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Volumn 185, Issue 4, 2003, Pages 1299-1315

Genetic and biochemical analysis of phosphatase activity of Escherichia coli NRII (NtrB) and its regulation by the PII signal transduction protein

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; GLNK SIGNAL TRANSDUCTION PROTEIN; PHOSPHATASE; PII SIGNAL TRANSDUCTION PROTEIN; UNCLASSIFIED DRUG;

EID: 0037312799     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.4.1299-1315.2003     Document Type: Article
Times cited : (32)

References (57)
  • 2
    • 0036777892 scopus 로고    scopus 로고
    • Context-dependent functions of the PII and GlnK signal transduction proteins in Escherichia coli
    • Atkinson, M. R., T. A. Blauwkamp, and A. J. Ninfa. 2002. Context-dependent functions of the PII and GlnK signal transduction proteins in Escherichia coli. J. Bacteriol. 184:5364-5375.
    • (2002) J. Bacteriol. , vol.184 , pp. 5364-5375
    • Atkinson, M.R.1    Blauwkamp, T.A.2    Ninfa, A.J.3
  • 3
    • 0036778131 scopus 로고    scopus 로고
    • Activation of the glnA, glnK, and nac promoters as Escherichia coli undergoes the transition from nitrogen-excess growth to nitrogen starvation
    • Atkinson, M. R., T. A. Blauwkamp, V. Bondarenko, V. Studitsky, and A. J. Ninfa. 2002. Activation of the glnA, glnK, and nac promoters as Escherichia coli undergoes the transition from nitrogen-excess growth to nitrogen starvation. J. Bacteriol. 184:5358-5363.
    • (2002) J. Bacteriol. , vol.184 , pp. 5358-5363
    • Atkinson, M.R.1    Blauwkamp, T.A.2    Bondarenko, V.3    Studitsky, V.4    Ninfa, A.J.5
  • 4
    • 0028061944 scopus 로고
    • Reversible uridytylation of the Escherichia coli PII signal transduction protein regulates its ability to stimulate the dephosphorylation of the transcription factor nitrogen regulator I (NRI or NtrC)
    • Atkinson, M. R., E. S. Kamberov, R. L. Weiss, and A. J. Ninfa. 1994. Reversible uridytylation of the Escherichia coli PII signal transduction protein regulates its ability to stimulate the dephosphorylation of the transcription factor nitrogen regulator I (NRI or NtrC). J. Biol. Chem. 269:28288-28293.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28288-28293
    • Atkinson, M.R.1    Kamberov, E.S.2    Weiss, R.L.3    Ninfa, A.J.4
  • 5
    • 0026647630 scopus 로고
    • Characterization of mutations in the glnL gene of Escherichia coli affecting nitrogen regulation
    • Atkinson, M. R., and A. J. Ninfa. 1992. Characterization of mutations in the glnL gene of Escherichia coli affecting nitrogen regulation. J. Bacteriol. 174:4538-4548.
    • (1992) J. Bacteriol. , vol.174 , pp. 4538-4548
    • Atkinson, M.R.1    Ninfa, A.J.2
  • 6
    • 0027441194 scopus 로고
    • Mutational analysis of the bacterial signal-transducing protein kinase/phosphatase nitrogen regulator II (NRII or NtrB)
    • Atkinson, M. R., and A. J. Ninfa. 1993. Mutational analysis of the bacterial signal-transducing protein kinase/phosphatase nitrogen regulator II (NRII or NtrB). J. Bacteriol. 175:7016-7023.
    • (1993) J. Bacteriol. , vol.175 , pp. 7016-7023
    • Atkinson, M.R.1    Ninfa, A.J.2
  • 7
    • 0031824606 scopus 로고    scopus 로고
    • Role of the GlnK signal transduction protein in the regulation of nitrogen assimilation in Escherichia coli
    • Atkinson, M. R., and A. J. Ninfa. 1998. Role of the GlnK signal transduction protein in the regulation of nitrogen assimilation in Escherichia coli. Mol. Microbiol. 29:431-447.
