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Volumn 185, Issue 16, 2003, Pages 4872-4882

Probing conservation of HAMP linker structure and signal transduction mechanism through analysis of hybrid sensor kinases

Author keywords

[No Author keywords available]

Indexed keywords

CHEMOTACTIC FACTOR; HYBRID PROTEIN; LIGAND; LINK PROTEIN; METHYL GROUP; NARQ PROTEIN; NARX PROTEIN; NITRATE; NITRITE; PHOSPHOTRANSFERASE; PROTEIN HAMP; UNCLASSIFIED DRUG;

EID: 0042561788     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.16.4872-4882.2003     Document Type: Article
Times cited : (69)

References (54)
  • 1
    • 0024276608 scopus 로고
    • Transmembrane signaling by bacterial chemoreceptors: E. coli transducers with locked signal output
    • Ames, P., and J. S. Parkinson. 1988. Transmembrane signaling by bacterial chemoreceptors: E. coli transducers with locked signal output. Cell 55:817-826.
    • (1988) Cell , vol.55 , pp. 817-826
    • Ames, P.1    Parkinson, J.S.2
  • 2
    • 0035091399 scopus 로고    scopus 로고
    • Rapid dephosphorylation of the TorR response regulator by the TorS unorthodox sensor in Escherichia coli
    • Ansaldi, M., C. Jourlin-Castelli, M. Lepelletier, L. Theraulaz, and V. Mejean. 2001. Rapid dephosphorylation of the TorR response regulator by the TorS unorthodox sensor in Escherichia coli. J. Bacteriol. 183:2691-2695.
    • (2001) J. Bacteriol. , vol.183 , pp. 2691-2695
    • Ansaldi, M.1    Jourlin-Castelli, C.2    Lepelletier, M.3    Theraulaz, L.4    Mejean, V.5
  • 3
    • 0037216619 scopus 로고    scopus 로고
    • Mutational analysis of a conserved signal-transducing element: The HAMP linker of the Escherichia coli nitrate sensor NarX
    • Appleman, J. A., and V. Stewart. 2003. Mutational analysis of a conserved signal-transducing element: the HAMP linker of the Escherichia coli nitrate sensor NarX. J. Bacteriol. 185:89-97.
    • (2003) J. Bacteriol. , vol.185 , pp. 89-97
    • Appleman, J.A.1    Stewart, V.2
  • 4
    • 0032766134 scopus 로고    scopus 로고
    • The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signaling proteins
    • Aravind, L., and C. P. Ponting. 1999. The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signaling proteins. FEMS Microbiol. Lett. 176:111-116.
    • (1999) FEMS Microbiol. Lett. , vol.176 , pp. 111-116
    • Aravind, L.1    Ponting, C.P.2
  • 5
    • 0028115617 scopus 로고
    • Transmembrane signaling by a hybrid protein: Communication from the domain of chemoreceptor Trg that recognizes sugar-binding proteins to the kinase/phosphatase domain of osmosensor EnvZ
    • Baumgartner, J. W., C. Kim, R. E. Brissette, M. Inouye, C. Park, and G. L. Hazelbauer. 1994. Transmembrane signaling by a hybrid protein: communication from the domain of chemoreceptor Trg that recognizes sugar-binding proteins to the kinase/phosphatase domain of osmosensor EnvZ. J. Bacteriol. 176:1157-1163.
    • (1994) J. Bacteriol. , vol.176 , pp. 1157-1163
    • Baumgartner, J.W.1    Kim, C.2    Brissette, R.E.3    Inouye, M.4    Park, C.5    Hazelbauer, G.L.6
  • 6
    • 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., L. A. Barnes, Y. Gitin, and J. S. Parkinson. 2000. 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) 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
  • 7
    • 0024789654 scopus 로고
    • Superpolylinkers in cloning and expression vectors
    • Brosius, J. 1989. Superpolylinkers in cloning and expression vectors. DNA 8:759-777.
    • (1989) DNA , vol.8 , pp. 759-777
    • Brosius, J.1
  • 8
    • 0032575326 scopus 로고    scopus 로고
    • Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor
    • Butler, S. L., and J. J. Falke. 1998. Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor. Biochemistry (Moscow) 37:10746-10756.
