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Volumn 269, Issue 4, 2003, Pages 574-581

Identification and analysis of Escherichia coli proteins that interact with the histidine kinase NtrB in a yeast two-hybrid system

Author keywords

Aspartase; GlnK; Nitrogen interaction network; NtrB

Indexed keywords

BACTERIAL PROTEIN; NITROGEN; PROTEIN HISTIDINE KINASE;

EID: 0042122506     PISSN: 16174615     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00438-003-0866-7     Document Type: Article
Times cited : (9)

References (40)
  • 1
    • 0032895784 scopus 로고    scopus 로고
    • Characterization of the GlnK protein of Escherichia coli
    • Atkinson MR, Ninfa AJ (1999) Characterization of the GlnK protein of Escherichia coli. Mol Microbiol 32:301-313
    • (1999) Mol Microbiol , vol.32 , pp. 301-313
    • Atkinson, M.R.1    Ninfa, A.J.2
  • 2
    • 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 MR, Blauwkamp TA, Bondarenko V, Studitsky V, Ninfa AJ (2002a) 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
  • 3
    • 0036777892 scopus 로고    scopus 로고
    • Context-dependent functions of the PII and GlnK signal transduction proteins in Escherichia coli
    • Atkinson MR, Blauwkamp TA, Ninfa AJ (2002b) 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
  • 5
    • 0027255909 scopus 로고
    • Elimination of false positives that arise in using the two-hybrid system
    • Bartel P, Chien CT, Sternglanz R, Fields S (1993) Elimination of false positives that arise in using the two-hybrid system. Biotechniques 14:920-924
    • (1993) Biotechniques , vol.14 , pp. 920-924
    • Bartel, P.1    Chien, C.T.2    Sternglanz, R.3    Fields, S.4
  • 6
    • 19044365093 scopus 로고    scopus 로고
    • A glutamine-amidotransferase-like protein modulates FixT anti-kinase activity in Sinorhizobium meliloti
    • Berges H, Checroun C, Guiral S, Garnerone AM, Boistard P, Batut J (2001) A glutamine-amidotransferase-like protein modulates FixT anti-kinase activity in Sinorhizobium meliloti. BMC Microbiol 1:6
    • (2001) BMC Microbiol , vol.1 , pp. 6
    • Berges, H.1    Checroun, C.2    Guiral, S.3    Garnerone, A.M.4    Boistard, P.5    Batut, J.6
  • 7
    • 0025940629 scopus 로고
    • The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest
    • Chien CT, Bartel PL, Sternglanz R, Fields S (1991) The two-hybrid system: a method to identify and clone genes for proteins that interact with a protein of interest. Proc Natl Acad Sci USA 88:9578-9582
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9578-9582
    • Chien, C.T.1    Bartel, P.L.2    Sternglanz, R.3    Fields, S.4
  • 8
    • 0017085802 scopus 로고
    • A colony bank containing synthetic Col El hybrid plasmids representative of the entire E. coli genome
    • Clarke L, Carbon J (1976) A colony bank containing synthetic Col El hybrid plasmids representative of the entire E. coli genome. Cell 9:91-99
    • (1976) Cell , vol.9 , pp. 91-99
    • Clarke, L.1    Carbon, J.2
  • 9
    • 0036580169 scopus 로고    scopus 로고
    • Protein interactions: Two methods for assessment of the reliability of high throughput observations
    • Deane CM, Salwinski L, Xenarios I, Eisenberg D (2002) Protein interactions: two methods for assessment of the reliability of high throughput observations. Mol Cell Proteomics 1:349-356
    • (2002) Mol Cell Proteomics , vol.1 , pp. 349-356
    • Deane, C.M.1    Salwinski, L.2    Xenarios, I.3    Eisenberg, D.4
  • 10
    • 0028178392 scopus 로고
    • Determining the probability of obtaining a desired clone in an amplified or shuttle library
    • Finkel RA, Bent S, Schardl CL (1994) Determining the probability of obtaining a desired clone in an amplified or shuttle library. Biotechniques 16:580-582
    • (1994) Biotechniques , vol.16 , pp. 580-582
    • Finkel, R.A.1    Bent, S.2    Schardl, C.L.3
  • 12
    • 0033527742 scopus 로고    scopus 로고
    • Inhibition of the FixL sensor kinase by the FixT protein in Sinorhizobium meliloti
