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Volumn 72, Issue 4, 2009, Pages 978-994

Stimulation of the potassium sensor KdpD kinase activity by interaction with the phosphotransferase protein IIANtr in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; PHOSPHATASE; PHOSPHOTRANSFERASE; POTASSIUM; PROTEIN IIANTR; PROTEIN KDPFABC; PROTEIN TYROSINE KINASE A; SENSOR KINASE KDPD; SENSOR KINASE KDPE; UNCLASSIFIED DRUG;

EID: 65549161404     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06704.x     Document Type: Article
Times cited : (95)

References (68)
  • 2
    • 0023568427 scopus 로고
    • Plasmid curing of Escherichia coli and Salmonella typhimurium by treatment with sodium dodecyl sulfate and high temperature incubation
    • Bullock, W.O., Fernandex, J.M. Short, J.M. (1987) Xl1-Blue: a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection. Biotechniques 5 : 376 379. (Pubitemid 18067017)
    • (1987) Revista de Microbiologia , vol.18 , Issue.2 , pp. 178-183
    • Jungmann, D.M.1    De Souza Ferreira, L.C.2
  • 4
    • 0032589264 scopus 로고    scopus 로고
    • 54-dependent Pu promoter of the TOL plasmid
    • Ntr (PtsN) protein of Pseudomonas putida mediates the C source inhibition of the sigma54-dependent Pu promoter of the TOL plasmid. J Biol Chem 274 : 15562 15568. (Pubitemid 129518910)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.22 , pp. 15562-15568
    • Cases, I.1    Perez-Martin, J.2    De Lorenzo, V.3
  • 5
    • 34548548565 scopus 로고    scopus 로고
    • Simultaneous catabolite repression between glucose and toluene metabolism in Pseudomonas putida is channeled through different signaling pathways
    • DOI 10.1128/JB.00679-07
    • del Castillo, T. Ramos, J.L. (2007) Simultaneous catabolite repression between glucose and toluene metabolism in Pseudomonas putida is channeled through different signaling pathways. J Bacteriol 189 : 6602 6610. (Pubitemid 47397366)
    • (2007) Journal of Bacteriology , vol.189 , Issue.18 , pp. 6602-6610
    • Del Castillo, T.1    Ramos, J.L.2
  • 6
    • 47049107952 scopus 로고    scopus 로고
    • Characterization of the nitric oxide-reactive transcriptional activator NorR
    • D'Autreaux, B., Tucker, N., Spiro, S. Dixon, R. (2008) Characterization of the nitric oxide-reactive transcriptional activator NorR. Methods Enzymol 437 : 235 251.
    • (2008) Methods Enzymol , vol.437 , pp. 235-251
    • D'Autreaux, B.1    Tucker, N.2    Spiro, S.3    Dixon, R.4
  • 8
    • 42049092081 scopus 로고    scopus 로고
    • The mechanisms of carbon catabolite repression in bacteria
    • Deutscher, J. (2008) The mechanisms of carbon catabolite repression in bacteria. Curr Opin Microbiol 11 : 87 93.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 87-93
    • Deutscher, J.1
  • 9
    • 0028364161 scopus 로고
    • Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis
    • Deutscher, J., Reizer, J., Fischer, C., Galinier, A., Saier, M.H., Jr, Steinmetz, M. (1994) Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis. J Bacteriol 176 : 3336 3344. (Pubitemid 24166726)
    • (1994) Journal of Bacteriology , vol.176 , Issue.11 , pp. 3336-3344
    • Deutscher, J.1    Reizer, J.2    Fischer, C.3    Galinier, A.4    Saier Jr., M.H.5    Steinmetz, M.6
  • 10
    • 33845626641 scopus 로고    scopus 로고
    • How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria
    • Deutscher, J., Francke, C. Postma, P.W. (2006) How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria. Microbiol Mol Biol Rev 70 : 939 1031.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 939-1031
    • Deutscher, J.1    Francke, C.2    Postma, P.W.3
  • 11
    • 33644686444 scopus 로고    scopus 로고
    • A structural perspective on enzymes activated by monovalent cations
    • DOI 10.1074/jbc.R500023200
    • Di Cera, E. (2006) A structural perspective on enzymes activated by monovalent cations. J Biol Chem 281 : 1305 1308. (Pubitemid 43752441)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.3 , pp. 1305-1308
    • Di Cera, E.1
  • 12
    • 0026769761 scopus 로고
    • New cloning vectors for integration in the lambda attachment site attB of the Escherichia coli chromosome
    • Diederich, L., Rasmussen, L.J. Messer, W. (1992) New cloning vectors for integration in the lambda attachment site attB of the Escherichia coli chromosome. Plasmid 28 : 14 24.
