메뉴 건너뛰기




Volumn 75, Issue 2, 2010, Pages 394-412

Asymmetric cross-regulation between the nitrate-responsive NarX-NarL and NarQ-NarP two-component regulatory systems from Escherichia coli K-12

Author keywords

[No Author keywords available]

Indexed keywords

NITRATE; NITRITE; PROTEIN NARL; PROTEIN NARP; PROTEIN NARQ; PROTEIN NARX; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 74349106185     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06987.x     Document Type: Article
Times cited : (91)

References (70)
  • 2
    • 0037383238 scopus 로고    scopus 로고
    • Comparative analysis of prototype two-component systems with either bifunctional or monofunctional sensors: Differences in molecular structure and physiological function
    • Alves, R. Savageau, M.A. (2003) Comparative analysis of prototype two-component systems with either bifunctional or monofunctional sensors: differences in molecular structure and physiological function. Mol Microbiol 48 : 25 51.
    • (2003) Mol Microbiol , vol.48 , pp. 25-51
    • Alves, R.1    Savageau, M.A.2
  • 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. Stewart, V. (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
    • 0026647630 scopus 로고
    • Characterization of Escherichia coli glnL mutations affecting nitrogen regulation
    • Atkinson, M.R. Ninfa, A.J. (1992) Characterization of Escherichia coli glnL mutations affecting nitrogen regulation. J Bacteriol 174 : 4538 4548.
    • (1992) J Bacteriol , vol.174 , pp. 4538-4548
    • Atkinson, M.R.1    Ninfa, A.J.2
  • 5
    • 0037025378 scopus 로고    scopus 로고
    • EnvZ-OmpR interaction and osmoregulation in Escherichia coli
    • Cai, S.J. Inouye, M. (2002) EnvZ-OmpR interaction and osmoregulation in Escherichia coli. J Biol Chem 277 : 24155 24161.
    • (2002) J Biol Chem , vol.277 , pp. 24155-24161
    • Cai, S.J.1    Inouye, M.2
  • 6
    • 70349795241 scopus 로고    scopus 로고
    • Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction
    • Casino, P., Rubio, V. Marina, A. (2009) Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction. Cell 139 : 325 336.
    • (2009) Cell , vol.139 , pp. 325-336
    • Casino, P.1    Rubio, V.2    Marina, A.3
  • 7
    • 0029042437 scopus 로고
    • The NarX and NarQ sensor-transmitter proteins of Escherichia coli each require two conserved histidines for nitrate-dependent signal transduction to NarL
    • Cavicchioli, R., Schröder, I., Constanti, M. Gunsalus, R.P. (1995) The NarX and NarQ sensor-transmitter proteins of Escherichia coli each require two conserved histidines for nitrate-dependent signal transduction to NarL. J Bacteriol 177 : 2416 2424.
    • (1995) J Bacteriol , vol.177 , pp. 2416-2424
    • Cavicchioli, R.1    Schröder, I.2    Constanti, M.3    Gunsalus, R.P.4
  • 8
    • 0026740927 scopus 로고
    • Identification and characterization of narQ, a second nitrate sensor for nitrate-dependent gene regulation in Escherichia coli
    • Chiang, R.C., Cavicchioli, R. Gunsalus, R.P. (1992) Identification and characterization of narQ, a second nitrate sensor for nitrate-dependent gene regulation in Escherichia coli. Mol Microbiol 6 : 1913 1923.
    • (1992) Mol Microbiol , vol.6 , pp. 1913-1923
    • Chiang, R.C.1    Cavicchioli, R.2    Gunsalus, R.P.3
  • 9
    • 0029030757 scopus 로고
    • Expression of the narX, narL, narP, and narQ genes of Escherichia coli K-12: Regulation of the regulators
    • Darwin, A.J. Stewart, V. (1995a) Expression of the narX, narL, narP, and narQ genes of Escherichia coli K-12: regulation of the regulators. J Bacteriol 177 : 3865 3869.
