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Volumn 48, Issue 1, 2003, Pages 25-51

Comparative analysis of prototype two-component systems with either bifunctional or monofunctional sensors: Differences in molecular structure and physiological function

Author keywords

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Indexed keywords

PROTEIN;

EID: 0037383238     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03344.x     Document Type: Article
Times cited : (83)

References (58)
  • 1
    • 0033665572 scopus 로고    scopus 로고
    • Extending the method of mathematically controlled comparison to include numerical comparisons
    • Alves, R., and Savageau, M.A. (2000a) Extending the method of mathematically controlled comparison to include numerical comparisons. Bioinformatics 16: 786-798.
    • (2000) Bioinformatics , vol.16 , pp. 786-798
    • Alves, R.1    Savageau, M.A.2
  • 2
    • 0033828273 scopus 로고    scopus 로고
    • Systemic properties of ensembles of metabolic networks: Application of graphical and statistical methods to simple unbranched pathways
    • Alves, R., and Savageau, M.A. (2000b) Systemic properties of ensembles of metabolic networks: application of graphical and statistical methods to simple unbranched pathways. Bioinformatics 16: 534-547.
    • (2000) Bioinformatics , vol.16 , pp. 534-547
    • Alves, R.1    Savageau, M.A.2
  • 3
    • 0033832419 scopus 로고    scopus 로고
    • Comparing systemic properties of ensembles of biological networks by graphical and statistical methods
    • Alves, R., and Savageau, M.A. (2000c) Comparing systemic properties of ensembles of biological networks by graphical and statistical methods. Bioinformatics 16: 527-533.
    • (2000) Bioinformatics , vol.16 , pp. 527-533
    • Alves, R.1    Savageau, M.A.2
  • 4
    • 0031026581 scopus 로고    scopus 로고
    • The Vans sensor negatively controls VanR-mediated transcriptional activation of glycopeptide resistance genes of Tn1546 and related elements in the absence of induction
    • Arthur, M., Depardieu, F., Gerbaud, G., Galimand, M., Leclercq, R., and Courvalin, P. (1997) The Vans sensor negatively controls VanR-mediated transcriptional activation of glycopeptide resistance genes of Tn1546 and related elements in the absence of induction. J Bacteriol 179: 97-106.
    • (1997) J Bacteriol , vol.179 , pp. 97-106
    • Arthur, M.1    Depardieu, F.2    Gerbaud, G.3    Galimand, M.4    Leclercq, R.5    Courvalin, P.6
  • 6
    • 18144446008 scopus 로고    scopus 로고
    • Regulation of phosphatase activity in bacterial chemotaxis
    • Blat, Y., Gillespie, B., Bren, A., Dahlquist, F.W., and Eisenbach, M. (1998) Regulation of phosphatase activity in bacterial chemotaxis. J Mol Biol 284: 1191-1199.
    • (1998) J Mol Biol , vol.284 , pp. 1191-1199
    • Blat, Y.1    Gillespie, B.2    Bren, A.3    Dahlquist, F.W.4    Eisenbach, M.5
  • 7
    • 0030739086 scopus 로고    scopus 로고
    • Locked on and locked off signal transduction mutations in the periplasmic domain of the Escherichia coli NarQ and NarX sensors affect nitrate and nitrite dependent regulation by NarL and NarP
    • Chiang, R.C., Cavicchioli, R., and Gunsalus, R.P. (1997) Locked on and locked off signal transduction mutations in the periplasmic domain of the Escherichia coli NarQ and NarX sensors affect nitrate and nitrite dependent regulation by NarL and NarP. Mol Microbiol 24: 1049-1060.
    • (1997) Mol Microbiol , vol.24 , pp. 1049-1060
    • Chiang, R.C.1    Cavicchioli, R.2    Gunsalus, R.P.3
  • 9
    • 0029977826 scopus 로고    scopus 로고
    • Control of bacterial chemotaxis
    • Eisenbach, M. (1996) Control of bacterial chemotaxis. Mol Microbiol 20: 903-910.
