메뉴 건너뛰기




Volumn 34, Issue 5, 1999, Pages 915-925

Activation of CheY mutant D57N by phosphorylation at an alternative site, Ser-56

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ASPARAGINE; ASPARTIC ACID; BACTERIAL PROTEIN; MUTANT PROTEIN; PHOSPHOPEPTIDE; REGULATOR PROTEIN; SERINE;

EID: 0033458903     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01653.x     Document Type: Article
Times cited : (27)

References (53)
  • 2
    • 0032456891 scopus 로고    scopus 로고
    • Proposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator active-site quintet
    • Appleby, J.L., and Bourret, R.B. (1998) Proposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator active-site quintet. J Bacteriol 180: 3563-3569.
    • (1998) J Bacteriol , vol.180 , pp. 3563-3569
    • Appleby, J.L.1    Bourret, R.B.2
  • 3
    • 0028014538 scopus 로고
    • Phosphorylation-dependent binding of the chemotaxis signal molecule CheY to its phosphatase CheZ
    • Blat, Y., and Eisenbach, M. (1994) Phosphorylation-dependent binding of the chemotaxis signal molecule CheY to its phosphatase CheZ. Biochemistry 33: 902-906.
    • (1994) Biochemistry , vol.33 , pp. 902-906
    • Blat, Y.1    Eisenbach, M.2
  • 4
    • 0025021988 scopus 로고
    • Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY
    • Bourret, R.B., Hess, J.F., and Simon, M.I. (1990) Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY. Proc Natl Acad Sci USA 87: 41-45.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 41-45
    • Bourret, R.B.1    Hess, J.F.2    Simon, M.I.3
  • 6
    • 0027231876 scopus 로고
    • Computer simulation of the phosphorylation cascade controlling bacterial chemotaxis
    • Bray, D., Bourret, R.B., and Simon, M.I. (1993) Computer simulation of the phosphorylation cascade controlling bacterial chemotaxis. Mol Biol Cell 4: 469-482.
    • (1993) Mol Biol Cell , vol.4 , pp. 469-482
    • Bray, D.1    Bourret, R.B.2    Simon, M.I.3
  • 7
    • 0031454154 scopus 로고    scopus 로고
    • Phytochrome: If it looks and smells like a histidine kinase, is it a histidine kinase?
    • Chory, J., and Elich, T.D. (1997) Phytochrome: if it looks and smells like a histidine kinase, is it a histidine kinase? Cell 91: 713-716.
    • (1997) Cell , vol.91 , pp. 713-716
    • Chory, J.1    Elich, T.D.2
  • 8
    • 0026773209 scopus 로고
    • Structure and mechanism of alkaline phosphatase
    • Coleman, J.E. (1992) Structure and mechanism of alkaline phosphatase. Annu Rev Biophys Biomol Struct 21: 441-483.
    • (1992) Annu Rev Biophys Biomol Struct , vol.21 , pp. 441-483
    • Coleman, J.E.1
  • 9
    • 0025909522 scopus 로고
    • Mutational analysis of the Bacillus subtilis DegU regulator and its phosphorylation by the DegS protein kinase
    • Dahl, M.K., Msadek, T., Kunst, F., and Rapoport, G. (1991) Mutational analysis of the Bacillus subtilis DegU regulator and its phosphorylation by the DegS protein kinase. J Bacteriol 173: 2539-2547.
    • (1991) J Bacteriol , vol.173 , pp. 2539-2547
    • Dahl, M.K.1    Msadek, T.2    Kunst, F.3    Rapoport, G.4
  • 10
    • 0031020834 scopus 로고    scopus 로고
    • Protein phosphorylation affects binding of the Escherichia coli transcription activator UhpA to the UhpT promoter
    • Dahl, J.L., Wei, B.Y., and Kadner, R.J. (1997) Protein phosphorylation affects binding of the Escherichia coli transcription activator UhpA to the uhpT promoter. J Biol Chem 272: 1910-1919.
    • (1997) J Biol Chem , vol.272 , pp. 1910-1919
    • Dahl, J.L.1    Wei, B.Y.2    Kadner, R.J.3
  • 11
    • 0025799544 scopus 로고
    • Mutational analysis of nitrate regulatory gene narl in Escherichia coli K-12
    • Egan, S.M., and 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
  • 12
    • 0021117878 scopus 로고
    • Techniques in the detection and characterization of phosphoramidate-containing proteins
    • Fujitaki, J.M., and Smith, R.A. (1984) Techniques in the detection and characterization of phosphoramidate-containing proteins. Methods Enzymol 107: 23-36.