    • (1995) J Bacteriol , vol.177 , pp. 3865-3869
    • Darwin, A.J.1    Stewart, V.2
  • 10
    • 0029086289 scopus 로고
    • Nitrate and nitrite regulation of the Fnr-dependent aeg-46.5 promoter of Escherichia coli K-12 is mediated by competition between homologous response regulators (NarL and NarP) for a common DNA-binding site
    • Darwin, A.J. Stewart, V. (1995b) Nitrate and nitrite regulation of the Fnr-dependent aeg-46.5 promoter of Escherichia coli K-12 is mediated by competition between homologous response regulators (NarL and NarP) for a common DNA-binding site. J Mol Biol 251 : 15 29.
    • (1995) J Mol Biol , vol.251 , pp. 15-29
    • Darwin, A.J.1    Stewart, V.2
  • 11
    • 0032730205 scopus 로고    scopus 로고
    • Histidine kinases: Diversity of domain organization
    • Dutta, R., Qin, L. Inouye, M. (1999) Histidine kinases: diversity of domain organization. Mol Microbiol 34 : 633 640.
    • (1999) Mol Microbiol , vol.34 , pp. 633-640
    • Dutta, R.1    Qin, L.2    Inouye, M.3
  • 12
    • 0025108798 scopus 로고
    • Nitrate regulation of anaerobic respiratory gene expression in narX deletion mutants of Escherichia coli K-12
    • Egan, S.M. Stewart, V. (1990) Nitrate regulation of anaerobic respiratory gene expression in narX deletion mutants of Escherichia coli K-12. J Bacteriol 172 : 5020 5029.
    • (1990) J Bacteriol , vol.172 , pp. 5020-5029
    • Egan, S.M.1    Stewart, V.2
  • 13
    • 0025799544 scopus 로고
    • Mutational analysis of nitrate regulatory gene narL in Escherichia coli K-12
    • Egan, S.M. Stewart, V. (1991) Mutational analysis of nitrate regulatory gene narL in Escherichia coli K-12. J Bacteriol 173 : 4424 4432.
    • (1991) J Bacteriol , vol.173 , pp. 4424-4432
    • Egan, S.M.1    Stewart, V.2
  • 15
    • 0029960165 scopus 로고    scopus 로고
    • Kinetic comparison of the specificity of the vancomycin resistance VanS for two response regulators, VanR and PhoB
    • Fisher, S.L., Kim, S.K., Wanner, B.L. Walsh, C.T. (1996) Kinetic comparison of the specificity of the vancomycin resistance VanS for two response regulators, VanR and PhoB. Biochemistry 35 : 4732 4740.
    • (1996) Biochemistry , vol.35 , pp. 4732-4740
    • Fisher, S.L.1    Kim, S.K.2    Wanner, B.L.3    Walsh, C.T.4
  • 16
    • 70349541000 scopus 로고    scopus 로고
    • Biological insights from structures of two-component proteins
    • Gao, R. Stock, A.M. (2009) Biological insights from structures of two-component proteins. Annu Rev Microbiol 63 : 133 154.
    • (2009) Annu Rev Microbiol , vol.63 , pp. 133-154
    • Gao, R.1    Stock, A.M.2
  • 17
    • 0000598585 scopus 로고    scopus 로고
    • Respiration
    • In. Neidhardt, F.C. Curtiss, R., III. Ingraham, J.L. Lin, E.C.C. Low, K.B. Magasanik, B.,*et al. eds). Washington, DC. ASM Press. pp.
    • Gennis, R.B. Stewart, V. (1996) Respiration. In Escherichia coli and Salmonella Cellular and Molecular Biology. Neidhardt, F.C., Curtiss, R., III., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., et al. (eds). Washington, DC : ASM Press, pp. 217 261.
    • (1996) Escherichia Coli and Salmonella Cellular and Molecular Biology , pp. 217-261
    • Gennis, R.B.1    Stewart, V.2
  • 18
    • 0033277340 scopus 로고    scopus 로고
    • The histidine kinase superfamily
    • Grebe, T.W. Stock, J.B. (1999) The histidine kinase superfamily. Adv Microbial Physiol 41 : 139 227.