    • Garnerone AM, Cabanes D, Foussard M, Boistard P, Batut J (1999) Inhibition of the FixL sensor kinase by the FixT protein in Sinorhizobium meliloti. J Biol Chem 274:32500-32506
    • (1999) J Biol Chem , vol.274 , pp. 32500-32506
    • Garnerone, A.M.1    Cabanes, D.2    Foussard, M.3    Boistard, P.4    Batut, J.5
  • 13
    • 0032436622 scopus 로고    scopus 로고
    • Transcriptional regulation and organization of the dcuA and dcuB genes, encoding homologous anaerobic C4-dicarboxylate transporters in Escherichia coli
    • Golby P, Kelly DJ, Guest JR, Andrews SC (1998) Transcriptional regulation and organization of the dcuA and dcuB genes, encoding homologous anaerobic C4-dicarboxylate transporters in Escherichia coli. J Bacteriol 180:6586-65896
    • (1998) J Bacteriol , vol.180 , pp. 6586-65896
    • Golby, P.1    Kelly, D.J.2    Guest, J.R.3    Andrews, S.C.4
  • 15
    • 0000075317 scopus 로고
    • Techniques for transformation of Escherichia coli
    • Glover D (ed). IRL Press, Oxford
    • Hanahan D (1985) Techniques for transformation of Escherichia coli. In: Glover D (ed) DNA cloning (vol 1). IRL Press, Oxford, pp 109-135
    • (1985) DNA Cloning , vol.1 , pp. 109-135
    • Hanahan, D.1
  • 16
    • 0027496935 scopus 로고
    • The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin- dependent kinases
    • Harper JW, Adami GR, Wei N, Keyomarsi K, Elledge SJ (1993) The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin- dependent kinases. Cell 75:805-816
    • (1993) Cell , vol.75 , pp. 805-816
    • Harper, J.W.1    Adami, G.R.2    Wei, N.3    Keyomarsi, K.4    Elledge, S.J.5
  • 17
    • 0034879819 scopus 로고    scopus 로고
    • Keeping signals straight in phosphorelay signal transduction
    • Hoch JA, Varughese KI (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
  • 18
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two- hybrid selection in yeast
    • James P, Halladay J, Craig EA (1996) Genomic libraries and a host strain designed for highly efficient two- hybrid selection in yeast. Genetics 144:1425-1436
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 19
    • 0032994344 scopus 로고    scopus 로고
    • Regulation of autophosphorylation of Escherichia coli nitrogen regulator II by the PII signal transduction protein
    • Jiang P, Ninfa AJ (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
  • 20
    • 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, Peliska JA, Ninfa AJ (1998a) 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.A.2    Ninfa, A.J.3
  • 21
    • 0032530304 scopus 로고    scopus 로고
    • Enzymological characterization of the signal-transducing uridylyltransferase/uridylyl-removing enzyme (EC 2.7.7.59) of Escherichia coli and its interaction with the PII protein
    • Jiang P, Peliska JA, Ninfa AJ (1998b) Enzymological characterization of the signal-transducing uridylyltransferase/uridylyl-removing enzyme (EC 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.A.2    Ninfa, A.J.3
  • 22
    • 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, Atkinson MR, Srisawat C, Sun Q, Ninfa AJ (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
  • 23
    • 0033988715 scopus 로고    scopus 로고
    • A highly representative two-hybrid genomic library for the yeast Yarrowia lipolytica
    • Kabani M, Boisrame A, Beckerich JM, Gaillardin C (2000) A highly representative two-hybrid genomic library for the yeast Yarrowia lipolytica. Gene 241:309-315
    • (2000) Gene , vol.241 , pp. 309-315
    • Kabani, M.1    Boisrame, A.2    Beckerich, J.M.3    Gaillardin, C.4
  • 24
    • 0033733468 scopus 로고    scopus 로고
    • Interaction mating methods in two-hybrid systems
    • Kolonin MG, Zhong J, Finley RL (2000) Interaction mating methods in two-hybrid systems. Methods Enzymol 328:26-46
    • (2000) Methods Enzymol , vol.328 , pp. 26-46
    • Kolonin, M.G.1    Zhong, J.2    Finley, R.L.3
  • 25
    • 0036280134 scopus 로고    scopus 로고
