메뉴 건너뛰기




Volumn 180, Issue 14, 1998, Pages 3563-3569

Proposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator active-site quintet

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; PROTEIN CHEY; REGULATOR PROTEIN; SERINE; THREONINE; UNCLASSIFIED DRUG;

EID: 0032456891     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.14.3563-3569.1998     Document Type: Article
Times cited : (66)

References (36)
  • 2
    • 0026572085 scopus 로고
    • Correlation between phosphorylation of the chemotaxis protein CheY and its activity at the flagellar motor
    • Barak, R., and M. Eisenbach. 1992. Correlation between phosphorylation of the chemotaxis protein CheY and its activity at the flagellar motor. Biochemistry 31:1821-1826.
    • (1992) Biochemistry , vol.31 , pp. 1821-1826
    • Barak, R.1    Eisenbach, M.2
  • 4
    • 0025021988 scopus 로고
    • Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY
    • Bourret, R. B., J. F. Hess, and M. I. Simon. 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
  • 5
    • 0027231876 scopus 로고
    • Computer simulation of the phosphorylation cascade controlling bacterial chemotaxis
    • Bray, D., R. B. Bourret, and M. I. Simon. 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
  • 6
    • 0025785385 scopus 로고
    • Intramolecular second-site revertants to the phosphorylation site mutation in OmpR, a kinase-dependent transcriptional activator in Escherichia coli
    • Brissette, R. E., K. Tsung, and M. Inouye. 1991. Intramolecular second-site revertants to the phosphorylation site mutation in OmpR, a kinase-dependent transcriptional activator in Escherichia coli. J. Bacteriol. 173:3749-3755.
    • (1991) J. Bacteriol. , vol.173 , pp. 3749-3755
    • Brissette, R.E.1    Tsung, K.2    Inouye, M.3
  • 7
    • 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., H. Wang, P. Matsumura, and K. Volz. 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
  • 8
    • 0026345261 scopus 로고
    • Phosphorylation assays for proteins of the two-component regulatory system controlling chemotaxis in Escherichia coli
    • Hess, J. F., R. B. Bourret, and M. I. Simon. 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
  • 10
    • 0024759933 scopus 로고
    • Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor
    • Igo, M. M., A. J. Ninfa, J. B. Stock, and T. J. Silhavy. 1989. Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor. Genes Dev. 3:1725-1734.
    • (1989) Genes Dev. , vol.3 , pp. 1725-1734
    • Igo, M.M.1    Ninfa, A.J.2    Stock, J.B.3    Silhavy, T.J.4
  • 11
    • 0031007417 scopus 로고    scopus 로고
    • Uncoupled phosphorylation and activation in bacterial chemotaxis: The 2.3-Å structure of an aspartate to lysine mutant at position 13 of CheY
    • Jiang, M., R. B. Bourret, M. I. Simon, and K. Volz. 1997. Uncoupled phosphorylation and activation in bacterial chemotaxis: the 2.3-Å structure of an aspartate to lysine mutant at position 13 of CheY. J. Biol. Chem. 272:11850-11855.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11850-11855
    • Jiang, M.1    Bourret, R.B.2    Simon, M.I.3    Volz, K.4
  • 12
    • 33947463386 scopus 로고
    • Effect of catalysts on the hydrolysis of acetyl phosphate: Nucleophilic displacement mechanisms in enzymatic reactions
    • Koshland, D. E., Jr. 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 Jr., D.E.1
  • 13
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts, and R. Zakour. 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
  • 14
    • 0024316868 scopus 로고
    • Role of CheW protein in coupling membrane receptors to the intracellular signaling system of bacterial chemotaxis
    • Liu, J. D., and J. S. Parkinson. 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
  • 15
  • 16
    • 0025881094 scopus 로고
    • Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis
    • Lukat, G. S., B. H. Lee, J. M. Mottonen, A. M. Stock, and J. B. Stock. 1991. Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis. J. Biol. Chem. 266:8348-5354.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8348-15354
    • Lukat, G.S.1    Lee, B.H.2    Mottonen, J.M.3    Stock, A.M.4    Stock, J.B.5
  • 18
    • 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
  • 19
    • 0026761084 scopus 로고
    • A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations
    • Roman, S. J., M. Meyers, K. Volz, and P. Matsumura. 1992. A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations. J. Bacteriol. 174:6247-6255.
    • (1992) J. Bacteriol. , vol.174 , pp. 6247-6255
    • Roman, S.J.1    Meyers, M.2    Volz, K.3    Matsumura, P.4
  • 20
    • 0024787464 scopus 로고
    • Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY
    • Sanders, D. A., B. L. Gillece-Castro, A. M. Stock, A. L. Burlingame, and D. E. Koshland, Jr. 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 Jr., D.E.5
  • 21
    • 0028959024 scopus 로고
    • Three-dimensional structure of chemotactic CheY protein in aqueous solution by nuclear magnetic resonance methods