    • (1999) Adv Microbial Physiol , vol.41 , pp. 139-227
    • Grebe, T.W.1    Stock, J.B.2
  • 19
    • 67449095110 scopus 로고    scopus 로고
    • Kinetic buffering of cross talk between bacterial two-component sensors
    • Groban, E.S., Clarke, E.J., Salis, H.M., Miller, S.M. Voigt, C.A. (2009) Kinetic buffering of cross talk between bacterial two-component sensors. J Mol Biol 390 : 380 393.
    • (2009) J Mol Biol , vol.390 , pp. 380-393
    • Groban, E.S.1    Clarke, E.J.2    Salis, H.M.3    Miller, S.M.4    Voigt, C.A.5
  • 20
    • 0024834564 scopus 로고
    • A reliable method for random mutagenesis: The generation of mutant libraries using spiked oligodeoxyribonucleotide primers
    • Hermes, J.D., Parekh, S.M., Blacklow, S.C., Koster, H. Knowles, J.R. (1989) A reliable method for random mutagenesis: the generation of mutant libraries using spiked oligodeoxyribonucleotide primers. Gene 84 : 143 151.
    • (1989) Gene , vol.84 , pp. 143-151
    • Hermes, J.D.1    Parekh, S.M.2    Blacklow, S.C.3    Koster, H.4    Knowles, J.R.5
  • 21
    • 0034879819 scopus 로고    scopus 로고
    • Keeping signals straight in phosphorelay signal transduction
    • Hoch, J.A. Varughese, K.I. (2001) Keeping signals straight in phosphorelay signal transduction. J Bacteriol 183 : 4941 4949.
    • (2001) J Bacteriol , vol.183 , pp. 4941-4949
    • Hoch, J.A.1    Varughese, K.I.2
  • 22
    • 0031782823 scopus 로고    scopus 로고
    • Mutations that alter the kinase and phosphatase activities of the two-component sensor EnvZ
    • Hsing, W., Russo, F.D., Bernd, K.K. Silhavy, T.J. (1998) Mutations that alter the kinase and phosphatase activities of the two-component sensor EnvZ. J Bacteriol 180 : 4538 4546.
    • (1998) J Bacteriol , vol.180 , pp. 4538-4546
    • Hsing, W.1    Russo, F.D.2    Bernd, K.K.3    Silhavy, T.J.4
  • 23
    • 0024670936 scopus 로고
    • A bacterial environmental sensor that functions as a protein kinase and stimulates transcriptional activation
    • Igo, M.M., Ninfa, A.J. Silhavy, T.J. (1989) A bacterial environmental sensor that functions as a protein kinase and stimulates transcriptional activation. Genes Dev 3 : 598 605.
    • (1989) Genes Dev , vol.3 , pp. 598-605
    • Igo, M.M.1    Ninfa, A.J.2    Silhavy, T.J.3
  • 24
    • 11844275257 scopus 로고    scopus 로고
    • Kinetic analysis of YPD1-dependent phosphotransfer reactions in the yeast osmoregulatory phosphorelay system
    • Janiak-Spens, F., Cook, P.F. West, A.H. (2005) Kinetic analysis of YPD1-dependent phosphotransfer reactions in the yeast osmoregulatory phosphorelay system. Biochemistry 44 : 377 386.
    • (2005) Biochemistry , vol.44 , pp. 377-386
    • Janiak-Spens, F.1    Cook, P.F.2    West, A.H.3
  • 25
    • 0032993415 scopus 로고    scopus 로고
    • Alanine mutants of the Spo0F response regulator modifying specificity for sensor kinases in sporulation initiation
    • Jiang, M., Tzeng, Y.L., Feher, V.A., Perego, M. Hoch, J.A. (1999) Alanine mutants of the Spo0F response regulator modifying specificity for sensor kinases in sporulation initiation. Mol Microbiol 33 : 389 395.