    • (1996) Mol Microbiol , vol.20 , pp. 903-910
    • Eisenbach, M.1
  • 10
    • 0026662751 scopus 로고
    • Role of phosphorylated metabolic intermediates in the regulation of glutamine synthetase synthesis
    • Feng, J., Atkinson, M.R., McCleary, W., Stock, J.B., Wanner, B.L., and Ninfa, A.J. (1992) Role of phosphorylated metabolic intermediates in the regulation of glutamine synthetase synthesis. J Bacteriol 174: 6061-6070.
    • (1992) J Bacteriol , vol.174 , pp. 6061-6070
    • Feng, J.1    Atkinson, M.R.2    McCleary, W.3    Stock, J.B.4    Wanner, B.L.5    Ninfa, A.J.6
  • 11
    • 0028363906 scopus 로고
    • Cross talk between the two component regulatory systems NodVW and NwsAB of Bradyrhizobium japonicum
    • Grob, P., Hennecke, H., and Gottfert, M. (1994) Cross talk between the two component regulatory systems NodVW and NwsAB of Bradyrhizobium japonicum. FEMS Microbiol Lett 120: 349-353.
    • (1994) FEMS Microbiol Lett , vol.120 , pp. 349-353
    • Grob, P.1    Hennecke, H.2    Gottfert, M.3
  • 12
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling
    • Guex, N., and Peitsch, M.C. (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling. Electrophoresis 18: 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 14
    • 0029033413 scopus 로고
    • Subunit structure of regulator proteins influences the design of gene circuitry: Analysis of perfectly coupled and completely uncoupled circuits
    • Hlavacek, W.S., and Savageau, M.A. (1995) Subunit structure of regulator proteins influences the design of gene circuitry: Analysis of perfectly coupled and completely uncoupled circuits. J Mol Biol 248: 739-755.
    • (1995) J Mol Biol , vol.248 , pp. 739-755
    • Hlavacek, W.S.1    Savageau, M.A.2
  • 15
    • 0030002954 scopus 로고    scopus 로고
    • Rules for coupled expression of regulator and effector genes in inducible circuits
    • Hlavacek, W.S., and Savageau, M.A. (1996) Rules for coupled expression of regulator and effector genes in inducible circuits. J Mol Biol 255: 121-139.
    • (1996) J Mol Biol , vol.255 , pp. 121-139
    • Hlavacek, W.S.1    Savageau, M.A.2
  • 16
    • 0031588690 scopus 로고    scopus 로고
    • Completely uncoupled and perfectly coupled gene expression in repressible systems
    • Hlavacek, W.S., and Savageau, M.A. (1997) Completely uncoupled and perfectly coupled gene expression in repressible systems. J Mol Biol 266: 538-558.
    • (1997) J Mol Biol , vol.266 , pp. 538-558
    • Hlavacek, W.S.1    Savageau, M.A.2
  • 18
    • 0031782823 scopus 로고    scopus 로고
    • Mutations that alter the kinase and phosphatase activities of the two-component sensor EnvZ
    • Hsing, W.H, Russo, F.D., Bernd, K.K., and 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.H.1    Russo, F.D.2    Bernd, K.K.3    Silhavy, T.J.4
  • 19
    • 0029976302 scopus 로고    scopus 로고
    • The signal-transduction network for Pho regulation in Bacillus subtilis
    • Hulett, F.M. (1996) The signal-transduction network for Pho regulation in Bacillus subtilis. Mol Microbiol 19: 933-939.
    • (1996) Mol Microbiol , vol.19 , pp. 933-939
    • Hulett, F.M.1
  • 20
    • 0024759933 scopus 로고
    • Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor
    • Igo, M.M., Ninfa, A.J., Stock, J.B., and Silhavy, T.J. (1989) Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor. Gene Devel 3: 1725-1734.