    • (1998) Mol. Microbiol. , vol.29 , pp. 431-447
    • Atkinson, M.R.1    Ninfa, A.J.2
  • 8
    • 0032895784 scopus 로고    scopus 로고
    • Characterization of the GlnK protein of Escherichia coli
    • Atkinson, M. R., and A. J. Ninfa. 1999. Characterization of the GlnK protein of Escherichia coli. Mol. Microbiol. 32:301-314.
    • (1999) Mol. Microbiol. , vol.32 , pp. 301-314
    • Atkinson, M.R.1    Ninfa, A.J.2
  • 9
    • 0032743935 scopus 로고    scopus 로고
    • Chromatographic methods to study protein-protein interactions
    • Beeckmans, S. 1999. Chromatographic methods to study protein-protein interactions. Methods 19:278-305.
    • (1999) Methods , vol.19 , pp. 278-305
    • Beeckmans, S.1
  • 10
    • 0033534368 scopus 로고    scopus 로고
    • Structure of CheA, a signal-transducing histidine kinase
    • Bilwes, A. M., L. A. Alex, B. R. Crane, and M. I. Simon. 1999. Structure of CheA, a signal-transducing histidine kinase. Cell 96:131-141.
    • (1999) Cell , vol.96 , pp. 131-141
    • Bilwes, A.M.1    Alex, L.A.2    Crane, B.R.3    Simon, M.I.4
  • 11
    • 0036065001 scopus 로고    scopus 로고
    • Nac-mediated repression of the sera promoter of Escherichia coli
    • Blauwkamp, T. A., and A. J. Ninfa. 2002. Nac-mediated repression of the sera promoter of Escherichia coli. Mol. Microbiol. 45:351-363.
    • (2002) Mol. Microbiol. , vol.45 , pp. 351-363
    • Blauwkamp, T.A.1    Ninfa, A.J.2
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 13
    • 0022402203 scopus 로고
    • Role of glnB and glnD gene products in regulation of the glnALG operon of Escherichia coli
    • Bueno, R., G. Pahel, and B. Magasanik. 1985. Role of glnB and glnD gene products in regulation of the glnALG operon of Escherichia coli. J. Bacteriol. 164:816-822.
    • (1985) J. Bacteriol. , vol.164 , pp. 816-822
    • Bueno, R.1    Pahel, G.2    Magasanik, B.3
  • 15
    • 0029843812 scopus 로고    scopus 로고
    • Role of the periplasmic domain of the Escherichia coli NarX sensor-transmitter protein in nitrate-dependent signal transduction and gene regulation
    • Cavicchioli, R., R. C. Chiang, L. V. Kalman, and R. P. Gunsalus. 1996. Role of the periplasmic domain of the Escherichia coli NarX sensor-transmitter protein in nitrate-dependent signal transduction and gene regulation. Mol. Microbiol. 21:901-911.
    • (1996) Mol. Microbiol. , vol.21 , pp. 901-911
    • Cavicchioli, R.1    Chiang, R.C.2    Kalman, L.V.3    Gunsalus, R.P.4
  • 17
    • 0020070412 scopus 로고
    • Characterization of a gene, glnL, the product of which is involved in the regulation of nitrogen utilization in Escherichia coli
    • Chen, Y.-M., K. Backman, and B. Magasanik. 1982. Characterization of a gene, glnL, the product of which is involved in the regulation of nitrogen utilization in Escherichia coli. J. Bacteriol. 150:214-220.