    • (1999) Mol Microbiol , vol.33 , pp. 389-395
    • Jiang, M.1    Tzeng, Y.L.2    Feher, V.A.3    Perego, M.4    Hoch, J.A.5
  • 26
    • 0034595228 scopus 로고    scopus 로고
    • Asymmetry in the autophosphorylation of the two-component regulatory system transmitter protein nitrogen regulator II of Escherichia coli
    • Jiang, P., Peliska, J.A. Ninfa, A.J. (2000) Asymmetry in the autophosphorylation of the two-component regulatory system transmitter protein nitrogen regulator II of Escherichia coli. Biochemistry 39 : 5057 5065.
    • (2000) Biochemistry , vol.39 , pp. 5057-5065
    • Jiang, P.1    Peliska, J.A.2    Ninfa, A.J.3
  • 27
    • 27744443258 scopus 로고    scopus 로고
    • Genome update: Distribution of two-component transduction systems in 250 bacterial genomes
    • Kiil, K., Ferchaud, J.B., David, C., Binnewies, T.T., Wu, H., Sicheritz-Ponten, T., et al. (2005) Genome update: distribution of two-component transduction systems in 250 bacterial genomes. Microbiology 151 : 3447 3452.
    • (2005) Microbiology , vol.151 , pp. 3447-3452
    • Kiil, K.1    Ferchaud, J.B.2    David, C.3    Binnewies, T.T.4    Wu, H.5    Sicheritz-Ponten, T.6
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 : 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 44449112421 scopus 로고    scopus 로고
    • Specificity in two-component signal transduction pathways
    • Laub, M.T. Goulian, M. (2007) Specificity in two-component signal transduction pathways. Annu Rev Genet 41 : 121 145.
    • (2007) Annu Rev Genet , vol.41 , pp. 121-145
    • Laub, M.T.1    Goulian, M.2
  • 30
    • 0032835113 scopus 로고    scopus 로고
    • Signal-dependent phosphorylation of the membrane-bound NarX two-component sensor-transmitter protein of Escherichia coli: Nitrate elicits a superior anion ligand response compared to nitrite
    • Lee, A.I., Delgado, A. Gunsalus, R.P. (1999) Signal-dependent phosphorylation of the membrane-bound NarX two-component sensor-transmitter protein of Escherichia coli: nitrate elicits a superior anion ligand response compared to nitrite. J Bacteriol 181 : 5309 5316.
    • (1999) J Bacteriol , vol.181 , pp. 5309-5316
    • Lee, A.I.1    Delgado, A.2    Gunsalus, R.P.3
  • 31
    • 0028023092 scopus 로고
    • In vitro interaction of nitrate-responsive regulatory protein NarL with DNA target sequences in the fdnG, narG, narK and frdA operon control regions of Escherichia coli K-12
    • Li, J., Kustu, S. Stewart, V. (1994) In vitro interaction of nitrate-responsive regulatory protein NarL with DNA target sequences in the fdnG, narG, narK and frdA operon control regions of Escherichia coli K-12. J Mol Biol 241 : 150 165.
    • (1994) J Mol Biol , vol.241 , pp. 150-165
    • Li, J.1    Kustu, S.2    Stewart, V.3
  • 32
    • 0024565620 scopus 로고
    • Genetics and sequence analysis of the pcnB locus, an Escherichia coli gene involved in plasmid copy number control
    • Liu, J. Parkinson, J.S. (1989) Genetics and sequence analysis of the pcnB locus, an Escherichia coli gene involved in plasmid copy number control. J Bacteriol 171 : 1254 1261.
    • (1989) J Bacteriol , vol.171 , pp. 1254-1261
    • Liu, J.1    Parkinson, J.S.2
  • 33
    • 17444424974 scopus 로고    scopus 로고
    • The structure of α-helical coiled coils
    • Lupas, A.N. Gruber, M. (2005) The structure of α-helical coiled coils. Adv Protein Chem 70 : 37 78.
    • (2005) Adv Protein Chem , vol.70 , pp. 37-78
    • Lupas, A.N.1    Gruber, M.2
  • 35
    • 0037192777 scopus 로고    scopus 로고
    • Phosphorylation alters the interaction of the response regulator OmpR with its sensor kinase EnvZ
    • Mattison, K. Kenney, L.J. (2002) Phosphorylation alters the interaction of the response regulator OmpR with its sensor kinase EnvZ. J Biol Chem 277 : 11143 11148.