    • (1989) Gene Devel , vol.3 , pp. 1725-1734
    • Igo, M.M.1    Ninfa, A.J.2    Stock, J.B.3    Silhavy, T.J.4
  • 22
    • 0021925233 scopus 로고
    • Network regulation of the immune response: Alternative control points for suppressor modulation of effector lymphocytes
    • Irvine, D.H., and Savageau, M.A. (1985) Network regulation of the immune response: alternative control points for suppressor modulation of effector lymphocytes. J Immunol 134: 99-109.
    • (1985) J Immunol , vol.134 , pp. 99-109
    • Irvine, D.H.1    Savageau, M.A.2
  • 23
    • 0032994344 scopus 로고    scopus 로고
    • Regulation of autophosphorylation of Escherichia coli Nitrogen regulator II by the PII signal transduction protein
    • Jiang, P., and Ninfa, A.J. (1999) Regulation of autophosphorylation of Escherichia coli Nitrogen regulator II by the PII signal transduction protein. J Bacteriol 181: 1906-1911.
    • (1999) J Bacteriol , vol.181 , pp. 1906-1911
    • Jiang, P.1    Ninfa, A.J.2
  • 24
    • 0032500535 scopus 로고    scopus 로고
    • Individual substitutions of clustered arginine residues of the sensor kinase KdpD of Escherichia coli modulate the ratio of kinase to phosphatase activity
    • Jung, K., and Altendorf, K. (1998) Individual substitutions of clustered arginine residues of the sensor kinase KdpD of Escherichia coli modulate the ratio of kinase to phosphatase activity. J Biol Chem 273: 26415-26420.
    • (1998) J Biol Chem , vol.273 , pp. 26415-26420
    • Jung, K.1    Altendorf, K.2
  • 25
    • 0030935385 scopus 로고    scopus 로고
    • Purification, reconstitution, and characterization of KdpD, the turgor sensor of Escherichia coli
    • Jung, K., Tjaden, B., and Altendorf, K. (1997) Purification, reconstitution, and characterization of KdpD, the turgor sensor of Escherichia coli. J Biol Chem 272: 10847-10852.
    • (1997) J Biol Chem , vol.272 , pp. 10847-10852
    • Jung, K.1    Tjaden, B.2    Altendorf, K.3
  • 26
    • 0002650761 scopus 로고    scopus 로고
    • Cytoplasmic membrane
    • Neidhardt, F.C., (ed). Washington D.C.: American Society for Microbiology Press
    • Kadner, R.J. (1996) Cytoplasmic membrane. In Escherichia Coli and Salmonella: Cellular and Molecular Biology. Neidhardt, F.C., (ed). Washington D.C.: American Society for Microbiology Press, pp. 58-87.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 58-87
    • Kadner, R.J.1
  • 27
    • 0024816538 scopus 로고
    • Signal transduction and osmoregulation in Escherichia coli. A single amino acid change in the protein kinase, EnvZ, results in loss of its phosphorylation and dephosphorylation abilities with respect to the activator protein, OmpR
    • Kanamaru, K., Aiba, H., Mizushima, S., and Mizuno, T. (1989) Signal transduction and osmoregulation in Escherichia coli. A single amino acid change in the protein kinase, EnvZ, results in loss of its phosphorylation and dephosphorylation abilities with respect to the activator protein, OmpR. J Biol Chem 264: 21633-21637.