    • (1992) Plasmid , vol.28 , pp. 14-24
    • Diederich, L.1    Rasmussen, L.J.2    Messer, W.3
  • 14
    • 0015155178 scopus 로고
    • Potassium transport loci in Escherichia coli K-12
    • Epstein, W. Kim, B.S. (1971) Potassium transport loci in Escherichia coli K-12. J Bacteriol 108 : 639 644.
    • (1971) J Bacteriol , vol.108 , pp. 639-644
    • Epstein, W.1    Kim, B.S.2
  • 16
    • 0342546514 scopus 로고    scopus 로고
    • +-translocating Kdp complex of Escherichia coli and is responsible for stabilization of the complex in vitro
    • DOI 10.1074/jbc.274.53.37901
    • Gassel, M., Möllenkamp, T., Puppe, W. Altendorf, K. (1999) The KdpF subunit is part of the K(+)-translocating Kdp complex of Escherichia coli and is responsible for stabilization of the complex in vitro. J Biol Chem 274 : 37901 37907. (Pubitemid 30026857)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.53 , pp. 37901-37907
    • Gassel, M.1    Mollenkamp, T.2    Puppe, W.3    Altendorf, K.4
  • 17
    • 0345299162 scopus 로고    scopus 로고
    • Catabolite control of Escherichia coli regulatory protein BglG activity by antagonistically acting phosphorylations
    • DOI 10.1093/emboj/18.12.3370
    • Görke, B. Rak, B. (1999) Catabolite control of Escherichia coli regulatory protein BglG activity by antagonistically acting phosphorylations. EMBO J 18 : 3370 3379. (Pubitemid 29276583)
    • (1999) EMBO Journal , vol.18 , Issue.12 , pp. 3370-3379
    • Gorke, B.1    Rak, B.2
  • 18
    • 47549110972 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria: Many ways to make the most out of nutrients
    • Görke, B. Stülke, J. (2008) Carbon catabolite repression in bacteria: many ways to make the most out of nutrients. Nat Rev Microbiol 6 : 613 624.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 613-624
    • Görke, B.1    Stülke, J.2
  • 19
    • 36448997409 scopus 로고    scopus 로고
    • Computational methods in noncoding RNA research
    • DOI 10.1007/s00285-007-0122-6, RNA: Advances in algorithms and mathematics related to the structural biology of RNA
    • Görke, B. Vogel, J. (2008) Noncoding RNA control of the making and breaking of sugars. Genes Dev 22 : 2914 2925. (Pubitemid 50004866)
    • (2008) Journal of Mathematical Biology , vol.56 , Issue.1-2 , pp. 15-49
    • MacHado-Lima, A.1    Del Portillo, H.A.2    Durham, A.M.3
  • 22
    • 45249100907 scopus 로고    scopus 로고
    • The extracytoplasmic stress factor, sigma E, is required to maintain cell envelope integrity in Escherichia coli
    • Hayden, J.D. Ades, S.E. (2008) The extracytoplasmic stress factor, sigma E, is required to maintain cell envelope integrity in Escherichia coli. PLoS ONE 3 : e1573.
