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Volumn 263, Issue 5, 1996, Pages 671-684

The effect of self-association on the interaction of the Escherichia coli regulatory protein TyrR with DNA

Author keywords

Analytical ultracentrifugation; DNA protein interactions; Heterogeneous associations; Sedimentation equilibrium; TyrR

Indexed keywords

FLUORESCEIN ISOTHIOCYANATE; OLIGONUCLEOTIDE; REGULATOR PROTEIN;

EID: 0030589088     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0607     Document Type: Article
Times cited : (38)

References (40)
  • 1
    • 0026326004 scopus 로고
    • Importance of the position of TyrR boxes for repression and activation of the tyrP and aroF genes in Escherichia coli
    • Andrews, A. E., Dickson, B., Lawley, B., Cobbett, C. & Pittard, A. J. (1991a). Importance of the position of TyrR boxes for repression and activation of the tyrP and aroF genes in Escherichia coli. J. Bacteriol. 173, 5079-5085.
    • (1991) J. Bacteriol. , vol.173 , pp. 5079-5085
    • Andrews, A.E.1    Dickson, B.2    Lawley, B.3    Cobbett, C.4    Pittard, A.J.5
  • 2
    • 0026317737 scopus 로고
    • Mutational analysis of repression and activation of the tyrP gene in Escherichia coli
    • Andrews, A. E., Lawley, B. & Pittard, A. J. (1991b). Mutational analysis of repression and activation of the tyrP gene in Escherichia coli. J. Bacteriol. 173, 5068-5078.
    • (1991) J. Bacteriol. , vol.173 , pp. 5068-5078
    • Andrews, A.E.1    Lawley, B.2    Pittard, A.J.3
  • 3
    • 0028095496 scopus 로고
    • Purification of the Escherichia coli regulatory protein TyrR and analysis of its interactions with ATP, tyrosine, phenylalanine, and tryptophan
    • Argaet, V. P., Wilson, T. J. & Davidson, B. E. (1994). Purification of the Escherichia coli regulatory protein TyrR and analysis of its interactions with ATP, tyrosine, phenylalanine, and tryptophan. J. Biol. Chem. 269, 5171-5178.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5171-5178
    • Argaet, V.P.1    Wilson, T.J.2    Davidson, B.E.3
  • 4
    • 0028827717 scopus 로고
    • The interaction between the Escherichia coli regulatory protein TyrR and DNA: A fluorescence footprinting study
    • Bailey, M., Hagmar, P., Millar, D. P., Davidson, B. E., Tong, G., Haralambidis, J. & Sawyer, W. H. (1995). The interaction between the Escherichia coli regulatory protein TyrR and DNA: a fluorescence footprinting study. Biochemistry, 34, 15802-15812.
    • (1995) Biochemistry , vol.34 , pp. 15802-15812
    • Bailey, M.1    Hagmar, P.2    Millar, D.P.3    Davidson, B.E.4    Tong, G.5    Haralambidis, J.6    Sawyer, W.H.7
  • 5
    • 0025305138 scopus 로고
    • Identification of the promoter, operator and 5′ and 3′ ends of the mRNA of the Escherichia coli K-12 gene aroG
    • Baseggio, N., Davies, W. D. & Davidson, B. E. (1990). Identification of the promoter, operator and 5′ and 3′ ends of the mRNA of the Escherichia coli K-12 gene aroG. J. Bacteriol. 172, 2547-2557.
    • (1990) J. Bacteriol. , vol.172 , pp. 2547-2557
    • Baseggio, N.1    Davies, W.D.2    Davidson, B.E.3
  • 6
    • 0020443521 scopus 로고
    • Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography
    • Bochner, B. R. & Ames, B. N. (1982). Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography. J. Biol. Chem. 257, 9759-9769.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9759-9769
    • Bochner, B.R.1    Ames, B.N.2
  • 7
    • 0022636950 scopus 로고
    • Structure of the Escherichia coli K12 regulatory gene tyrR. Nucleotide sequence and sites of initiation of transcription and translation