    • (1982) J. Bacteriol. , vol.150 , pp. 214-220
    • Chen, Y.-M.1    Backman, K.2    Magasanik, B.3
  • 18
    • 0026662751 scopus 로고
    • Role of phosphorylated metabolic intermediates in the regulation of glutamine synthetase synthesis in Escherichia coli
    • Feng, J., M. R. Atkinson, W. McCleary, J. B. Stock, B. L. Wanner, and A. J. Ninfa. 1992. Role of phosphorylated metabolic intermediates in the regulation of glutamine synthetase synthesis in Escherichia coli. 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
  • 19
    • 0034619515 scopus 로고    scopus 로고
    • Functional dissection of the dimerization and enzymatic activities of Escherichia coli nitrogen regulator II and their regulation by the PII protein
    • Jiang, P., M. R. Atkinson, C. Srisawat, Q. Sun, and A. J. Ninfa. 2000. Functional dissection of the dimerization and enzymatic activities of Escherichia coli nitrogen regulator II and their regulation by the PII protein. Biochemistry 39:13433-13449.
    • (2000) Biochemistry , vol.39 , pp. 13433-13449
    • Jiang, P.1    Atkinson, M.R.2    Srisawat, C.3    Sun, Q.4    Ninfa, A.J.5
  • 20
    • 0032994344 scopus 로고    scopus 로고
    • Regulation of the autophosphorylation of Escherichia coli NRII by the PII signal transduction protein
    • Jiang, P., and A. J. Ninfa. 1999. Regulation of the autophosphorylation of Escherichia coli NRII 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
  • 21
    • 0013118030 scopus 로고    scopus 로고
    • Asymmetry in the autophosphorylation of the two-component system transmitter protein NRII (NtrB) of Escherichia coli
    • Jiang, P., and A. J. Ninfa. 2000. Asymmetry in the autophosphorylation of the two-component system transmitter protein NRII (NtrB) of Escherichia coli. Biochemistry 39:5058-5065.
    • (2000) Biochemistry , vol.39 , pp. 5058-5065
    • Jiang, P.1    Ninfa, A.J.2
  • 22
    • 0032530304 scopus 로고    scopus 로고
    • Enzymological characterization of the signal-transducing uridylyltransferase/uiridylyl-removing enzyme (E.C. 2.7.7.59) of Escherichia coli and its interaction with the PII protein
    • Jiang, P, J. Peliska, and A. J. Ninfa. 1998. Enzymological characterization of the signal-transducing uridylyltransferase/uiridylyl-removing enzyme (E.C. 2.7.7.59) of Escherichia coli and its interaction with the PII protein. Biochemistry 37:12782-12794.
    • (1998) Biochemistry , vol.37 , pp. 12782-12794
    • Jiang, P.1    Peliska, J.2    Ninfa, A.J.3
  • 23
    • 0032530305 scopus 로고    scopus 로고
    • Reconstitution of the signal transduction bicyclic cascade responsible for the regulation of Ntr gene transcription in Escherichia coli
    • Jiang, P., J. Peliska, and A. J. Ninfa. 1998. Reconstitution of the signal transduction bicyclic cascade responsible for the regulation of Ntr gene transcription in Escherichia coli. Biochemistry 37:12795-12801.
    • (1998) Biochemistry , vol.37 , pp. 12795-12801
    • Jiang, P.1    Peliska, J.2    Ninfa, A.J.3
  • 24
    • 0030743733 scopus 로고    scopus 로고
    • Structure/function analysis of the PII signal transduction protein of Escherichia coli: Genetic separation of interactions with protein receptors
    • Jiang, P., P. Zucker, M. R. Atkinson, E. S. Kamberov, W. Tirasophon, P. Chandran, B. R. Schefke, and A. J. Ninfa. 1997. Structure/function analysis of the PII signal transduction protein of Escherichia coli: genetic separation of interactions with protein receptors. J. Bacteriol. 179:4342-4353.