    • (2008) PLoS ONE , vol.3
    • Hayden, J.D.1    Ades, S.E.2
  • 23
    • 0034595636 scopus 로고    scopus 로고
    • The hydrophilic N-terminal domain complements the membrane-anchored C- terminal domain of the sensor kinase KdpD of Escherichia coli
    • DOI 10.1074/jbc.M000093200
    • Heermann, R., Altendorf, K. Jung, K. (2000) The hydrophilic N-terminal domain complements the membrane-anchored C-terminal domain of the sensor kinase KdpD of Escherichia coli. J Biol Chem 275 : 17080 17085. (Pubitemid 30398951)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 17080-17085
    • Heermann, R.1    Altendorf, K.2    Jung, K.3
  • 24
    • 0345803937 scopus 로고    scopus 로고
    • The N-terminal Input Domain of the Sensor Kinase KdpD of Escherichia coli Stabilizes the Interaction between the Cognate Response Regulator KdpE and the Corresponding DNA-binding Site
    • DOI 10.1074/jbc.M303801200
    • Heermann, R., Altendorf, K. Jung, K. (2003) The N-terminal input domain of the sensor kinase KdpD of Escherichia coli stabilizes the interaction between the cognate response regulator KdpE and the corresponding DNA-binding site. J Biol Chem 278 : 51277 51284. (Pubitemid 38020365)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.51 , pp. 51277-51284
    • Heermann, R.1    Altendorf, K.2    Jung, K.3
  • 25
    • 58549117080 scopus 로고    scopus 로고
    • The universal stress protein UspC scaffolds the KdpD/KdpE signaling cascade of Escherichia coli under salt stress
    • Heermann, R., Weber, A., Mayer, B., Ott, M., Hauser, E., Gabriel, G., et al. (2009) The universal stress protein UspC scaffolds the KdpD/KdpE signaling cascade of Escherichia coli under salt stress. J Mol Biol 386 : 134 148.
    • (2009) J Mol Biol , vol.386 , pp. 134-148
    • Heermann, R.1    Weber, A.2    Mayer, B.3    Ott, M.4    Hauser, E.5    Gabriel, G.6
  • 27
    • 16844377790 scopus 로고    scopus 로고
    • GAF domains: Cyclic nucleotides come full circle
    • Hurley, J.H. (2003) GAF domains: cyclic nucleotides come full circle. Sci STKE 2003 : PE1.
    • (2003) Sci STKE , vol.2003
    • Hurley, J.H.1
  • 28
    • 0032504256 scopus 로고    scopus 로고
    • Truncation of amino acids 12-128 causes deregulation of the phosphatase activity of the sensor kinase KdpD of escherichia coli
    • DOI 10.1074/jbc.273.28.17406
    • Jung, K. Altendorf, K. (1998a) Truncation of amino acids 12-128 causes deregulation of the phosphatase activity of the sensor kinase KdpD of Escherichia coli. J Biol Chem 273 : 17406 17410. (Pubitemid 28355068)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.28 , pp. 17406-17410
    • Jung, K.1    Altendorf, K.2
  • 29
    • 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
    • DOI 10.1074/jbc.273.41.26415
    • Jung, K. Altendorf, K. (1998b) 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. (Pubitemid 28471647)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.41 , pp. 26415-26420
    • Jung, K.1    Altendorf, K.2
  • 30
    • 0030935385 scopus 로고    scopus 로고
    • Purification, reconstitution, and characterization of KdpD, the turgor sensor of Escherichia coli
    • DOI 10.1074/jbc.272.16.10847
    • Jung, K., Tjaden, B. Altendorf, K. (1997) Purification, reconstitution, and characterization of KdpD, the turgor sensor of Escherichia coli. J Biol Chem 272 : 10847 10852. (Pubitemid 27181101)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.16 , pp. 10847-10852
    • Jung, K.1    Tjaden, B.2    Altendorf, K.3
  • 31
    • 0034704146 scopus 로고    scopus 로고
    • + and ionic strength directly influence the autophosphorylation activity of the putative turgor sensor KdpD of Escherichia coli
    • DOI 10.1074/jbc.M008917200
    • + and ionic strength directly influence the autophosphorylation activity of the putative turgor sensor KdpD of Escherichia coli. J Biol Chem 275 : 40142 40147. (Pubitemid 32064641)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.51 , pp. 40142-40147
    • Jung, K.1    Veen, M.2    Altendorf, K.3
  • 32
    • 34548317154 scopus 로고    scopus 로고
    • Feedback control of glucosamine-6-phosphate synthase GlmS expression depends on the small RNA GlmZ and involves the novel protein YhbJ in Escherichia coli
    • DOI 10.1111/j.1365-2958.2007.05888.x
    • Kalamorz, F., Reichenbach, B., März, W., Rak, B. Görke, B. (2007) Feedback control of glucosamine-6-phosphate synthase GlmS expression depends on the small RNA GlmZ and involves the novel protein YhbJ in Escherichia coli. Mol Microbiol 65 : 1518 1533. (Pubitemid 47347835)
    • (2007) Molecular Microbiology , vol.65 , Issue.6 , pp. 1518-1533
    • Kalamorz, F.1    Reichenbach, B.2    Marz, W.3    Rak, B.4    Gorke, B.5
  • 35
    • 0035151432 scopus 로고    scopus 로고
    • Protein-protein interaction between Bacillus stearothermophilus tyrosyl-tRNA synthetase subdomains revealed by a bacterial two-hybrid system
    • Karimova, G., Ullmann, A. Ladant, D. (2001) Protein-protein interaction between Bacillus stearothermophilus tyrosyl-tRNA synthetase subdomains revealed by a bacterial two-hybrid system. J Mol Microbiol Biotechnol 3 : 73 82. (Pubitemid 32094171)
    • (2001) Journal of Molecular Microbiology and Biotechnology , vol.3 , Issue.1 , pp. 73-82
    • Karimova, G.1    Ullmann, A.2    Ladant, D.3
  • 36
    • 0025841773 scopus 로고
    • Uses of transposons with emphasis on Tn10
    • Kleckner, N., Bender, J. Gottesman, S. (1991) Uses of transposons with emphasis on Tn10. Methods Enzymol 204 : 139 180.