    • (2002) J Biol Chem , vol.277 , pp. 11143-11148
    • Mattison, K.1    Kenney, L.J.2
  • 36
  • 37
    • 0000451424 scopus 로고
    • Covalent modification of the glnG product, NRI, by the glnL product, NRII, regulates the transcription of the glnALG operon in Escherichia coli
    • Ninfa, A.J. Magasanik, B. (1986) Covalent modification of the glnG product, NRI, by the glnL product, NRII, regulates the transcription of the glnALG operon in Escherichia coli. Proc Natl Acad Sci USA 83 : 5909 5913.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 5909-5913
    • Ninfa, A.J.1    Magasanik, B.2
  • 38
    • 0024061466 scopus 로고
    • Cross talk between bacterial chemotaxis signal transduction proteins and regulators of transcription of the Ntr regulon: Evidence that nitrogen assimilation and chemotaxis are controlled by a common phosphotransfer mechanism
    • Ninfa, A.J., Ninfa, E.G., Lupas, A.N., Stock, A., Magasanik, B. Stock, J. (1988) Cross talk between bacterial chemotaxis signal transduction proteins and regulators of transcription of the Ntr regulon: evidence that nitrogen assimilation and chemotaxis are controlled by a common phosphotransfer mechanism. Proc Natl Acad Sci USA 85 : 5492 5496.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5492-5496
    • Ninfa, A.J.1    Ninfa, E.G.2    Lupas, A.N.3    Stock, A.4    Magasanik, B.5    Stock, J.6
  • 40
    • 44349144008 scopus 로고    scopus 로고
    • Autophosphorylation and dephosphorylation by soluble forms of the nitrate-responsive sensors NarX and NarQ from Escherichia coli K-12
    • Noriega, C.E., Schmidt, R., Gray, M.J., Chen, L.-L. Stewart, V. (2008) Autophosphorylation and dephosphorylation by soluble forms of the nitrate-responsive sensors NarX and NarQ from Escherichia coli K-12. J Bacteriol 190 : 3869 3876.
    • (2008) J Bacteriol , vol.190 , pp. 3869-3876
    • Noriega, C.E.1    Schmidt, R.2    Gray, M.J.3    Chen, L.-L.4    Stewart, V.5
  • 41
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson, J.S. Kofoid, E.C. (1992) Communication modules in bacterial signaling proteins. Annu Rev Genet 26 : 71 112.
    • (1992) Annu Rev Genet , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 42
    • 0037312799 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of phosphatase activity of Escherichia coli NRII (NtrB) and its regulation by the PII signal transduction protein
    • Pioszak, A.A. Ninfa, A.J. (2003) Genetic and biochemical analysis of phosphatase activity of Escherichia coli NRII (NtrB) and its regulation by the PII signal transduction protein. J Bacteriol 185 : 1299 1315.
    • (2003) J Bacteriol , vol.185 , pp. 1299-1315
    • Pioszak, A.A.1    Ninfa, A.J.2
  • 43
    • 63449129765 scopus 로고    scopus 로고
    • Purine utilization by Klebsiella oxytoca M5al: Genes for ring-oxidizing and -opening enzymes
    • Pope, S.D., Chen, L.-L. Stewart, V. (2009) Purine utilization by Klebsiella oxytoca M5al: genes for ring-oxidizing and -opening enzymes. J Bacteriol 191 : 1006 1017.
    • (2009) J Bacteriol , vol.191 , pp. 1006-1017
    • Pope, S.D.1    Chen, L.-L.2    Stewart, V.3
  • 44
    • 0001427734 scopus 로고
    • Porin regulon of Escherichia coli
    • In. Hoch, J.A. Silhavy, T.J. eds). Washington DC. ASM Press. pp.
    • Pratt, L.A. Silhavy, T.J. (1995) Porin regulon of Escherichia coli. In Two-Component Signal Transduction. Hoch, J.A. Silhavy, T.J. (eds). Washington DC : ASM Press, pp. 105 127.