    • (1989) J Biol Chem , vol.264 , pp. 21633-21637
    • Kanamaru, K.1    Aiba, H.2    Mizushima, S.3    Mizuno, T.4
  • 28
    • 0024040412 scopus 로고
    • Protein kinase and phosphoprotein phosphatase activities of nitrogen regulatory proteins NTRB and NTRC of enteric bacteria: Roles of the conserved amino-terminal domain of NTRC
    • Keener, J., and Kustu, S. (1988) Protein kinase and phosphoprotein phosphatase activities of nitrogen regulatory proteins NTRB and NTRC of enteric bacteria: roles of the conserved amino-terminal domain of NTRC. Proc Natl Acad Sci USA 85: 4976-4980.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4976-4980
    • Keener, J.1    Kustu, S.2
  • 29
    • 0026512864 scopus 로고
    • Phosphorylation of bacterial response regulator proteins by low molecular weight phosphodonors
    • Lukat, G.S., McCleary, W.R., Stock, A.M., and Stock, J.B. (1992) Phosphorylation of bacterial response regulator proteins by low molecular weight phosphodonors. Proc Natl Acad Sci USA 89: 718-722.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 718-722
    • Lukat, G.S.1    McCleary, W.R.2    Stock, A.M.3    Stock, J.B.4
  • 30
    • 0033596698 scopus 로고    scopus 로고
    • Kinetic characterization of CheY phosphorylation reactions: Comparison of P-CheA and small-molecule phosphodonors
    • Mayover, T.L., Halkides, C.J., and Stewart, R.C. (1999) Kinetic characterization of CheY phosphorylation reactions: Comparison of P-CheA and small-molecule phosphodonors. Biochemistry 38: 2259-2271.
    • (1999) Biochemistry , vol.38 , pp. 2259-2271
    • Mayover, T.L.1    Halkides, C.J.2    Stewart, R.C.3
  • 31
    • 0029896773 scopus 로고    scopus 로고
    • The activation of PhoB by Acetylphosphate
    • McCleary, W.R. (1996) The activation of PhoB by Acetylphosphate. Mol Microbiol 20: 1155-1163.
    • (1996) Mol Microbiol , vol.20 , pp. 1155-1163
    • McCleary, W.R.1
  • 32
    • 0028961335 scopus 로고
    • SCOP, a structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T., and Chothia, C. (1995) SCOP, a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247: 536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 33
    • 0024061466 scopus 로고
    • Crosstalk 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., and Stock, J. (1988) Crosstalk 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 84: 5492-5496.
    • (1988) Proc Natl Acad Sci USA , vol.84 , pp. 5492-5496
    • Ninfa, A.J.1    Ninfa, E.G.2    Lupas, A.N.3    Stock, A.4    Magasanik, B.5    Stock, J.6
  • 34
    • 0025830353 scopus 로고
    • Reconstitution of the bacterial chemotaxis signal transduction system from purified components
    • Ninfa, E.G., Stock, A., Mowbray, S., and Stock, J. (1991) Reconstitution of the bacterial chemotaxis signal transduction system from purified components. J Biol Chem 266: 9764-9770.
    • (1991) J Biol Chem , vol.266 , pp. 9764-9770
    • Ninfa, E.G.1    Stock, A.2    Mowbray, S.3    Stock, J.4
  • 35
    • 0027243652 scopus 로고
    • Signal transduction schemes of bacteria
    • Parkinson, J.S. (1993) Signal transduction schemes of bacteria. Cell 73: 857-871.
    • (1993) Cell , vol.73 , pp. 857-871
    • Parkinson, J.S.1
  • 36
    • 0029869294 scopus 로고    scopus 로고
    • Protein aspartate phosphatases control the output of two-component signal transduction systems
    • Perego, M., and Hoch, J.A. (1996) Protein aspartate phosphatases control the output of two-component signal transduction systems. Trends Genetics 12: 97-101.
    • (1996) Trends Genetics , vol.12 , pp. 97-101
    • Perego, M.1    Hoch, J.A.2
  • 37
    • 0037312799 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of the phosphatase activity of Escherichia coli NRII (NtrB) and its regulation by the PII signal transduction protein
    • Pioszak, A.A., and Ninfa, A.J. (2003) Genetic and biochemical analysis of the 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
  • 38
    • 0032035043 scopus 로고    scopus 로고
    • Signal transduction by MAP kinase cascades in budding yeast
    • Posas, F., Takekawa, M., and Saito, H. (1998) Signal transduction by MAP kinase cascades in budding yeast. Curr Op Microbiol 1: 175-182.