    • (1991) Methods Enzymol , vol.204 , pp. 139-180
    • Kleckner, N.1    Bender, J.2    Gottesman, S.3
  • 37
    • 0027246260 scopus 로고
    • ATP-driven potassium transport in right-side-out membrane vesicles via the Kdp system of Escherichia coli
    • DOI 10.1016/0005-2728(93)90216-3
    • Kollmann, R. Altendorf, K. (1993) ATP-driven potassium transport in right-side-out membrane vesicles via the Kdp system of Escherichia coli. Biochim Biophys Acta 1143 : 62 66. (Pubitemid 23170338)
    • (1993) Biochimica et Biophysica Acta - Bioenergetics , vol.1143 , Issue.1 , pp. 62-66
    • Kollmann, R.1    Altendorf, K.2
  • 40
    • 0017359705 scopus 로고
    • EK2 derivatives of bacteriophage lambda useful in the cloning of DNA from higher organisms: The λgtWES system
    • Leder, P., Tiemeier, D. Enquist, L. (1977) EK2 derivatives of bacteriophage lambda useful in the cloning of DNA from higher organisms: the lambdagtWES system. Science 196 : 175 177. (Pubitemid 8067681)
    • (1977) Science , vol.196 , Issue.4286 , pp. 175-177
    • Leder, P.1    Tiemeier, D.2    Enquist, L.3
  • 42
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY. Cold Spring Harbor Laboratory Press.
    • Miller, J. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, NY : Cold Spring Harbor Laboratory Press.
    • (1972) Experiments in Molecular Genetics.
    • Miller, J.1
  • 43
    • 53549100745 scopus 로고    scopus 로고
    • Signal integration in bacterial two-component regulatory systems
    • Mitrophanov, A.Y. Groisman, E.A. (2008) Signal integration in bacterial two-component regulatory systems. Genes Dev 22 : 2601 2611.
    • (2008) Genes Dev , vol.22 , pp. 2601-2611
    • Mitrophanov, A.Y.1    Groisman, E.A.2
  • 44
    • 0031732150 scopus 로고    scopus 로고
    • The functional importance of structural differences between the mannitol-specific IIA(mannitol) and the regulatory IIA(nitrogen)
    • nitrogen. Protein Sci 7 : 2210 2216. (Pubitemid 28495809)
    • (1998) Protein Science , vol.7 , Issue.10 , pp. 2210-2216
    • Van Montfort, R.L.M.1    Dijkstra, B.W.2
  • 46
    • 0026643223 scopus 로고
    • Phosphotransfer signal transduction between two regulatory factors involved in the osmoregulated kdp operon in Escherichia coli
    • Nakashima, K., Sugiura, A., Momoi, H. Mizuno, T. (1992) Phosphotransfer signal transduction between two regulatory factors involved in the osmoregulated kdp operon in Escherichia coli. Mol Microbiol 6 : 1777 1784.