    • (1997) J. Bacteriol. , vol.179 , pp. 4342-4353
    • Jiang, P.1    Zucker, P.2    Atkinson, M.R.3    Kamberov, E.S.4    Tirasophon, W.5    Chandran, P.6    Schefke, B.R.7    Ninfa, A.J.8
  • 25
    • 0028113011 scopus 로고
    • Effect of mutations in Escherichia coli glnL (ntrB), encoding nitrogen regulator II (NRII or NtrB), on the phosphatase activity involved in bacterial nitrogen regulation
    • Kamberov, E. S., M. R. Atkinson, P. Chandran, and A. J. Ninfa. 1994. Effect of mutations in Escherichia coli glnL (ntrB), encoding nitrogen regulator II (NRII or NtrB), on the phosphatase activity involved in bacterial nitrogen regulation. J. Biol. Chem. 269:28294-28299.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28294-28299
    • Kamberov, E.S.1    Atkinson, M.R.2    Chandran, P.3    Ninfa, A.J.4
  • 27
    • 0029051027 scopus 로고
    • The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP
    • Kamberov, E. S., M. R. Atkinson, and A. J. Ninfa. 1995. The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP. J. Biol. Chem. 270:17797-17807.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17797-17807
    • Kamberov, E.S.1    Atkinson, M.R.2    Ninfa, A.J.3
  • 28
    • 0024040412 scopus 로고
    • Protein kinase and phosphoprotein phosphatase activities of nitrogen regulatory proteins NTRB and NTRC of enteric bacteria: Roles of conserved amino terminal domain of NTRC
    • Keener, J., and S. Kustu. 1988. Protein kinase and phosphoprotein phosphatase activities of nitrogen regulatory proteins NTRB and NTRC of enteric bacteria: roles of 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
    • 0033582232 scopus 로고    scopus 로고
    • Functional dissection of the transmitter module of the histidine kinase NtrB in Escherichia coli
    • Kramer, G., and V. Weiss. 1999. Functional dissection of the transmitter module of the histidine kinase NtrB in Escherichia coli. Proc. Natl. Acad. Sci. USA 96:604-609.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 604-609
    • Kramer, G.1    Weiss, V.2
  • 31
    • 0028891890 scopus 로고
    • Activation of the dephosphorylation of nitrogen regulator I-phosphate of Escherichia coli
    • Liu, J., and B. Magasanik. 1995. Activation of the dephosphorylation of nitrogen regulator I-phosphate of Escherichia coli. J. Bacteriol. 177:926-931.
    • (1995) J. Bacteriol. , vol.177 , pp. 926-931
    • Liu, J.1    Magasanik, B.2
  • 33
    • 0035798570 scopus 로고    scopus 로고
    • Structural and mutational analysis of the PhoQ histidine kinase catalytic domain: Insight into the reaction mechanism
    • Marina, A., C. Mott, A. Auyzenberg, W. A. Hendrickson, and C. D. Waldburger. 2001. Structural and mutational analysis of the PhoQ histidine kinase catalytic domain: insight into the reaction mechanism. J. Biol. Chem. 276:41182-41190.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41182-41190
    • Marina, A.1    Mott, C.2    Auyzenberg, A.3    Hendrickson, W.A.4    Waldburger, C.D.5
  • 34
    • 0036135534 scopus 로고    scopus 로고
    • Domain Interactions on the ntr signal transduction pathway: Two-hybrid analysis of mutant and truncated derivatives of histidine kinase NtrB
    • Martinez-Argudo, I., P. Salinas, R. Maldonado, and A. Contreras. 2002. Domain Interactions on the ntr signal transduction pathway: two-hybrid analysis of mutant and truncated derivatives of histidine kinase NtrB. J. Bacteriol. 184:200-206.
    • (2002) J. Bacteriol. , vol.184 , pp. 200-206
    • Martinez-Argudo, I.1    Salinas, P.2    Maldonado, R.3    Contreras, A.4
  • 35
    • 0034176532 scopus 로고    scopus 로고
    • PII signal transduction proteins
    • Ninfa, A. J., and M. R. Atkinson. 2000. PII signal transduction proteins. Trends Microbiol. 8:172-179.
    • (2000) Trends Microbiol. , vol.8 , pp. 172-179
    • Ninfa, A.J.1    Atkinson, M.R.2
  • 37
    • 0002207296 scopus 로고
    • The role of NRI phosphate in the activation of transcription from the nitrogen-regulated promoter glnAp2
    • Ninfa, A. J., E. Brodsky, and B. Magasanik. 1989. The role of NRI phosphate in the activation of transcription from the nitrogen-regulated promoter glnAp2. UCLA Symp. Mol. Cell. Biol. 95:43-52.