    • (1998) Biochemistry (Moscow) , vol.37 , pp. 10746-10756
    • Butler, S.L.1    Falke, J.J.2
  • 9
    • 0017129243 scopus 로고
    • Transposition and fusion of lac genes to selected promoters in Escherichia coli using bacteriophages lambda and mu
    • Casadaban, M. J. 1976. Transposition and fusion of lac genes to selected promoters in Escherichia coli using bacteriophages lambda and mu. J. Mol. Biol. 104:541-555.
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 10
    • 0026747875 scopus 로고
    • Mutational analysis reveals functional similarity between NarX, a nitrate sensor in Escherichia coli K-12, and the methyl-accepting chemotaxis proteins
    • Collins, L. A., S. M. Egan, and V. Stewart. 1992. Mutational analysis reveals functional similarity between NarX, a nitrate sensor in Escherichia coli K-12, and the methyl-accepting chemotaxis proteins. J. Bacteriol. 174:3667-3675.
    • (1992) J. Bacteriol. , vol.174 , pp. 3667-3675
    • Collins, L.A.1    Egan, S.M.2    Stewart, V.3
  • 11
    • 0031905590 scopus 로고    scopus 로고
    • CpxP, a stress-combative member of the Cpx regulon
    • Danese, P. N., and T. Silhavy. 1998. CpxP, a stress-combative member of the Cpx regulon. J. Bacteriol. 180:831-839.
    • (1998) J. Bacteriol. , vol.180 , pp. 831-839
    • Danese, P.N.1    Silhavy, T.2
  • 12
    • 0029990165 scopus 로고    scopus 로고
    • Analysis of nitrate regulatory protein NarL-binding sites in the fdnG and narG operon control regions of Escherichia coli K-12
    • Darwin, A. J., J. Li, and V. Stewart. 1996. Analysis of nitrate regulatory protein NarL-binding sites in the fdnG and narG operon control regions of Escherichia coli K-12. Mol. Microbiol. 20:621-632.
    • (1996) Mol. Microbiol. , vol.20 , pp. 621-632
    • Darwin, A.J.1    Li, J.2    Stewart, V.3
  • 13
    • 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
  • 14
    • 0033931244 scopus 로고    scopus 로고
    • Structure of a conserved receptor domain that regulates kinase activity: The cytoplasmic domain of bacterial taxis receptors
    • Falke, J. J., and S.-H. Kim. 2000. Structure of a conserved receptor domain that regulates kinase activity: the cytoplasmic domain of bacterial taxis receptors. Curr. Opin. Struct. Biol. 10:462-469.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 462-469
    • Falke, J.J.1    Kim, S.-H.2
  • 15
    • 0023272340 scopus 로고
    • Interposon mutagenesis of soil and water bacteria: A family of DNA fragments designed for in vitro insertional mutagenesis of gram-negative bacteria
    • Fellay, R., J. Frey, and H. Krisch. 1987. Interposon mutagenesis of soil and water bacteria: a family of DNA fragments designed for in vitro insertional mutagenesis of gram-negative bacteria. Gene 52:147-154.
    • (1987) Gene , vol.52 , pp. 147-154
    • Fellay, R.1    Frey, J.2    Krisch, H.3
  • 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. Baumgartner, and G. 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.2    Hazelbauer, G.3
  • 17
    • 0033277340 scopus 로고    scopus 로고
    • The histidine protein kinase superfamily
    • Grebe, T. W., and J. B. Stock. 1999. The histidine protein kinase superfamily. Adv. Microb. Physiol. 41:139-227.
    • (1999) Adv. Microb. Physiol. , vol.41 , pp. 139-227
    • Grebe, T.W.1    Stock, J.B.2
  • 18
    • 0029910516 scopus 로고    scopus 로고
    • Transcriptional regulation of Salmonella virulence: A PhoQ periplasmic domain mutation results in increased net phosphotransfer to PhoP
    • Gunn, J. S., E. L. Hohmann, and S. I. Miller. 1996. Transcriptional regulation of Salmonella virulence: a PhoQ periplasmic domain mutation results in increased net phosphotransfer to PhoP. J. Bacteriol. 178:6369-6373.