    • (1984) Methods Enzymol , vol.107 , pp. 23-36
    • Fujitaki, J.M.1    Smith, R.A.2
  • 13
    • 0029150733 scopus 로고
    • Uncoupled phosphorylation and activation in bacterial chemotaxis: The 2.1-Å structure of a threonine to isoleucine mutant at position 87 of CheY
    • Ganguli, S., Wang, H., Matsumura, P., and Volz, K. (1995) Uncoupled phosphorylation and activation in bacterial chemotaxis: the 2.1-Å structure of a threonine to isoleucine mutant at position 87 of CheY. J Biol Chem 270: 17386-17393.
    • (1995) J Biol Chem , vol.270 , pp. 17386-17393
    • Ganguli, S.1    Wang, H.2    Matsumura, P.3    Volz, K.4
  • 15
    • 0026341931 scopus 로고
    • A genetic analysis of Spo0A structure and function
    • Green, B.D., Olmedo, G., and Youngman, P. (1991) A genetic analysis of Spo0A structure and function. Res Microbiol 142: 825-830.
    • (1991) Res Microbiol , vol.142 , pp. 825-830
    • Green, B.D.1    Olmedo, G.2    Youngman, P.3
  • 16
    • 0032578435 scopus 로고    scopus 로고
    • Synthesis and biochemical characterization of an analogue of CheY-phosphate, a signal transduction protein in bacterial chemotaxis
    • Halkides, C.J., Zhu, X., Phillion, D.P., Matsumura, P., and Dahlquist, F.W. (1998) Synthesis and biochemical characterization of an analogue of CheY-phosphate, a signal transduction protein in bacterial chemotaxis. Biochemistry 37: 13674-13680.
    • (1998) Biochemistry , vol.37 , pp. 13674-13680
    • Halkides, C.J.1    Zhu, X.2    Phillion, D.P.3    Matsumura, P.4    Dahlquist, F.W.5
  • 17
    • 0030769818 scopus 로고    scopus 로고
    • Studies on the regulation of the mitochondrial α-ketoacid dehydrogenase complexes and their kinases
    • Harris, R.A., Hawes, J.W., Popov, K.M., Zhao, Y., Shimomura, Y., Sato, J., et al. (1997) Studies on the regulation of the mitochondrial α-ketoacid dehydrogenase complexes and their kinases. Adv Enzyme Regul 37: 271-293.
    • (1997) Adv Enzyme Regul , vol.37 , pp. 271-293
    • Harris, R.A.1    Hawes, J.W.2    Popov, K.M.3    Zhao, Y.4    Shimomura, Y.5    Sato, J.6
  • 18
    • 0026345261 scopus 로고
    • Phosphorylation assays for proteins of the two-component regulatory system controlling chemotaxis in Escherichia coli
    • Hess, J.F., Bourret, R.B., and Simon, M.I. (1991) Phosphorylation assays for proteins of the two-component regulatory system controlling chemotaxis in Escherichia coli. Methods Enzymol 200: 188-204.
    • (1991) Methods Enzymol , vol.200 , pp. 188-204
    • Hess, J.F.1    Bourret, R.B.2    Simon, M.I.3
  • 19
    • 0025033903 scopus 로고
    • Phosphorylation of the VirG protein of agrobacterium tumefaciens by the autophosphorylated vira protein: Essential role in biological activity of virg
    • Jin, S., Prusti, R.K., Roitsch, T., Ankenbauer, R.G., and Nester, E.W. (1990) Phosphorylation of the VirG protein of Agrobacterium tumefaciens by the autophosphorylated VirA protein: essential role in biological activity of VirG. J Bacteriol 172: 4945-4950.
    • (1990) J Bacteriol , vol.172 , pp. 4945-4950
    • Jin, S.1    Prusti, R.K.2    Roitsch, T.3    Ankenbauer, R.G.4    Nester, E.W.5
  • 20
    • 33947463386 scopus 로고
    • Effect of catalysts on the hydrolysis of acetyl phosphate: Nucleophilic displacement mechanisms in enzymatic reactions
    • Koshland, Jr, D.E. (1952) Effect of catalysts on the hydrolysis of acetyl phosphate: nucleophilic displacement mechanisms in enzymatic reactions. J Am Chem Soc 74: 2286-2292.
