메뉴 건너뛰기




Volumn 9, Issue 5, 2000, Pages 898-906

Evidence for phosphorylation-dependent conformational changes in methylesterase CheB

Author keywords

Activation; Conformational change; Limited proteolysis; MALDI mass spectrometry; Phosphorylation; Response regulator

Indexed keywords

BACTERIAL ENZYME; ESTERASE;

EID: 0034129478     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.5.898     Document Type: Article
Times cited : (16)

References (24)
  • 1
    • 0032739281 scopus 로고    scopus 로고
    • C-terminal DNA binding stimulates N-terminal phosphorylation of the outer membrane protein regulator OmpR from Escherichia coli
    • Ames SK, Frankema N, Kenney LJ. 1999. C-terminal DNA binding stimulates N-terminal phosphorylation of the outer membrane protein regulator OmpR from Escherichia coli. Proc Natl Acad Sci USA 96:11792-11797.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11792-11797
    • Ames, S.K.1    Frankema, N.2    Kenney, L.J.3
  • 2
    • 0032491213 scopus 로고    scopus 로고
    • Activation of methylesterase CheB: Evidence of a dual role for the regulatory domain
    • Anand GS, Goudreau PN, Stock AM. 1998. Activation of methylesterase CheB: evidence of a dual role for the regulatory domain. Biochemistry 37:14038-14047.
    • (1998) Biochemistry , vol.37 , pp. 14038-14047
    • Anand, G.S.1    Goudreau, P.N.2    Stock, A.M.3
  • 3
    • 0030595328 scopus 로고    scopus 로고
    • Signal transduction via the multistep phosphorelay: Not necessarily a road less traveled
    • Appleby JL, Parkinson JS, Bourret RB. 1996. Signal transduction via the multistep phosphorelay: Not necessarily a road less traveled. Cell 86:845-848.
    • (1996) Cell , vol.86 , pp. 845-848
    • Appleby, J.L.1    Parkinson, J.S.2    Bourret, R.B.3
  • 5
    • 0026240806 scopus 로고
    • Ribbons 2.0
    • Carson M. 1991. Ribbons 2.0. J Appl Cryst 24:958-961.
    • (1991) J Appl Cryst , vol.24 , pp. 958-961
    • Carson, M.1
  • 6
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J, Haeberli P, Smithies O. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12:387-395.
    • (1984) Nucleic Acids Res , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 7
    • 0032539671 scopus 로고    scopus 로고
    • Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain
    • Djordjevic S, Goudreau PN, Xu Q, Stock AM, West AH. 1998. Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain. Proc Natl Acad Sci USA 95:1381-1386.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1381-1386
    • Djordjevic, S.1    Goudreau, P.N.2    Xu, Q.3    Stock, A.M.4    West, A.H.5
  • 8
    • 0031455398 scopus 로고    scopus 로고
    • The two-component signaling pathway of bacterial chemotaxis: A molecular view of signal transduction by receptors, kinases, and adaptation enzymes
    • Falke JJ, Bass RB, Butler SL, Chervitz SA, Danielson MA. 1997. The two-component signaling pathway of bacterial chemotaxis: A molecular view of signal transduction by receptors, kinases, and adaptation enzymes. Annu Rev Cell Dev Biol 13:457-512.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 457-512
    • Falke, J.J.1    Bass, R.B.2    Butler, S.L.3    Chervitz, S.A.4    Danielson, M.A.5
  • 9
    • 0028914318 scopus 로고
    • Analysis of a chemotaxis operon in Rhizobium meliloti
    • Greek M, Platzer J, Sourjik V, Schmitt R. 1995. Analysis of a chemotaxis operon in Rhizobium meliloti. Mol Microbiol 15:989-1000.
    • (1995) Mol Microbiol , vol.15 , pp. 989-1000
    • Greek, M.1    Platzer, J.2    Sourjik, V.3    Schmitt, R.4
  • 11
    • 0030884924 scopus 로고    scopus 로고
    • Analysis at a chemotaxis operon from Rhodospirillum centenum
    • Jiang Z-Y, Bauer CE. 1997. Analysis at a chemotaxis operon from Rhodospirillum centenum. J Bacteriol 179:5712-5719.
    • (1997) J Bacteriol , vol.179 , pp. 5712-5719
    • Jiang, Z.-Y.1    Bauer, C.E.2
  • 12
    • 0029026859 scopus 로고
    • Phosphorylation-dependent conformational changes in OmpR, an osmoregulatory DNA-binding protein of Escherichia coli
    • Kenney LJ, Bauer MD, Silhavy TJ. 1995. Phosphorylation-dependent conformational changes in OmpR, an osmoregulatory DNA-binding protein of Escherichia coli. Proc Natl Acad Sci USA 92:8866-8870.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8866-8870
    • Kenney, L.J.1    Bauer, M.D.2    Silhavy, T.J.3
  • 13
    • 0033599026 scopus 로고    scopus 로고
    • Structure of a transiently phosphorylated switch in bacterial signal transduction
    • Kern D, Volkman BF, Luginbühl P, Nohaile MJ, Kustu S, Wemmer DE. 1999. Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature 402:894-898.
    • (1999) Nature , vol.402 , pp. 894-898
    • Kern, D.1    Volkman, B.F.2    Luginbühl, P.3    Nohaile, M.J.4    Kustu, S.5    Wemmer, D.E.6
  • 15
    • 0025314338 scopus 로고
    • Divalent metal ion binding to the CheY protein and its significance to phosphotransfer in bacterial chemotaxis
    • Lukat GS, Stock AM, Stock JB. 1990. Divalent metal ion binding to the CheY protein and its significance to phosphotransfer in bacterial chemotaxis. Biochemistry 29:5436-5442.
    • (1990) Biochemistry , vol.29 , pp. 5436-5442
    • Lukat, G.S.1    Stock, A.M.2    Stock, J.B.3
  • 16
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp K, Honig B, 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 4:281-296.
    • (1991) Proteins , vol.4 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 20
    • 0022405719 scopus 로고
    • Multiple forms of the CheB methylesterase in bacterial chemosensing
    • Simms SA, Keane MG, Stock J. 1985. Multiple forms of the CheB methylesterase in bacterial chemosensing. J Biol Chem 260:10161-10168.
    • (1985) J Biol Chem , vol.260 , pp. 10161-10168
    • Simms, S.A.1    Keane, M.G.2    Stock, J.3
  • 21
    • 0027470710 scopus 로고
    • Activating and inhibitory mutations in the regulatory domain of CheB, the methylesterase in bacterial chemotaxis
    • Stewart RC. 1993. Activating and inhibitory mutations in the regulatory domain of CheB, the methylesterase in bacterial chemotaxis. J Biol Chem 268: 1921-1930.
    • (1993) J Biol Chem , vol.268 , pp. 1921-1930
    • Stewart, R.C.1
  • 23
    • 0000621729 scopus 로고    scopus 로고
    • Chemotaxis
    • Neidhardl FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE, eds. Washington, DC: ASM Press
    • Stock JB, Surette MG. 1996. Chemotaxis. In: Neidhardl FC, Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE, eds. Escherichia coli and salmonella: Cellular and molecular biology, 2nd ed. Washington, DC: ASM Press, pp 1103-1129.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 1103-1129
    • Stock, J.B.1    Surette, M.G.2
  • 24
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.