    • Santoro, J., M. Bruix, J. Pascual, E. Lopez, L. Serrano, and M. Rico. 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
  • 23
    • 0030817793 scopus 로고    scopus 로고
    • The catalytic mechanism of phosphorylation and dephosphorylation of CheY: Kinetic characterization of imidazole-phosphates as phosphodonors and the role of acid catalysis
    • Silversmith, R. E., J. L. Appleby, and R. B. Bourret. 1997. The catalytic mechanism of phosphorylation and dephosphorylation of CheY: kinetic characterization of imidazole-phosphates 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
  • 25
    • 0024562159 scopus 로고
    • Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
    • Stock, A. M., J. M. Mottonen, J. B. Stock, and C. E. Schutt. 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    Mottonen, J.M.2    Stock, J.B.3    Schutt, C.E.4
  • 26
    • 0000621729 scopus 로고    scopus 로고
    • Chemotaxis, p. 1103-1129
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), ASM Press, Washington, D.C.
    • Stock, J. B., and M. G. Surette. 1996. Chemotaxis, p. 1103-1129. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed.
    • Stock, J.B.1    Surette, M.G.2
  • 27
    • 0001792698 scopus 로고
    • Two-component signal transduction systems: Structure-function relationships and mechanisms of catalysis, p. 25-51
    • J. A. Hoch and T. J. Silhavy (ed.), ASM Press, Washington, D.C.
    • Stock, J. B., M. G. Surrette, M. Levit, and P. Park. 1995. Two-component signal transduction systems: structure-function relationships and mechanisms of catalysis, p. 25-51. In J. A. Hoch and T. J. Silhavy (ed.), Two-component signal transduction. ASM Press, Washington, D.C.
    • (1995) Two-component Signal Transduction
    • Stock, J.B.1    Surrette, M.G.2    Levit, M.3    Park, P.4
  • 28
    • 0028138668 scopus 로고
    • Histidine and aspartate phosphorylation: Two-component regulatory systems and the limits of homology
    • Swanson, R. V., L. A. Alex, and M. I. Simon. 1994. Histidine and aspartate phosphorylation: two-component regulatory systems and the limits of homology. Trends Biochem. Sci. 19:485-490.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 485-490
    • Swanson, R.V.1    Alex, L.A.2    Simon, M.I.3
  • 29
    • 0030813090 scopus 로고    scopus 로고
    • Molecular recognition in signal transduction: The interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis
    • Tzeng, Y.-L., and J. A. Hoch. 1997. Molecular recognition in signal transduction: the interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis. J. Mol. Biol. 272:200-212.
    • (1997) J. Mol. Biol. , vol.272 , pp. 200-212
    • Tzeng, Y.-L.1    Hoch, J.A.2
  • 30
    • 0027366420 scopus 로고
    • Structural conservation in the CheY superfamily
    • Volz, K. 1993. Structural conservation in the CheY superfamily. Biochemistry 32:11741-11753.
    • (1993) Biochemistry , vol.32 , pp. 11741-11753
    • Volz, K.1
  • 31
    • 0025741662 scopus 로고
    • Crystal structure of Escherichia coli CheY refined at 1.7-Å resolution
    • Volz, K., and P. Matsumura. 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
  • 32
    • 0026783517 scopus 로고
    • Isolation of phosphorylation-deficient mutants of the Rhizobium meliloti two-component regulatory protein, FixJ
    • Weinstein, M., A. F. Lois, E. K. Monson, G. S. Ditta, and D. R. Helinski. 1992. Isolation of phosphorylation-deficient mutants of the Rhizobium meliloti two-component regulatory protein, FixJ. Mol. Microbiol. 6:2041-2049.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2041-2049
    • Weinstein, M.1    Lois, A.F.2    Monson, E.K.3    Ditta, G.S.4    Helinski, D.R.5
  • 33
    • 0007809063 scopus 로고
    • Migration of bacteria in semisolid agar
    • Wolfe, A. J., and H. C. Berg. 1989. Migration of bacteria in semisolid agar. Proc. Natl. Acad. Sci. USA 86:6973-6977.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6973-6977
    • Wolfe, A.J.1    Berg, H.C.2
  • 34
    • 0029900040 scopus 로고    scopus 로고
    • Tyrosine 106 of CheY plays an important role in chemotaxis signal transduction in Escherichia coli
    • Zhu, X., C. D. Amsler, K. Volz, and P. Matsumura. 1996. Tyrosine 106 of CheY plays an important role in chemotaxis signal transduction in Escherichia coli. J. Bacteriol. 178:4208-4215.
    • (1996) J. Bacteriol. , vol.178 , pp. 4208-4215
    • Zhu, X.1    Amsler, C.D.2    Volz, K.3    Matsumura, P.4
  • 35
    • 0031058440 scopus 로고    scopus 로고
    • Crystal structures of CheY mutants Y106W and T87I/Y106W: CheY activation correlates with movement of residue 106
    • Zhu, X., J. Rebello, P. Matsumura, and K. Volz. 1997. Crystal structures of CheY mutants Y106W and T87I/Y106W: CheY activation correlates with movement of residue 106. J. Biol. Chem. 272:5000-5006.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5000-5006
    • Zhu, X.1    Rebello, J.2    Matsumura, P.3    Volz, K.4
  • 36
    • 0030873934 scopus 로고    scopus 로고
    • The CheZ-binding surface of CheY overlaps with the CheA- and FliM-binding surfaces
    • Zhu, X., K. Volz, and P. Matsumura. 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.