    • (1998) Curr Op Microbiol , vol.1 , pp. 175-182
    • Posas, F.1    Takekawa, M.2    Saito, H.3
  • 39
    • 0029992419 scopus 로고    scopus 로고
    • From acids to osmZ: Multiple factors influence synthesis of the OmpF and OmpC porins in Escherichia coli
    • Pratt, L.A., Hsing, W.H., Gibson, K.E., and Silhavy, T.J. (1996) From acids to osmZ: Multiple factors influence synthesis of the OmpF and OmpC porins in Escherichia coli. Mol Microbiol 20: 911-917.
    • (1996) Mol Microbiol , vol.20 , pp. 911-917
    • Pratt, L.A.1    Hsing, W.H.2    Gibson, K.E.3    Silhavy, T.J.4
  • 40
    • 0024787464 scopus 로고
    • Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY
    • Sanders, D.A., Gillecastro, B.L., Stoch, A.M., Burlingame, A.L., and Koshland, D.E. (1989) Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY. J Biol Chem 264: 21770-21778.
    • (1989) J Biol Chem , vol.264 , pp. 21770-21778
    • Sanders, D.A.1    Gillecastro, B.L.2    Stoch, A.M.3    Burlingame, A.L.4    Koshland, D.E.5
  • 41
    • 0014658880 scopus 로고
    • Biochemical Systems Analysis II: The steady-state solution for an n-pool system using a power-law approximation
    • Savageau, M.A. (1969) Biochemical Systems Analysis II: The steady-state solution for an n-pool system using a power-law approximation. J Theor Biol 25: 370-379.
    • (1969) J Theor Biol , vol.25 , pp. 370-379
    • Savageau, M.A.1
  • 42
    • 0015103748 scopus 로고
    • Concepts relating the behaviour of biochemical systems to their underlying molecular properties
    • Savageau, M.A. (1971a) Concepts relating the behaviour of biochemical systems to their underlying molecular properties. Arch Biochem Biophys 145: 612-621.
    • (1971) Arch Biochem Biophys , vol.145 , pp. 612-621
    • Savageau, M.A.1
  • 43
    • 0015231849 scopus 로고
    • Parameter sensitivity as a criterion for evaluating and comparing the performance of biochemical systems
    • Savageau, M.A. (1971b) Parameter sensitivity as a criterion for evaluating and comparing the performance of biochemical systems. Nature 229: 542-544
    • (1971) Nature , vol.229 , pp. 542-544
    • Savageau, M.A.1
  • 44
    • 85012694370 scopus 로고
    • The behavior of intact biochemical control systems
    • Savageau, M.A. (1972) The behavior of intact biochemical control systems. Curr Top Cell Reg 6: 63-130.
    • (1972) Curr Top Cell Reg , vol.6 , pp. 63-130
    • Savageau, M.A.1
  • 45
    • 0016788494 scopus 로고
    • Optimal design of feedback control by inhibition: Dynamical considerations
    • Savageau, M.A. (1975) Optimal design of feedback control by inhibition: Dynamical considerations. J Mol Evol 5: 199-222.
    • (1975) J Mol Evol , vol.5 , pp. 199-222
    • Savageau, M.A.1
  • 47
    • 0031297087 scopus 로고    scopus 로고
    • Ethylene and cytokinin signalling in plants: The role of two-component systems
    • Schaller, G.E. (1997) Ethylene and cytokinin signalling in plants: the role of two-component systems. Essays Biochem 32: 101-111.
    • (1997) Essays Biochem , vol.32 , pp. 101-111
    • Schaller, G.E.1
  • 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
    • Schroder, I., Wolin, C.D., Cavicchioli, R., and 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: 4985-4991.