    • (1996) J. Bacteriol. , vol.178 , pp. 6369-6373
    • Gunn, J.S.1    Hohmann, E.L.2    Miller, S.I.3
  • 19
    • 0019158049 scopus 로고
    • Genetic and biochemical properties of Escherichia coli mutants with defects in serine chemotaxis
    • Hedblom, M., and J. Adler. 1980. Genetic and biochemical properties of Escherichia coli mutants with defects in serine chemotaxis. J. Bacteriol. 144:1048-1060.
    • (1980) J. Bacteriol. , vol.144 , pp. 1048-1060
    • Hedblom, M.1    Adler, J.2
  • 20
    • 0027214685 scopus 로고
    • Interplay between the membrane-associated UhpB and UhpC regulatory proteins
    • Island, M. D., and R. J. Kadner. 1993. Interplay between the membrane-associated UhpB and UhpC regulatory proteins. J. Bacteriol. 175:5028-5034.
    • (1993) J. Bacteriol. , vol.175 , pp. 5028-5034
    • Island, M.D.1    Kadner, R.J.2
  • 21
    • 0027202361 scopus 로고
    • Ligand binding to the receptor domain regulates the ratio of kinase to phosphatase activities of the signaling domain of the hybrid Escherichia coli transmembrane receptor, Taz1
    • Jin, T., and M. Inouye. 1993. Ligand binding to the receptor domain regulates the ratio of kinase to phosphatase activities of the signaling domain of the hybrid Escherichia coli transmembrane receptor, Taz1. J. Mol. Biol. 232:484-492.
    • (1993) J. Mol. Biol. , vol.232 , pp. 484-492
    • Jin, T.1    Inouye, M.2
  • 22
    • 0025606276 scopus 로고
    • Nitrate-independent and molybdenum-independent signal transduction mutations in narX that alter regulation of anaerobic respiratory genes in Escherichia coli
    • Kalman, L. V., and R. P. Gunsalus. 1990. Nitrate-independent and molybdenum-independent signal transduction mutations in narX that alter regulation of anaerobic respiratory genes in Escherichia coli. J. Bacteriol. 172:7049-7056.
    • (1990) J. Bacteriol. , vol.172 , pp. 7049-7056
    • Kalman, L.V.1    Gunsalus, R.P.2
  • 23
    • 0032781275 scopus 로고    scopus 로고
    • The periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor
    • Kaspar, S., R. Perozzo, S. Reinelt, M. Meyer, K. Pfister, L. Scapozza, and M. Bott. 1999. The periplasmic domain of the histidine autokinase CitA functions as a highly specific citrate receptor. Mol. Microbiol. 33:858-872.
    • (1999) Mol. Microbiol. , vol.33 , pp. 858-872
    • Kaspar, S.1    Perozzo, R.2    Reinelt, S.3    Meyer, M.4    Pfister, K.5    Scapozza, L.6    Bott, M.7
  • 25
    • 0037340214 scopus 로고    scopus 로고
    • The conserved cytoplasmic module of the transmembrane chemoreceptor McpC mediates carbohydrate chemotaxis in Bacillus subtilis
    • Kristich, C. J., G. D. Glekas, and G. W. Ordal. 2003. The conserved cytoplasmic module of the transmembrane chemoreceptor McpC mediates carbohydrate chemotaxis in Bacillus subtilis. Mol. Microbiol. 47:1353-1366.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1353-1366
    • Kristich, C.J.1    Glekas, G.D.2    Ordal, G.W.3
  • 26
    • 0022921901 scopus 로고
    • Mutations in a new chromosomal gene of Escherichia coli K-12, pcnB, reduce plasmid copy number of pBR322 and its derivatives
    • Lopilato, J., S. Bortner, and J. Beckwith. 1986. Mutations in a new chromosomal gene of Escherichia coli K-12, pcnB, reduce plasmid copy number of pBR322 and its derivatives. Mol. Gen. Genet. 205:285-290.