    • (1952) J Am Chem Soc , vol.74 , pp. 2286-2292
    • Koshland D.E., Jr.1
  • 21
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., Roberts, J.D., and Zakour, R. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol 154: 367-382.
    • (1987) Methods Enzymol , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.3
  • 22
    • 0016345728 scopus 로고
    • Change in direction of flagellar rotation is the basis of the chemotactic response in Escherichia coli
    • Larsen, S.H., Reader, R.W., Kort, E.N., Tso, W.-W., and Adler, J. (1974) Change in direction of flagellar rotation is the basis of the chemotactic response in Escherichia coli. Nature 249: 74-77.
    • (1974) Nature , vol.249 , pp. 74-77
    • Larsen, S.H.1    Reader, R.W.2    Kort, E.N.3    Tso, W.-W.4    Adler, J.5
  • 23
    • 0024316868 scopus 로고
    • Role of chew protein in coupling membrane receptors to the intracellular signaling system of bacterial chemotaxis
    • Liu, J.D., and Parkinson, J.S. (1989) Role of CheW protein in coupling membrane receptors to the intracellular signaling system of bacterial chemotaxis. Proc Natl Acad Sci USA 86: 8703-8707.
    • (1989) Proc Natl Acad Sci Usa , vol.86 , pp. 8703-8707
    • Liu, J.D.1    Parkinson, J.S.2
  • 24
    • 0030902120 scopus 로고    scopus 로고
    • NodV and nodW, a second flavonoid recognition system regulating nod gene expression in Bradyrhizobium japonicum
    • Loh, J., Garcia, M., and Stacey, G. (1997) NodV and NodW, a second flavonoid recognition system regulating nod gene expression in Bradyrhizobium japonicum. J Bacteriol 179: 3013-3020.
    • (1997) J Bacteriol , vol.179 , pp. 3013-3020
    • Loh, J.1    Garcia, M.2    Stacey, G.3
  • 25
    • 0025881094 scopus 로고
    • Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis
    • Lukat, G.S., Lee, B.H., Mottonen, J.M., Stock, A.M., and Stock, J.B. (1991) Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis. J Biol Chem 266: 8348-8354.
    • (1991) J Biol Chem , vol.266 , pp. 8348-8354
    • Lukat, G.S.1    Lee, B.H.2    Mottonen, J.M.3    Stock, A.M.4    Stock, J.B.5
  • 26
    • 0026512864 scopus 로고
    • Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors
    • Lukat, G.S., McCleary, W.R., Stock, A.M., and Stock, J.B. (1992) Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors. 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
  • 27
    • 0033603635 scopus 로고    scopus 로고
    • Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein flim
    • McEvoy, M.M., Bren, A., Eisenbach, M., and Dahlquist, F.W. (1999) Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein FliM. J Mol Biol 289: 1423-1433.
    • (1999) J Mol Biol , vol.289 , pp. 1423-1433
    • McEvoy, M.M.1    Bren, A.2    Eisenbach, M.3    Dahlquist, F.W.4
  • 28
    • 0026015290 scopus 로고
    • Determination and location of phosphoserine in proteins and peptides by conversion to S-ethylcysteine
    • Meyer, H.E., Hoffmann-Posorske, E., and Heilmeyer, Jr, L.M.G. (1991) Determination and location of phosphoserine in proteins and peptides by conversion to S-ethylcysteine. Methods Enzymol 201: 169-185.
    • (1991) Methods Enzymol , vol.201 , pp. 169-185
    • Meyer, H.E.1    Hoffmann-Posorske, E.2    Heilmeyer L.M.G., Jr.3
  • 29
    • 0027328345 scopus 로고
    • F, the first compartment-specific transcription factor of B. subtilis, is regulated by an anti-σ factor that is also a protein kinase
    • F, the first compartment-specific transcription factor of B. subtilis, is regulated by an anti-σ factor that is also a protein kinase. Cell 74: 735-742.
    • (1993) Cell , vol.74 , pp. 735-742
    • Min, K.T.1    Hilditch, C.M.2    Diederich, B.3    Errington, J.4    Yudkin, M.D.5
  • 30
  • 31
    • 0027262522 scopus 로고
    • Alterations of highly conserved residues in the regulatory domain of nitrogen regulator I (NtrC) of Escherichia coli
    • Moore, J.B., Shiau, S.P., and Reitzer, L.J. (1993) Alterations of highly conserved residues in the regulatory domain of nitrogen regulator I (NtrC) of Escherichia coli. J Bacteriol 175: 2692-2701.