    • (1992) Mol Microbiol , vol.6 , pp. 1777-1784
    • Nakashima, K.1    Sugiura, A.2    Momoi, H.3    Mizuno, T.4
  • 47
    • 0027454334 scopus 로고
    • Functional reconstitution of the putative Escherichia coli osmosensor, KdpD, into liposomes
    • Nakashima, K., Sugiura, A. Mizuno, T. (1993) Functional reconstitution of the putative Escherichia coli osmosensor, KdpD, into liposomes. J Biochem 114 : 615 621. (Pubitemid 23311493)
    • (1993) Journal of Biochemistry , vol.114 , Issue.4 , pp. 615-621
    • Nakashima, K.1    Sugiura, A.2    Mizuno, T.3
  • 49
    • 0023656666 scopus 로고
    • An immediate and steep increase in ATP concentration in response to reduced turgor pressure in Escherichia coli B
    • Ohwada, T. Sagisaka, S. (1987) An immediate and steep increase in ATP concentration in response to reduced turgor pressure in Escherichia coli B. Arch Biochem Biophys 259 : 157 163.
    • (1987) Arch Biochem Biophys , vol.259 , pp. 157-163
    • Ohwada, T.1    Sagisaka, S.2
  • 50
    • 33745299907 scopus 로고    scopus 로고
    • + in enzyme function
    • DOI 10.1152/physrev.00008.2006
    • + in enzyme function. Physiol Rev 86 : 1049 1092. (Pubitemid 44521648)
    • (2006) Physiological Reviews , vol.86 , Issue.4 , pp. 1049-1092
    • Page, M.J.1    Di Cera, E.2
  • 51
    • 42549106523 scopus 로고    scopus 로고
    • Evidence of in vivo cross talk between the nitrogen-related and fructose-related branches of the carbohydrate phosphotransferase system of Pseudomonas putida
    • Pflüger, K. de Lorenzo, V. (2008) Evidence of in vivo cross talk between the nitrogen-related and fructose-related branches of the carbohydrate phosphotransferase system of Pseudomonas putida. J Bacteriol 190 : 3374 3380.
    • (2008) J Bacteriol , vol.190 , pp. 3374-3380
    • Pflüger, K.1    De Lorenzo, V.2
  • 54
    • 0033543658 scopus 로고    scopus 로고
    • Ntr from Escherichia coli: A novel enzyme of the phosphoenolpyruvate-dependent phosphotransferase system exhibiting strict specificity for its phosphoryl acceptor, NPr
    • Ntr from Escherichia coli. A novel enzyme of the phosphoenolpyruvate- dependent phosphotransferase system exhibiting strict specificity for its phosphoryl acceptor, NPr. J Biol Chem 274 : 26185 26191. (Pubitemid 129520046)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.37 , pp. 26185-26191
    • Rabus, R.1    Reizer, J.2    Paulsen, I.3    Saier Jr., M.H.4
  • 55
    • 0030605252 scopus 로고    scopus 로고
    • Novel phosphotransferase-encoding genes revealed by analysis of the Escherichia coli genome: A chimeric gene encoding an Enzyme i homologue that possesses a putative sensory transduction domain
    • DOI 10.1016/S0378-1119(96)00481-7, PII S0378111996004817
    • Reizer, J., Reizer, A., Merrick, M.J., Plunkett, G., 3rd, Rose, D.J. Saier, M.H., Jr (1996) Novel phosphotransferase-encoding genes revealed by analysis of the Escherichia coli genome: a chimeric gene encoding an Enzyme I homologue that possesses a putative sensory transduction domain. Gene 181 : 103 108. (Pubitemid 26418254)
    • (1996) Gene , vol.181 , Issue.1-2 , pp. 103-108
    • Reizer, J.1    Reizer, A.2    Merrick, M.J.3    Plunkett Iii, G.4    Rose, D.J.5    Saier Jr., M.H.6
  • 57
    • 0035191622 scopus 로고    scopus 로고
    • Trans-acting mutations in loci other than kdpDE that affect kdp operon regulation in Escherichia coli: Effects of cytoplasmic thiol oxidation status and nucleoid protein H-NS on kdp expression
    • DOI 10.1128/JB.183.1.86-93.2001
    • Sardesai, A.A. Gowrishankar, J. (2001) trans-acting mutations in loci other than kdpDE that affect kdp operon regulation in Escherichia coli: effects of cytoplasmic thiol oxidation status and nucleoid protein H-NS on kdp expression. J Bacteriol 183 : 86 93. (Pubitemid 32003111)
    • (2001) Journal of Bacteriology , vol.183 , Issue.1 , pp. 86-93
    • Sardesai, A.A.1    Gowrishankar, J.2
  • 58
    • 0002021273 scopus 로고    scopus 로고
    • Transport of inorganic cations
    • In. Neidhardt, F.C. Curtiss, R., III. Ingraham, J.L. Lin, C.C. Brooks, L.K. Magasanik, B. eds. Washington, DC. American Society for Microbiology Press.