    • (1986) Mol. Gen. Genet. , vol.205 , pp. 285-290
    • Lopilato, J.1    Bortner, S.2    Beckwith, J.3
  • 28
    • 0037965621 scopus 로고    scopus 로고
    • A sensitive, versatile microfluidic assay for bacterial chemotaxis
    • Mao, H., P. S. Cremer, and M. D. Manson. 2003. A sensitive, versatile microfluidic assay for bacterial chemotaxis. Proc. Natl. Acad. Sci. USA 100:5449-5454.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5449-5454
    • Mao, H.1    Cremer, P.S.2    Manson, M.D.3
  • 29
    • 0021359871 scopus 로고
    • Novel high-level expression cloning vehicles: 104-Fold amplifications of Escherichia coli minor protein
    • Masui, Y., T. Mizumo, and M. Inouye. 1984. Novel high-level expression cloning vehicles: 104-fold amplifications of Escherichia coli minor protein. Bio/Technology 2:81-85.
    • (1984) Bio/Technology , vol.2 , pp. 81-85
    • Masui, Y.1    Mizumo, T.2    Inouye, M.3
  • 30
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 31
    • 0033543590 scopus 로고    scopus 로고
    • A piston model for transmembrane signaling of the aspartate receptor
    • Ottemann, K. M., W. Xiao, Y.-K. Shin, and D. E. Koshland, Jr. 1999. A piston model for transmembrane signaling of the aspartate receptor. Science 285:1751-1754.
    • (1999) Science , vol.285 , pp. 1751-1754
    • Ottemann, K.M.1    Xiao, W.2    Shin, Y.-K.3    Koshland D.E., Jr.4
  • 32
    • 0030811371 scopus 로고    scopus 로고
    • Mutational analysis of the linker region of EnvZ, an osmosensor in Escherichia coli
    • Park, H., and M. Inouye. 1997. Mutational analysis of the linker region of EnvZ, an osmosensor in Escherichia coli. J. Bacteriol. 179:4382-4390.
    • (1997) J. Bacteriol. , vol.179 , pp. 4382-4390
    • Park, H.1    Inouye, M.2
  • 33
    • 0036129397 scopus 로고    scopus 로고
    • Modeling the transmembrane domain of bacterial chemoreceptors
    • Peach, M. L., G. Hazelbauer, and T. P. Lybrand. 2002. Modeling the transmembrane domain of bacterial chemoreceptors. Protein Sci. 11:912-923.
    • (2002) Protein Sci. , vol.11 , pp. 912-923
    • Peach, M.L.1    Hazelbauer, G.2    Lybrand, T.P.3
  • 34
    • 0027251261 scopus 로고
    • Dual response regulators (NarL and NarP) interact with dual sensors (NarX and NarQ) to control nitrate- and nitrite-regulated gene expression in Escherichia coli K-12
    • Rabin, R., and V. Stewart. 1993. Dual response regulators (NarL and NarP) interact with dual sensors (NarX and NarQ) to control nitrate- and nitrite-regulated gene expression in Escherichia coli K-12. J. Bacteriol. 175:3259-3268.
    • (1993) J. Bacteriol. , vol.175 , pp. 3259-3268
    • Rabin, R.1    Stewart, V.2
  • 35
    • 0041293635 scopus 로고
    • Either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12
    • Rabin, R., and V. Stewart. 1993. Either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12. Proc. Natl. Acad. Sci. USA 88:6941-6945.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6941-6945
    • Rabin, R.1    Stewart, V.2
  • 36
    • 0025355396 scopus 로고
    • The Cpx proteins of Escherichia coli K-12: Evidence that cpxA, ecfB, ssd, and eup mutations all identify the same gene
    • Rainwater, S., and P. M. Silverman. 1990. The Cpx proteins of Escherichia coli K-12: evidence that cpxA, ecfB, ssd, and eup mutations all identify the same gene. J. Bacteriol. 172:2456-2461.
    • (1990) J. Bacteriol. , vol.172 , pp. 2456-2461
    • Rainwater, S.1    Silverman, P.M.2
  • 37
    • 0033812832 scopus 로고    scopus 로고
    • Tethering of CpxP to the inner membrane prevents spheroplast induction of the Cpx envelope stress response
    • Raivio, T. L., M. W. Laird, J. C. Joly, and T. J. Silhavy. 2000. Tethering of CpxP to the inner membrane prevents spheroplast induction of the Cpx envelope stress response. Mol. Microbiol. 37:1186-1197.