    • (1993) J Bacteriol , vol.175 , pp. 2692-2701
    • Moore, J.B.1    Shiau, S.P.2    Reitzer, L.J.3
  • 33
    • 0021359008 scopus 로고
    • Demethylation of methyl-accepting chemotaxis proteins in Escherichia coli induced by the repellents glycerol and ethylene glycol
    • Oosawa, K., and Imae, Y. (1984) Demethylation of methyl-accepting chemotaxis proteins in Escherichia coli induced by the repellents glycerol and ethylene glycol. J Bacteriol 157: 576-581.
    • (1984) J Bacteriol , vol.157 , pp. 576-581
    • Oosawa, K.1    Imae, Y.2
  • 34
    • 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
  • 35
    • 0028268070 scopus 로고
    • FixL of Rhizobium meliloti enhances the transcriptional activity of a mutant FixJD54N protein by phosphorylation of an alternate residue
    • Reyrat, J.-M., David, M., Batut, J., and Boistard, P. (1994) FixL of Rhizobium meliloti enhances the transcriptional activity of a mutant FixJD54N protein by phosphorylation of an alternate residue. J Bacteriol 176: 1969-1976.
    • (1994) J Bacteriol , vol.176 , pp. 1969-1976
    • Reyrat, J.-M.1    David, M.2    Batut, J.3    Boistard, P.4
  • 36
    • 0016360069 scopus 로고
    • Deamidation of glutaminyl and asparaginyl residues in peptides and proteins
    • Robinson, A.B., and Rudd, C.J. (1974) Deamidation of glutaminyl and asparaginyl residues in peptides and proteins. Curr Topics Cell Regul 8: 247-295.
    • (1974) Curr Topics Cell Regul , vol.8 , pp. 247-295
    • Robinson, A.B.1    Rudd, C.J.2
  • 37
    • 0024787464 scopus 로고
    • Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY
    • Sanders, D.A., Gillece-Castro, B.L., Stock, A.M., Burlingame, A.L., and Koshland, Jr, 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    Gillece-Castro, B.L.2    Stock, A.M.3    Burlingame, A.L.4    Koshland D.E., Jr.5
  • 38
    • 0028959024 scopus 로고
    • Three-dimensional structure of chemotactic CheY protein in aqueous solution by nuclear magnetic resonance methods
    • Santoro, J., Bruix, M., Pascual, J., Lopez, E., Serrano, L., and Rico, M. (1995) Three-dimensional structure of chemotactic CheY protein in aqueous solution by nuclear magnetic resonance methods. J Mol Biol 247: 717-725.
    • (1995) J Mol Biol , vol.247 , pp. 717-725
    • Santoro, J.1    Bruix, M.2    Pascual, J.3    Lopez, E.4    Serrano, L.5    Rico, M.6
  • 39
    • 0019953987 scopus 로고
    • Signal processing times in bacterial chemotaxis
    • Segall, J.E., Manson, M.D., and Berg, H.C. (1982) Signal processing times in bacterial chemotaxis. Nature 296: 855-857.
    • (1982) Nature , vol.296 , pp. 855-857
    • Segall, J.E.1    Manson, M.D.2    Berg, H.C.3
  • 40
    • 0030817793 scopus 로고    scopus 로고
    • The catalytic mechanism of phosphorylation and dephosphorylation of CheY: Kinetic characterization of imidazolephosphates as phosphodonors and the role of acid catalysis
    • Silversmith, R.E., Appleby, J.L., and Bourret, R.B. (1997) The catalytic mechanism of phosphorylation and dephosphorylation of CheY: kinetic characterization of imidazolephosphates as phosphodonors and the role of acid catalysis. Biochemistry 36: 14965-14974.
    • (1997) Biochemistry , vol.36 , pp. 14965-14974
    • Silversmith, R.E.1    Appleby, J.L.2    Bourret, R.B.3
  • 41
    • 0031895361 scopus 로고    scopus 로고
    • Synthesis and characterization of a stable analogue of the phosphorylated form of the chemotaxis protein CheY
    • Silversmith, R.E., and Bourret, R.B. (1998) Synthesis and characterization of a stable analogue of the phosphorylated form of the chemotaxis protein CheY. Protein Eng 11: 205-212.
