/j.jmb.2010.04.049
    • (2010) J. Mol. Biol. , vol.400 , pp. 335-353
    • Zhang, Z.1    Hendrickson, W.A.2
  • 53
    • 84869232446 scopus 로고    scopus 로고
    • The Bacillus subtilis chemoreceptor McpC senses multiple ligands using two discrete mechanisms
    • Glekas, G. D., Mulhern, B. J., Kroc, A., Duelfer, K. A., Lei, V., Rao, C. V., and Ordal, G. W. (2012) The Bacillus subtilis chemoreceptor McpC senses multiple ligands using two discrete mechanisms J. Biol. Chem. 287, 39412-39418 10.1074/jbc.M112.413518
    • (2012) J. Biol. Chem. , vol.287 , pp. 39412-39418
    • Glekas, G.D.1    Mulhern, B.J.2    Kroc, A.3    Duelfer, K.A.4    Lei, V.5    Rao, C.V.6    Ordal, G.W.7
  • 54
    • 84863238091 scopus 로고    scopus 로고
    • A parallel diffusion-based microfluidic device for bacterial chemotaxis analysis
    • Si, G., Yang, W., Bi, S., Luo, C., and Ouyang, Q. (2012) A parallel diffusion-based microfluidic device for bacterial chemotaxis analysis Lab Chip 12, 1389-1394 10.1039/c2lc21219f
    • (2012) Lab Chip , vol.12 , pp. 1389-1394
    • Si, G.1    Yang, W.2    Bi, S.3    Luo, C.4    Ouyang, Q.5
  • 55
    • 80053291460 scopus 로고    scopus 로고
    • Ligand-binding PAS domains in a genomic, cellular, and structural context
    • Henry, J. T. and Crosson, S. (2011) Ligand-binding PAS domains in a genomic, cellular, and structural context Annu. Rev. Microbiol. 65, 261-286 10.1146/annurev-micro-121809-151631
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 261-286
    • Henry, J.T.1    Crosson, S.2
  • 57
    • 84929275058 scopus 로고    scopus 로고
    • A high-throughput screen for ligand binding reveals the specificities of three amino acid chemoreceptors from Pseudomonas syringae pv. Actinidiae
    • McKellar, J. L., Minnell, J. J., and Gerth, M. L. (2015) A high-throughput screen for ligand binding reveals the specificities of three amino acid chemoreceptors from Pseudomonas syringae pv. actinidiae Mol. Microbiol. 96, 694-707 10.1111/mmi.12964
    • (2015) Mol. Microbiol. , vol.96 , pp. 694-707
    • McKellar, J.L.1    Minnell, J.J.2    Gerth, M.L.3
  • 58
    • 84929283398 scopus 로고    scopus 로고
    • Tackling the bottleneck in bacterial signal transduction research: High-throughput identification of signal molecules
    • Krell, T. (2015) Tackling the bottleneck in bacterial signal transduction research: high-throughput identification of signal molecules Mol. Microbiol. 96, 685-688 10.1111/mmi.12975
    • (2015) Mol. Microbiol. , vol.96 , pp. 685-688
    • Krell, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.