    • (2000) Mol. Microbiol. , vol.37 , pp. 1186-1197
    • Raivio, T.L.1    Laird, M.W.2    Joly, J.C.3    Silhavy, T.J.4
  • 38
    • 0032851357 scopus 로고    scopus 로고
    • The Cpx envelope stress response is controlled by amplification and feedback inhibition
    • Raivio, T. L., D. L. Popkin, and T. J. Silhavy. 1999. The Cpx envelope stress response is controlled by amplification and feedback inhibition. J. Bacteriol. 181:5263-5272.
    • (1999) J. Bacteriol. , vol.181 , pp. 5263-5272
    • Raivio, T.L.1    Popkin, D.L.2    Silhavy, T.J.3
  • 39
    • 0033106492 scopus 로고    scopus 로고
    • e and Cpx regulatory pathways: Overlappíng but distinct envelope stress responses
    • e and Cpx regulatory pathways: overlappíng but distinct envelope stress responses. Curr. Opin. Microbiol. 2:159-165.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 159-165
    • Raivio, T.L.1    Silhavy, T.J.2
  • 40
    • 0034029031 scopus 로고    scopus 로고
    • Pas domain residues involved in signal transduction by the Aer redox sensor of Escherichia coli
    • Repik, A., A. Rebbapragada, M. S. Johnson, J. O. Haznedar, I. B. Zhulin, and B. L. Taylor. 2000. Pas domain residues involved in signal transduction by the Aer redox sensor of Escherichia coli. Mol. Microbiol. 36:806-816.
    • (2000) Mol. Microbiol. , vol.36 , pp. 806-816
    • Repik, A.1    Rebbapragada, A.2    Johnson, M.S.3    Haznedar, J.O.4    Zhulin, I.B.5    Taylor, B.L.6
  • 41
    • 0032539854 scopus 로고    scopus 로고
    • Computational learning reveals coiled coil-like motifs in histidine kinase linker domains
    • Singh, M., B. Berger, P. S. Kim, J. M. Berger, and A. G. Cochran. 1998. Computational learning reveals coiled coil-like motifs in histidine kinase linker domains. Proc. Natl. Acad. Sci. USA 95:2738-2743.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2738-2743
    • Singh, M.1    Berger, B.2    Kim, P.S.3    Berger, J.M.4    Cochran, A.G.5
  • 42
    • 0036274158 scopus 로고    scopus 로고
    • Quorum sensing Escherichia coli regulators B and C (QseBC): A novel two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli
    • Sperandio, V., A. G. Torres, and J. B. Kaper. 2002. Quorum sensing Escherichia coli regulators B and C (QseBC): a novel two-component regulatory system involved in the regulation of flagella and motility by quorum sensing in E. coli. Mol. Microbiol. 43:809-821.
    • (2002) Mol. Microbiol. , vol.43 , pp. 809-821
    • Sperandio, V.1    Torres, A.G.2    Kaper, J.B.3
  • 43
    • 0022719327 scopus 로고
    • pHG165: A pBR322 copy number derivative of pUC8 for cloning and expression
    • Stewart, G. S. A. B., S. Lubinsky-Mink, C. G. Jackson, A. Kassel, and J. Kuhn. 1986. pHG165: a pBR322 copy number derivative of pUC8 for cloning and expression. Plasmid 15:172-181.
    • (1986) Plasmid , vol.15 , pp. 172-181
    • Stewart, G.S.A.B.1    Lubinsky-Mink, S.2    Jackson, C.G.3    Kassel, A.4    Kuhn, J.5
  • 44
    • 0037326468 scopus 로고    scopus 로고
    • Nitrate- and nitrite-responsive sensors NarX and NarQ of proteobacteria
    • Stewart, V. 2003. Nitrate- and nitrite-responsive sensors NarX and NarQ of proteobacteria. Biochem. Soc. Trans. 33:1-10.
    • (2003) Biochem. Soc. Trans. , vol.33 , pp. 1-10
    • Stewart, V.1
  • 45
    • 0020377789 scopus 로고
    • Requirement of FNR and NarL functions for nitrate reductase expression in Escherichia coli K-12
    • Stewart, V. 1982. Requirement of FNR and NarL functions for nitrate reductase expression in Escherichia coli K-12. J. Bacteriol. 151:1320-1325.