    • Cornish, E. C., Argyropoulos, V. P., Pittard, A. J. & Davidson, B. E. (1986). Structure of the Escherichia coli K12 regulatory gene tyrR. Nucleotide sequence and sites of initiation of transcription and translation. J. Biol. Chem. 261, 403-410.
    • (1986) J. Biol. Chem. , vol.261 , pp. 403-410
    • Cornish, E.C.1    Argyropoulos, V.P.2    Pittard, A.J.3    Davidson, B.E.4
  • 8
    • 0027394309 scopus 로고
    • A mutational analysis of the structural basis for transcriptional activation and monomer-monomer interaction in the TyrR system of Escherichia coli K-12
    • Cui, J. & Somerville, R. L. (1993a). A mutational analysis of the structural basis for transcriptional activation and monomer-monomer interaction in the TyrR system of Escherichia coli K-12. J. Bacteriol. 268, 1777-1784.
    • (1993) J. Bacteriol. , vol.268 , pp. 1777-1784
    • Cui, J.1    Somerville, R.L.2
  • 9
    • 0027513995 scopus 로고
    • The TyrR protein of Escherichia coli, analysis by limited proteolysis of domain structure and ligand-mediated conformational changes
    • Cui, J. & Somerville, R. L. (1993b). The TyrR protein of Escherichia coli, analysis by limited proteolysis of domain structure and ligand-mediated conformational changes. J. Biol. Chem. 268, 5040-5047.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5040-5047
    • Cui, J.1    Somerville, R.L.2
  • 10
    • 0027469325 scopus 로고
    • Mutational uncoupling of the transcriptional activation function of the TyrR protein of Escherichia coli K-12 from the repression function
    • Cui, J. & Somerville, R. L. (1993c). Mutational uncoupling of the transcriptional activation function of the TyrR protein of Escherichia coli K-12 from the repression function. J. Bacteriol. 175, 303-306.
    • (1993) J. Bacteriol. , vol.175 , pp. 303-306
    • Cui, J.1    Somerville, R.L.2
  • 11
    • 0000926337 scopus 로고
    • Cell division: Parameter values and the process
    • (Neidhardt, F. C., Ingraham, J. L., Brooks-Low, K., Magasanic, B., Schaechter, M. & Umbarger, H. E., eds), American Society for Microbiology, Washington, DC
    • Donachie, W. D. & Robinson, A. C. (1987). Cell division: parameter values and the process. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology (Neidhardt, F. C., Ingraham, J. L., Brooks-Low, K., Magasanic, B., Schaechter, M. & Umbarger, H. E., eds), pp. 1578-1593, American Society for Microbiology, Washington, DC.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 1578-1593
    • Donachie, W.D.1    Robinson, A.C.2
  • 12
    • 0002258696 scopus 로고
    • Specific volumes of biological macromolecules and some other molecules of biological interest
    • (Hinz, H.-J., ed.), Springer-Verlag, New York
    • Durchschlag, H. (1986). Specific volumes of biological macromolecules and some other molecules of biological interest. In Thermodynamic Data for Biochemistry and Biotechnology (Hinz, H.-J., ed.), pp. 45-115, Springer-Verlag, New York.
    • (1986) Thermodynamic Data for Biochemistry and Biotechnology , pp. 45-115
    • Durchschlag, H.1
  • 13
    • 0029026511 scopus 로고
    • Synthesis and characterisation of fluorescent oligonucleotides. Effect of internal labelling on protein recognition
    • Hagmar, P., Bailey, M., Tong, G., Haralambidis, J., Sawyer, W. H. & Davidson, B. E. (1995). Synthesis and characterisation of fluorescent oligonucleotides. Effect of internal labelling on protein recognition. Biochim. Biophys. Acta, 1244, 259-268.
    • (1995) Biochim. Biophys. Acta , vol.1244 , pp. 259-268
    • Hagmar, P.1    Bailey, M.2    Tong, G.3    Haralambidis, J.4    Sawyer, W.H.5    Davidson, B.E.6
  • 14
    • 0023915473 scopus 로고
    • Detection of protein similarities using nucleotide sequence databases