    • Silver, S. (1996) Transport of inorganic cations. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology. Neidhardt, F.C., Curtiss, R., III., Ingraham, J.L., Lin, C.C., Brooks, L.K. Magasanik, B., eds. Washington, DC : American Society for Microbiology Press.
    • (1996) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology.
    • Silver, S.1
  • 59
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F.W. Moffatt, B.A. (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189 : 113 130.
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 60
    • 0026770506 scopus 로고
    • Clarification of the structural and functional features of the osmoregulated kdp operon of Escherichia coli
    • Sugiura, A., Nakashima, K., Tanaka, K. Mizuno, T. (1992) Clarification of the structural and functional features of the osmoregulated kdp operon of Escherichia coli. Mol Microbiol 6 : 1769 1776.
    • (1992) Mol Microbiol , vol.6 , pp. 1769-1776
    • Sugiura, A.1    Nakashima, K.2    Tanaka, K.3    Mizuno, T.4
  • 61
    • 34250334306 scopus 로고    scopus 로고
    • The phosphotransferase system formed by PtsP, PtsO, and PtsN proteins controls production of polyhydroxyalkanoates in Pseudomonas putida
    • DOI 10.1128/JB.00033-07
    • Velazquez, F., Pflüger, K., Cases, I., De Eugenio, L.I. de Lorenzo, V. (2007) The phosphotransferase system formed by PtsP, PtsO, and PtsN proteins controls production of polyhydroxyalkanoates in Pseudomonas putida. J Bacteriol 189 : 4529 4533. (Pubitemid 46919641)
    • (2007) Journal of Bacteriology , vol.189 , Issue.12 , pp. 4529-4533
    • Velazquez, F.1    Pfluger, K.2    Cases, I.3    De Eugenio, L.I.4    De Lorenzo, V.5
  • 62
    • 0026544871 scopus 로고
    • KdpD and KdpE, proteins that control expression of the kdpABC operon, are members of the two-component sensor-effector class of regulators
    • Walderhaug, M.O., Polarek, J.W., Voelkner, P., Daniel, J.M., Hesse, J.E., Altendorf, K. Epstein, W. (1992) KdpD and KdpE, proteins that control expression of the kdpABC operon, are members of the two-component sensor-effector class of regulators. J Bacteriol 174 : 2152 2159.
    • (1992) J Bacteriol , vol.174 , pp. 2152-2159
    • Walderhaug, M.O.1    Polarek, J.W.2    Voelkner, P.3    Daniel, J.M.4    Hesse, J.E.5    Altendorf, K.6    Epstein, W.7
  • 63
    • 0018701477 scopus 로고
    • High-frequency generalised transduction by bacteriophage T4
    • DOI 10.1038/280080a0
    • Wilson, G.G., Young, K.Y., Edlin, G.J. Konigsberg, W. (1979) High-frequency generalised transduction by bacteriophage T4. Nature 280 : 80 82. (Pubitemid 10231991)
    • (1979) Nature , vol.280 , Issue.5717 , pp. 80-82
    • Wilson, G.G.1    Young, K.K.Y.2    Edlin, G.J.3    Konigsberg, W.4
  • 65
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • DOI 10.1016/0378-1119(85)90120-9
    • 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. (Pubitemid 15122816)
    • (1985) Gene , vol.33 , Issue.1 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 67
    • 35048885741 scopus 로고    scopus 로고
    • The extension of the fourth transmembrane helix of the sensor kinase KdpD of Escherichia coli is involved in sensing
    • DOI 10.1128/JB.00976-07
    • Zimmann, P., Steinbrügge, A., Schniederberend, M., Jung, K. Altendorf, K. (2007) The extension of the fourth transmembrane helix of the sensor kinase KdpD of Escherichia coli is involved in sensing. J Bacteriol 189 : 7326 7334. (Pubitemid 47557347)
    • (2007) Journal of Bacteriology , vol.189 , Issue.20 , pp. 7326-7334
    • Zimmann, P.1    Steinbrugge, A.2    Schniederberend, M.3    Jung, K.4    Altendorf, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.