    • PII T-loop mutations affecting signal transduction to NtrB also abolish yeast two-hybrid interactions
    • Martinez-Argudo I, Contreras A (2002) PII T-loop mutations affecting signal transduction to NtrB also abolish yeast two-hybrid interactions. J Bacteriol 184:3746-3748
    • (2002) J Bacteriol , vol.184 , pp. 3746-3748
    • Martinez-Argudo, I.1    Contreras, A.2
  • 27
    • 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, Salinas P, Maldonado R, Contreras A (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
  • 28
    • 0033655445 scopus 로고    scopus 로고
    • Integration of antagonistic signals in the regulation of nitrogen assimilation in Escherichia coli
    • Ninfa AJ, Jiang P, Atkinson MR, Peliska JA (2000) Integration of antagonistic signals in the regulation of nitrogen assimilation in Escherichia coli. Curr Top Cell Regul 36:31-75
    • (2000) Curr Top Cell Regul , vol.36 , pp. 31-75
    • Ninfa, A.J.1    Jiang, P.2    Atkinson, M.R.3    Peliska, J.A.4
  • 29
    • 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 AA, Ninfa AJ (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
  • 30
    • 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 AA, Jiang P, Ninfa AJ (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
  • 31
    • 0030588222 scopus 로고    scopus 로고
    • Refinement of vectors for use in the yeast two-hybrid system
    • Roder KH, Wolf SS, Schweizer M (1996) Refinement of vectors for use in the yeast two-hybrid system. Anal Biochem 241:260-262
    • (1996) Anal Biochem , vol.241 , pp. 260-262
    • Roder, K.H.1    Wolf, S.S.2    Schweizer, M.3
  • 33
    • 0029882332 scopus 로고    scopus 로고
    • An in vitro assay of beta-galactosidase from yeast
    • Schneider S, Buchert M, Hovens CM (1996) An in vitro assay of beta-galactosidase from yeast. Biotechniques 20:960-962
    • (1996) Biotechniques , vol.20 , pp. 960-962
    • Schneider, S.1    Buchert, M.2    Hovens, C.M.3
  • 35
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor BL, Zhulin IB (1999) PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol Mol Biol Rev 63:479-506
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 36
    • 0033658180 scopus 로고    scopus 로고
    • L-aspartase: New tricks from an old enzyme
    • Viola RE (2000) L-aspartase: new tricks from an old enzyme. Adv Enzymol Relat Areas Mol Biol 74:295-341
    • (2000) Adv Enzymol Relat Areas Mol Biol , vol.74 , pp. 295-341
    • Viola, R.E.1
  • 37
    • 0030764211 scopus 로고    scopus 로고
    • A novel histidine kinase inhibitor regulating development in Bacillus subtilis
    • Wang L, Grau R, Perego M, Hoch JA (1997) A novel histidine kinase inhibitor regulating development in Bacillus subtilis. Genes Dev 11:2569-2579
    • (1997) Genes Dev , vol.11 , pp. 2569-2579
    • Wang, L.1    Grau, R.2    Perego, M.3    Hoch, J.A.4
  • 38
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signaling systems
    • West AH, Stock AM (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
  • 39
    • 0024403543 scopus 로고
    • The Q-linker: A class of interdomain sequences found in bacterial multidomain regulatory proteins
    • Wootton JC, Drummond MH (1989) The Q-linker: a class of interdomain sequences found in bacterial multidomain regulatory proteins. Protein Eng 2:535-543
    • (1989) Protein Eng , vol.2 , pp. 535-543
    • Wootton, J.C.1    Drummond, M.H.2
  • 40
    • 0037215715 scopus 로고    scopus 로고
    • Common extra-cellular sensory domains in transmembrane receptors for diverse signal transduction pathways in bacteria and archaea
    • Zhulin IB, Nikolskaya AN, Galperin MY (2003) Common extra-cellular sensory domains in transmembrane receptors for diverse signal transduction pathways in bacteria and archaea. J Bacteriol 185:285-294
    • (2003) J Bacteriol , vol.185 , pp. 285-294
    • Zhulin, I.B.1    Nikolskaya, A.N.2    Galperin, M.Y.3


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