    • (1998) Protein Eng , vol.11 , pp. 205-212
    • Silversmith, R.E.1    Bourret, R.B.2
  • 42
    • 0017667528 scopus 로고
    • Sensory transduction in Escherichia coli: Two complementary pathways of information processing that involve methylated proteins
    • Springer, M.S., Goy, M.F., and Adler, J. (1977) Sensory transduction in Escherichia coli: two complementary pathways of information processing that involve methylated proteins. Proc Natl Acad Sci USA 74: 3312-3316.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 3312-3316
    • Springer, M.S.1    Goy, M.F.2    Adler, J.3
  • 43
    • 0024562159 scopus 로고
    • Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
    • Stock, A.M., Motionen, J.M., Stock, J.B., and Schutt, C.E. (1989) Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Nature 337: 745-749.
    • (1989) Nature , vol.337 , pp. 745-749
    • Stock, A.M.1    Motionen, J.M.2    Stock, J.B.3    Schutt, C.E.4
  • 45
    • 0001792698 scopus 로고
    • Two-component signal transduction systems: Structure-function relationships and mechanisms of catalysis
    • Hoch, J.A., and Silhavy, T.J. (eds). Washington, DC: American Society for Microbiology Press
    • Stock, J.B., Surette, M.G., Levit, M., and Park, P. (1995) Two-component signal transduction systems: structure -function relationships and mechanisms of catalysis. In Two-Component Signal Transduction. Hoch, J.A., and Silhavy, T.J. (eds). Washington, DC: American Society for Microbiology 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
  • 47
    • 0027366420 scopus 로고
    • Structural conservation in the CheY super-family
    • Volz, K. (1993) Structural conservation in the CheY super-family. Biochemistry 32: 11741-11753.
    • (1993) Biochemistry , vol.32 , pp. 11741-11753
    • Volz, K.1
  • 48
    • 0025741662 scopus 로고
    • Crystal structure of Escherichia coli CheY refined at 1.7-Å resolution
    • Volz, K., and Matsumura, P. (1991) Crystal structure of Escherichia coli CheY refined at 1.7-Å resolution. J Biol Chem 266: 15511-15519.
    • (1991) J Biol Chem , vol.266 , pp. 15511-15519
    • Volz, K.1    Matsumura, P.2
  • 49
    • 0027517812 scopus 로고
    • Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria
    • Welch, M., Oosawa, K., Aizawa, S.-I., and Eisenbach, M. (1993) Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. Proc Natl Acad Sci USA 90: 8787-8791.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8787-8791
    • Welch, M.1    Oosawa, K.2    Aizawa, S.-I.3    Eisenbach, M.4
  • 50
    • 0028167952 scopus 로고
    • 2+, and conformation of the chemotaxis protein CheY on its binding to the flagellar switch protein FliM
    • 2+, and conformation of the chemotaxis protein CheY on its binding to the flagellar switch protein FliM. Biochemistry 33: 10470-10476.
    • (1994) Biochemistry , vol.33 , pp. 10470-10476
    • Welch, M.1    Oosawa, K.2    Aizawa, S.-I.3    Eisenbach, M.4
  • 51
    • 0026320363 scopus 로고
    • Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins
    • Wright, HT. (1991) Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Crit Rev Biochem Mol Biol 26: 1-52.
    • (1991) Crit Rev Biochem Mol Biol , vol.26 , pp. 1-52
    • Wright, H.T.1
  • 52
    • 0032506138 scopus 로고    scopus 로고
    • Eukaryotic phytochromes: Light-regulated serine/threonine protein kinases with histidine kinase ancestry
    • Yeh, K.C., and Lagarias, J.C. (1998) Eukaryotic phytochromes: light-regulated serine/threonine protein kinases with histidine kinase ancestry. Proc Natl Acad Sci USA 95: 13976-13981.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13976-13981
    • Yeh, K.C.1    Lagarias, J.C.2
  • 53
    • 0030873934 scopus 로고    scopus 로고
    • The CheZ-binding surface of CheY overlaps with the CheA-and FliM-binding surfaces
    • Zhu, X., Volz, K., and Matsumura, P. (1997) The CheZ-binding surface of CheY overlaps with the CheA-and FliM-binding surfaces. J Biol Chem 272: 23758-23764.
    • (1997) J Biol Chem , vol.272 , pp. 23758-23764
    • Zhu, X.1    Volz, K.2    Matsumura, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.