    • (1995) Two-Component Signal Transduction , pp. 105-127
    • Pratt, L.A.1    Silhavy, T.J.2
  • 45
    • 40149098889 scopus 로고    scopus 로고
    • Horizontal gene transfer and the evolution of transcriptional regulation in Escherichia coli
    • Price, M.N., Dehal, P.S. Arkin, A.P. (2008) Horizontal gene transfer and the evolution of transcriptional regulation in Escherichia coli. Genome Biol 9 : R4.
    • (2008) Genome Biol , vol.9 , pp. 4
    • Price, M.N.1    Dehal, P.S.2    Arkin, A.P.3
  • 46
    • 0026705854 scopus 로고
    • Either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12
    • Rabin, R.S. Stewart, V. (1992) 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 89 : 8419 8423.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8419-8423
    • Rabin, R.S.1    Stewart, V.2
  • 47
    • 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.S. Stewart, V. (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.S.1    Stewart, V.2
  • 48
    • 0028021803 scopus 로고
    • Phosphorylation and dephosphorylation of the NarQ, NarX, and NarL proteins of the nitrate-dependent two-component regulatory system of Escherichia coli
    • Schröder, I., Wolin, C.D., Cavicchioli, R. Gunsalus, R.P. (1994) Phosphorylation and dephosphorylation of the NarQ, NarX, and NarL proteins of the nitrate-dependent two-component regulatory system of Escherichia coli. J Bacteriol 176 : 4985 4992.
    • (1994) J Bacteriol , vol.176 , pp. 4985-4992
    • Schröder, I.1    Wolin, C.D.2    Cavicchioli, R.3    Gunsalus, R.P.4
  • 49
    • 0032578489 scopus 로고    scopus 로고
    • In vivo characterization of the type A and B vancomycin-resistant enterococci (VRE) VanRS two-component systems in Escherichia coli: A nonpathogenic model for studying the VRE signal transduction pathways
    • Silva, J.C., Haldimann, A., Prahalad, M.K., Walsh, C.T. Wanner, B.L. (1998) In vivo characterization of the type A and B vancomycin-resistant enterococci (VRE) VanRS two-component systems in Escherichia coli: a nonpathogenic model for studying the VRE signal transduction pathways. Proc Natl Acad Sci USA 95 : 11951 11956.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11951-11956
    • Silva, J.C.1    Haldimann, A.2    Prahalad, M.K.3    Walsh, C.T.4    Wanner, B.L.5
  • 50
    • 52649164147 scopus 로고    scopus 로고
    • Cross-talk suppression between the CpxA-CpxR and EnvZ-OmpR two-component systems in E. coli
    • Siryaporn, A. Goulian, M. (2008) Cross-talk suppression between the CpxA-CpxR and EnvZ-OmpR two-component systems in E. coli. Mol Microbiol 70 : 494 506.
    • (2008) Mol Microbiol , vol.70 , pp. 494-506
    • Siryaporn, A.1    Goulian, M.2
  • 52
    • 26444481955 scopus 로고    scopus 로고
    • Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: A system-level analysis
    • Skerker, J.M., Prasol, M.S., Perchuk, B.S., Biondi, E.G. Laub, M.T. (2005) Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis. PLoS Biol 3 : e334.
    • (2005) PLoS Biol , vol.3 , pp. 334
    • Skerker, J.M.1    Prasol, M.S.2    Perchuk, B.S.3    Biondi, E.G.4    Laub, M.T.5
  • 53
    • 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 31 : 1 10.
    • (2003) Biochem Soc Trans , vol.31 , pp. 1-10
    • Stewart, V.1
  • 54
    • 0037377805 scopus 로고    scopus 로고
    • Synthetic lac operator substitutions to study the nitrate- and nitrite-responsive NarX-NarL and NarQ-NarP two-component regulatory systems of Escherichia coli K-12
    • Stewart, V. Bledsoe, P.J. (2003) Synthetic lac operator substitutions to study the nitrate- and nitrite-responsive NarX-NarL and NarQ-NarP two-component regulatory systems of Escherichia coli K-12. J Bacteriol 185 : 2104 2111.