    • (1989) UCLA Symp. Mol. Cell. Biol. , vol.95 , pp. 43-52
    • Ninfa, A.J.1    Brodsky, E.2    Magasanik, B.3
  • 38
    • 0013069544 scopus 로고    scopus 로고
    • Integration of antagonistic signals in the regulation of bacterial nitrogen assimilation
    • Ninfa, A. J., P. Jiang, M. R. Atkinson, and J. A. Peliska. 2000. Integration of antagonistic signals in the regulation of bacterial nitrogen assimilation. Curr. Top. Cell. Regul. 36:32-76.
    • (2000) Curr. Top. Cell. Regul. , vol.36 , pp. 32-76
    • Ninfa, A.J.1    Jiang, P.2    Atkinson, M.R.3    Peliska, J.A.4
  • 39
    • 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., and B. Magasanik. 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
  • 40
    • 0023665129 scopus 로고
    • Initiation of transcription at the bacterial glnAp2 promoter by purified Escherichia coli components is facilitated by enhancers
    • Ninfa, A. J., L. J. Reitzer, and B. Magasanik. 1987. Initiation of transcription at the bacterial glnAp2 promoter by purified Escherichia coli components is facilitated by enhancers. Cell 50:1039-1046.
    • (1987) Cell , vol.50 , pp. 1039-1046
    • Ninfa, A.J.1    Reitzer, L.J.2    Magasanik, B.3
  • 41
    • 0023036939 scopus 로고
    • Purification of nitrogen regulator II, the product of the glnL gene of Escherichia coli
    • Ninfa, A. J., S. Ueno-Nishio, T. P. Hunt, B. Robustell, and B. Magasanik. 1986. Purification of nitrogen regulator II, the product of the glnL gene of Escherichia coli. J. Bacteriol. 168:1002-1004.
    • (1986) J. Bacteriol. , vol.168 , pp. 1002-1004
    • Ninfa, A.J.1    Ueno-Nishio, S.2    Hunt, T.P.3    Robustell, B.4    Magasanik, B.5
  • 42
    • 0027439298 scopus 로고
    • Mechanism of autophosphorylation of Escherichia coli NRII: Trans-phosphorylation between subunits
    • Ninfa, E. G., M. R. Atkinson, E. S. Kamberov, and A. J. Ninfa. 1993. Mechanism of autophosphorylation of Escherichia coli NRII: trans-phosphorylation between subunits. J. Bacteriol. 175:7024-7032.
    • (1993) J. Bacteriol. , vol.175 , pp. 7024-7032
    • Ninfa, E.G.1    Atkinson, M.R.2    Kamberov, E.S.3    Ninfa, A.J.4
  • 43
    • 0017854557 scopus 로고
    • gltB gene and regulation of nitrogen metabolism by glutamine synthetase in Escherichia coli
    • Pahel, G., A. D. Zelentz, and B. M. Tyler. 1978. gltB gene and regulation of nitrogen metabolism by glutamine synthetase in Escherichia coli. J. Bacteriol. 133:139-148.
    • (1978) J. Bacteriol. , vol.133 , pp. 139-148
    • Pahel, G.1    Zelentz, A.D.2    Tyler, B.M.3
  • 44
    • 0034619512 scopus 로고    scopus 로고
    • The Escherichia coli PII signal transduction protein regulates the activities of the two-component system transmitter protein NRII by direct interaction with the kinase domain of the transmitter module
    • Pioszak, A. A., P. Jiang, and A. J. Ninfa. 2000. The Escherichia coli PII signal transduction protein regulates the activities of the two-component system transmitter protein NRII by direct interaction with the kinase domain of the transmitter module. Biochemistry 39:13450-13461.