    • (1982) J. Bacteriol. , vol.151 , pp. 1320-1325
    • Stewart, V.1
  • 46
    • 0023991777 scopus 로고
    • Identification and expression of genes narL and narX of the nar (nitrate reductase) locus in Escherichia coli
    • Stewart, V., and J. J. Parales. 1988. Identification and expression of genes narL and narX of the nar (nitrate reductase) locus in Escherichia coli. J. Bacteriol. 170:1589-1597.
    • (1988) J. Bacteriol. , vol.170 , pp. 1589-1597
    • Stewart, V.1    Parales, J.J.2
  • 47
    • 0001943573 scopus 로고
    • Dual sensors and dual response regulators interact to control nitrate- and nitrite-responsive gene expression in Escherichia coli
    • J. A. Hoch and T. J. Silhavy (ed.). American Society for Microbiology, Washington, D.C.
    • Stewart, V., and R. S. Rabin. 1995. Dual sensors and dual response regulators interact to control nitrate- and nitrite-responsive gene expression in Escherichia coli, p. 233-252. In J. A. Hoch and T. J. Silhavy (ed.), Two-component signal transduction. American Society for Microbiology, Washington, D.C.
    • (1995) Two-Component Signal Transduction , pp. 233-252
    • Stewart, V.1    Rabin, R.S.2
  • 49
    • 0024462539 scopus 로고
    • Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate
    • Utsumi, R., R. E. Brissette, A. Rampersaud, S. A. Forst, K. Oosawa, and M. Inouye. 1989. Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate. Science 245:1246-1249.
    • (1989) Science , vol.245 , pp. 1246-1249
    • Utsumi, R.1    Brissette, R.E.2    Rampersaud, A.3    Forst, S.A.4    Oosawa, K.5    Inouye, M.6
  • 50
    • 0036091152 scopus 로고    scopus 로고
    • A NarX-Tar chimera mediates repellent chemotaxis to nitrate and nitrite
    • Ward, S. M., A. Delgado, R. P. Gunsalus, and M. D. Manson. 2002. A NarX-Tar chimera mediates repellent chemotaxis to nitrate and nitrite. Mol. Microbiol. 44:709-719.
    • (2002) Mol. Microbiol. , vol.44 , pp. 709-719
    • Ward, S.M.1    Delgado, A.2    Gunsalus, R.P.3    Manson, M.D.4
  • 51
    • 0031931506 scopus 로고    scopus 로고
    • Chimeric chemoreceptors in Escherichia coli: Signaling properties of Tar-Tap and Tap-Tar hybrids
    • Weerasuriya, S., B. M. Schneider, and M. D. Manson. 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
  • 52
    • 0030694514 scopus 로고    scopus 로고
    • Discrimination between structurally related ligands nitrate and nitrite controls autokinase activity of the NarX transmembrane signal transducer of Escherichia coli
    • Williams, S. B., and V. Stewart. 1997. Discrimination between structurally related ligands nitrate and nitrite controls autokinase activity of the NarX transmembrane signal transducer of Escherichia coli. Mol. Microbiol. 26:911-925.
    • (1997) Mol. Microbiol. , vol.26 , pp. 911-925
    • Williams, S.B.1    Stewart, V.2
  • 53
    • 0032826834 scopus 로고    scopus 로고
    • Functional similarities among two-component sensors and methyl-accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmembrane signal transduction
    • Williams, S. B., and V. Stewart. 1999. Functional similarities among two-component sensors and methyl-accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmembrane signal transduction. Mol. Microbiol. 33:1093-1102.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1093-1102
    • Williams, S.B.1    Stewart, V.2
  • 54
    • 0031037309 scopus 로고    scopus 로고
    • Nitrate- and nitrite-sensing protein NarX of Escherichia coli K-12: Mutational analysis of the amino-terminal tail and first transmembrane segment
    • Williams, S. B., and V. Stewart. 1997. Nitrate- and nitrite-sensing protein NarX of Escherichia coli K-12: mutational analysis of the amino-terminal tail and first transmembrane segment. J. Bacteriol. 179:721-729.
    • (1997) J. Bacteriol. , vol.179 , pp. 721-729
    • Williams, S.B.1    Stewart, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.