    • (2003) J Bacteriol , vol.185 , pp. 2104-2111
    • Stewart, V.1    Bledsoe, P.J.2
  • 55
    • 0023991777 scopus 로고
    • Identification and expression of genes narL and narX of the nar (nitrate reductase) locus in Escherichia coli K-12
    • Stewart, V. Parales, J., Jr. (1988) Identification and expression of genes narL and narX of the nar (nitrate reductase) locus in Escherichia coli K-12. J Bacteriol 170 : 1589 1597.
    • (1988) J Bacteriol , vol.170 , pp. 1589-1597
    • Stewart, V.1    Parales Jr., J.2
  • 56
    • 0001943573 scopus 로고
    • Dual sensors and dual response regulators interact to control nitrate- and nitrite-responsive gene expression in Escherichia coli
    • In. Hoch, J.A. Silhavy, T.J. eds). Washington DC. ASM Press. pp.
    • Stewart, V. Rabin, R.S. (1995) Dual sensors and dual response regulators interact to control nitrate- and nitrite-responsive gene expression in Escherichia coli. In Two-Component Signal Transduction. Hoch, J.A. Silhavy, T.J. (eds). Washington DC : ASM Press, pp. 233 252.
    • (1995) Two-Component Signal Transduction. , pp. 233-252
    • Stewart, V.1    Rabin, R.S.2
  • 57
    • 0036182372 scopus 로고    scopus 로고
    • Periplasmic nitrate reductase (NapABC enzyme) supports anaerobic respiration by Escherichia coli K-12
    • Stewart, V., Lu, Y. Darwin, A.J. (2002) Periplasmic nitrate reductase (NapABC enzyme) supports anaerobic respiration by Escherichia coli K-12. J Bacteriol 184 : 1314 1323.
    • (2002) J Bacteriol , vol.184 , pp. 1314-1323
    • Stewart, V.1    Lu, Y.2    Darwin, A.J.3
  • 58
    • 0345689429 scopus 로고    scopus 로고
    • Response to culture aeration mediated by the nitrate and nitrite sensor NarQ of Escherichia coli K-12
    • Stewart, V., Chen, L.-L. Wu, H.C. (2003) Response to culture aeration mediated by the nitrate and nitrite sensor NarQ of Escherichia coli K-12. Mol Microbiol 50 : 1391 1399.
    • (2003) Mol Microbiol , vol.50 , pp. 1391-1399
    • Stewart, V.1    Chen, L.-L.2    Wu, H.C.3
  • 60
    • 0001792698 scopus 로고
    • Two-component signal transduction systems: Structure-function relationships and mechanisms of catalysis
    • In. Hoch, J.A. Silhavy, T.J. eds). Washington DC. ASM Press. pp.
    • Stock, J.B., Surette, M.G., Levit, M. Park, P. (1995) Two-component signal transduction systems: structure-function relationships and mechanisms of catalysis. In Two-Component Signal Transduction. Hoch, J.A. Silhavy, T.J. (eds). Washington DC : ASM Press, pp. 25 51.
    • (1995) Two-Component Signal Transduction. , pp. 25-51
    • Stock, J.B.1    Surette, M.G.2    Levit, M.3    Park, P.4
  • 61
    • 48249148736 scopus 로고    scopus 로고
    • Co-evolving motions at protein-protein interfaces of two-component signaling systems identified by covariance analysis
    • Szurmant, H., Bobay, B.G., White, R.A., Sullivan, D.M., Thompson, R.J., Hwa, T., et al. (2008) Co-evolving motions at protein-protein interfaces of two-component signaling systems identified by covariance analysis. Biochemistry 47 : 7782 7784.