    • (1994) J Bacteriol , vol.176 , pp. 4985-4991
    • Schroder, I.1    Wolin, C.D.2    Cavicchioli, R.3    Gunsalus, R.P.4
  • 49
    • 0344922161 scopus 로고    scopus 로고
    • Decay of activated Bacillus subtilis pho response regulator, PhoP-P, involves the PhoR-P intermediate
    • Shi, L., Liu, W., and Hulett, F.M. (1999) Decay of activated Bacillus subtilis pho response regulator, PhoP-P, involves the PhoR-P intermediate. Biochemistry 37: 14575-14584.
    • (1999) Biochemistry , vol.37 , pp. 14575-14584
    • Shi, L.1    Liu, W.2    Hulett, F.M.3
  • 50
    • 0026470975 scopus 로고
    • The tricarboxylic acid cycle in Dictyostelium discoideum II. Evaluation of model consistency and robustness
    • Shiraishi, F., and Savageau, M.A. (1992) The tricarboxylic acid cycle in Dictyostelium discoideum II. Evaluation of model consistency and robustness. J Biol Chem 267: 22919-22925.
    • (1992) J Biol Chem , vol.267 , pp. 22919-22925
    • Shiraishi, F.1    Savageau, M.A.2
  • 51
    • 0024673614 scopus 로고
    • A comparison of variant theories of intact biochemical systems 1. Enzyme-enzyme interactions and biochemical systems theory
    • Sorribas, A., and Savageau, M.A. (1989) A comparison of variant theories of intact biochemical systems 1, Enzyme-enzyme interactions and biochemical systems theory. Math Biosci 94: 161-193.
    • (1989) Math Biosci , vol.94 , pp. 161-193
    • Sorribas, A.1    Savageau, M.A.2
  • 52
    • 0023661067 scopus 로고
    • Accuracy of alternative representations for integrated biochemical systems
    • Voit, E.O., and Savageau, M.A. (1987) Accuracy of alternative representations for integrated biochemical systems. Biochemistry 26: 6869-6880.
    • (1987) Biochemistry , vol.26 , pp. 6869-6880
    • Voit, E.O.1    Savageau, M.A.2
  • 53
    • 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
  • 54
    • 0345353513 scopus 로고
    • Phosphorylation of nitrogen regulator I (NRI) of Escherichia coli
    • Weiss, V.V., and Magasanik, B. (1988) Phosphorylation of nitrogen regulator I (NRI) of Escherichia coli. Proc Natl Acad Sci USA 85: 5492-5496.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5492-5496
    • Weiss, V.V.1    Magasanik, B.2
  • 55
    • 0029823740 scopus 로고    scopus 로고
    • Identification of an asymmetrically localized sensor histidine kinase responsible for temporally and spatially regulated transcription
    • Wingrove, J.A., and Gober, J.W. (1996) Identification of an asymmetrically localized sensor histidine kinase responsible for temporally and spatially regulated transcription. Science 274: 597-601.
    • (1996) Science , vol.274 , pp. 597-601
    • Wingrove, J.A.1    Gober, J.W.2
  • 57
    • 0027164115 scopus 로고
    • Purification and characterization of VanR and the cytosolic domain of VanS - A two component regulatory system required for vancomycin resistance in Enterococcus faecium BM4147
    • Wright, G.D., Holman, T.R., and Walsh, C.T. (1993) Purification and characterization of VanR and the cytosolic domain of VanS - A two component regulatory system required for vancomycin resistance in Enterococcus faecium BM4147. Biochemistry 32: 5057-5063.
    • (1993) Biochemistry , vol.32 , pp. 5057-5063
    • Wright, G.D.1    Holman, T.R.2    Walsh, C.T.3
  • 58
    • 0034608954 scopus 로고    scopus 로고
    • Phosphatase activity of histidine kinase EnvZ without kinase catalytic domain
    • Zhu, Y., Qin, L., Yoshida, T., and Inouye, M. (2000) Phosphatase activity of histidine kinase EnvZ without kinase catalytic domain. Proc Natl Acad Sci USA 97: 7808-7813.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7808-7813
    • Zhu, Y.1    Qin, L.2    Yoshida, T.3    Inouye, M.4


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