    • (2000) Biochemistry , vol.39 , pp. 13450-13461
    • Pioszak, A.A.1    Jiang, P.2    Ninfa, A.J.3
  • 45
    • 0024598928 scopus 로고
    • Function of a bacterial activator protein that binds to transcriptional enhancers
    • Popham, D. L., D. Szeto, J. Keener, and S. Kustu. 1989. Function of a bacterial activator protein that binds to transcriptional enhancers. Science 243:629-635.
    • (1989) Science , vol.243 , pp. 629-635
    • Popham, D.L.1    Szeto, D.2    Keener, J.3    Kustu, S.4
  • 46
    • 0002437098 scopus 로고
    • Amplification of genomic DNA
    • M. A. Innis, D. H., Gelfand, J. J. Sninsky, and T. J. White (ed.). Academic Press, San Diego, Calif.
    • Saiki, R. K. 1990. Amplification of genomic DNA, p. 13-20 In M. A. Innis, D. H., Gelfand, J. J. Sninsky, and T. J. White (ed.), PCR protocols: a guide to methods and applications. Academic Press, San Diego, Calif.
    • (1990) PCR Protocols: A Guide to Methods and Applications , pp. 13-20
    • Saiki, R.K.1
  • 47
    • 0026648034 scopus 로고
    • Phosphorylation site of NtrC, a protein phosphatase whose covalent intermediate activates transcription
    • Sanders, D. A., B. L. Gillece-Castro, A. L. Burlingame, and D. E. Koshland, Jr. 1992. Phosphorylation site of NtrC, a protein phosphatase whose covalent intermediate activates transcription. J. Bacteriol. 174:5117-5122.
    • (1992) J. Bacteriol. , vol.174 , pp. 5117-5122
    • Sanders, D.A.1    Gillece-Castro, B.L.2    Burlingame, A.L.3    Koshland D.E., Jr.4
  • 48
    • 0023254924 scopus 로고
    • Inducible expression vectors incorporating the Escherichia coli atpE translation initiation region
    • Schauder, B., H., Blocker, R., Frank, and E. G. J. McCarthy. 1987. Inducible expression vectors incorporating the Escherichia coli atpE translation initiation region. Gene 52:279-283.
    • (1987) Gene , vol.52 , pp. 279-283
    • Schauder, B.1    Blocker, H.2    Frank, R.3    McCarthy, E.G.J.4
  • 49
    • 0031827017 scopus 로고    scopus 로고
    • Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli
    • Schneider, B. L., A. K. Kiupakis, and L. J. Reitzer. 1998. Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. J. Bacteriol. 180:4278-4286.
    • (1998) J. Bacteriol. , vol.180 , pp. 4278-4286
    • Schneider, B.L.1    Kiupakis, A.K.2    Reitzer, L.J.3
  • 51
    • 0025035371 scopus 로고
    • DNA-looping and enhancer activity: Association between DNA-bound NtrC activator and RNA polymerase at the glnA promoter
    • Su, W., S. Porter, S. Kustu, and H. Echols. 1990. DNA-looping and enhancer activity: association between DNA-bound NtrC activator and RNA polymerase at the glnA promoter. Proc. Natl. Acad. Sci. USA 87:5504-5508.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5504-5508
    • Su, W.1    Porter, S.2    Kustu, S.3    Echols, H.4
  • 53
    • 0024462539 scopus 로고
    • Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate
    • Utsumi, R., R. E. Brisette, 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    Brisette, R.E.2    Rampersaud, A.3    Forst, S.A.4    Oosawa, K.5    Inouye, M.6
  • 55
    • 0345353513 scopus 로고
    • Phosphorylation of nitrogen regulator I (NRI) of Escherichia coli
    • Weiss, V., and B. Magasanik. 1988. Phosphorylation of nitrogen regulator I (NRI) of Escherichia coli. Proc. Natl. Acad. Sci. USA 85:8919-8923.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8919-8923
    • Weiss, V.1    Magasanik, B.2
  • 56
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signaling systems
    • West, A. H., and A. M. Stock. 2001. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 26:369-376.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 369-376
    • West, A.H.1    Stock, A.M.2


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