    • (2008) Biochemistry , vol.47 , pp. 7782-7784
    • Szurmant, H.1    Bobay, B.G.2    White, R.A.3    Sullivan, D.M.4    Thompson, R.J.5    Hwa, T.6
  • 62
    • 0027532540 scopus 로고
    • Phosphorylation and dephosphorylation catalyzed in vitro by purified components of the nitrate sensing system, NarX and NarL
    • Walker, M.S. DeMoss, J.A. (1993) Phosphorylation and dephosphorylation catalyzed in vitro by purified components of the nitrate sensing system, NarX and NarL. J Biol Chem 268 : 8391 8393.
    • (1993) J Biol Chem , vol.268 , pp. 8391-8393
    • Walker, M.S.1    Demoss, J.A.2
  • 63
    • 0026576546 scopus 로고
    • Is cross regulation by phosphorylation of two-component response regulator proteins important in bacteria?
    • Wanner, B.L. (1992) Is cross regulation by phosphorylation of two-component response regulator proteins important in bacteria? J Bacteriol 174 : 2053 2058.
    • (1992) J Bacteriol , vol.174 , pp. 2053-2058
    • Wanner, B.L.1
  • 64
    • 0042796229 scopus 로고    scopus 로고
    • Are the multiple signal transduction pathways of the Pho regulon due to cross talk or cross regulation?
    • In. Lin, E.C.C. Lynch, A.S. eds). Georgetown, TX. R G Landes. pp.
    • Wanner, B.L., Jiang, W., Kim, S.-K., Yamagata, D., Haldimann, A. Daniels, L.L. (1996) Are the multiple signal transduction pathways of the Pho regulon due to cross talk or cross regulation? In Regulation of Gene Expression in Escherichia coli. Lin, E.C.C. Lynch, A.S. (eds). Georgetown, TX : R G Landes, pp. 297 315.
    • (1996) Regulation of Gene Expression in Escherichia Coli. , pp. 297-315
    • Wanner, B.L.1    Jiang, W.2    Kim, S.-K.3    Yamagata, D.4    Haldimann, A.5    Daniels, L.L.6
  • 65
    • 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 K-12
    • Williams, S.B. Stewart, V. (1997a) Discrimination between structurally related ligands nitrate and nitrite controls autokinase activity of the NarX transmembrane signal transducer of Escherichia coli K-12. Mol Microbiol 26 : 911 925.
    • (1997) Mol Microbiol , vol.26 , pp. 911-925
    • Williams, S.B.1    Stewart, V.2
  • 66
    • 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. Stewart, V. (1997b) 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
  • 67
    • 0036400593 scopus 로고    scopus 로고
    • Histidine protein kinases: Key signal transducers outside the animal kingdom
    • reviews3013. 3018.
    • Wolanin, P.M., Thomason, P.A. Stock, J.B. (2002) Histidine protein kinases: key signal transducers outside the animal kingdom. Genome Biol 3 : reviews3013. 3011 3013 3018.
    • (2002) Genome Biol , vol.3 , pp. 3011-3013
    • Wolanin, P.M.1    Thomason, P.A.2    Stock, J.B.3
  • 68
    • 12544258487 scopus 로고    scopus 로고
    • Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli
    • Yamamoto, K., Hirao, K., Oshima, T., Aiba, H., Utsumi, R. Ishihama, A. (2005) Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli. J Biol Chem 280 : 1448 1456.
    • (2005) J Biol Chem , vol.280 , pp. 1448-1456
    • Yamamoto, K.1    Hirao, K.2    Oshima, T.3    Aiba, H.4    Utsumi, R.5    Ishihama, A.6
  • 69
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J. Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33 : 103 119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 70
    • 0036886272 scopus 로고    scopus 로고
    • Interaction of EnvZ, a sensory histidine kinase, with phosphorylated OmpR, the cognate response regulator
    • DOI 10.1046/j.1365-2958.2002.03240.x
    • Yoshida, T., Cai, S. Inouye, M. (2002) Interaction of EnvZ, a sensory histidine kinase, with phosphorylated OmpR, the cognate response regulator. Mol Microbiol 46 : 1283 1294. (Pubitemid 36961263)
    • (2002) Molecular Microbiology , vol.46 , Issue.5 , pp. 1283-1294
    • Yoshida, T.1    Cai, S.J.2    Inouye, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.