    • Henikoff, S. & Wallace, J. C. (1988). Detection of protein similarities using nucleotide sequence databases. Nucl. Acids Res. 16, 6191-6204.
    • (1988) Nucl. Acids Res. , vol.16 , pp. 6191-6204
    • Henikoff, S.1    Wallace, J.C.2
  • 15
    • 0024284648 scopus 로고
    • Structure of the lambda complex at 2.5 Å resolution: Details of the repressor -operator interactions
    • Jordan, S. R. & Pabo, C. O. (1988). Structure of the lambda complex at 2.5 Å resolution: details of the repressor -operator interactions. Science, 242, 893-899.
    • (1988) Science , vol.242 , pp. 893-899
    • Jordan, S.R.1    Pabo, C.O.2
  • 16
    • 0028366006 scopus 로고
    • Interaction of the DNA-binding domain of Drosophila heat shock factor with its cognate DNA site: A thermodynamic analysis using analytical ultracentrifugation
    • Kim, S. J., Tsukiyama, T., Lewis, M. S. & Wu, C. (1994). Interaction of the DNA-binding domain of Drosophila heat shock factor with its cognate DNA site: a thermodynamic analysis using analytical ultracentrifugation. Protein Sci. 3, 1040-1051.
    • (1994) Protein Sci. , vol.3 , pp. 1040-1051
    • Kim, S.J.1    Tsukiyama, T.2    Lewis, M.S.3    Wu, C.4
  • 17
    • 0026717535 scopus 로고
    • Three-dimensional structure of the β subunit of E. Coli DNA polymerase III holoenzyme: A sliding DNA clamp
    • Kong, X.-P., Onrust, R., O'Donnell, M. & Kuriyan, J. (1992). Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp. Cell, 69, 425-437.
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.-P.1    Onrust, R.2    O'Donnell, M.3    Kuriyan, J.4
  • 18
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna, T. S. R., Kong, X.-P., Gary, S., Burgers, P. M. & Kuriyan, J. (1994). Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell, 79, 1233-1243.
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.R.1    Kong, X.-P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 21
    • 0027537906 scopus 로고
    • 5-Hydroxytryptophan as a new intrinsic probe for investigating protein-DNA interactions by analytical ultracentrifugation. Study of the effect of DNA on the self-assembly of the bacteriophage κ, cI repressor
    • Laue, T. M., Senear, D. F., Eaton, S. & Ross, A. J. B. (1993). 5-Hydroxytryptophan as a new intrinsic probe for investigating protein-DNA interactions by analytical ultracentrifugation. Study of the effect of DNA on the self-assembly of the bacteriophage κ, cI repressor. Biochemistry, 32, 2469-2472.
    • (1993) Biochemistry , vol.32 , pp. 2469-2472
    • Laue, T.M.1    Senear, D.F.2    Eaton, S.3    Ross, A.J.B.4
  • 22
    • 0027987492 scopus 로고
    • Regulation of aroL expression by TyrR protein and Trp repressor in Escherichia coli K-12
    • Lawley, B. & Pittard, A. J. (1994). Regulation of aroL expression by TyrR protein and Trp repressor in Escherichia coli K-12. J. Bacteriol. 176, 6921-6930.
    • (1994) J. Bacteriol. , vol.176 , pp. 6921-6930
    • Lawley, B.1    Pittard, A.J.2
  • 23
    • 0028893760 scopus 로고
    • The TyrR protein of Escherichia coli is a class I transcription activator
    • Lawley, B., Fujita, N., Ishihama, A. & Pittard, A. J. (1995). The TyrR protein of Escherichia coli is a class I transcription activator. J. Bacteriol. 177, 238-241.
    • (1995) J. Bacteriol. , vol.177 , pp. 238-241
    • Lawley, B.1    Fujita, N.2    Ishihama, A.3    Pittard, A.J.4
  • 26
    • 0019463941 scopus 로고
    • Structure of the catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA
    • McKay, D. B. & Steitz, T. A. (1981). Structure of the catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA. Nature, 290, 744-749.
    • (1981) Nature , vol.290 , pp. 744-749
    • McKay, D.B.1    Steitz, T.A.2
  • 27
    • 0027340543 scopus 로고
    • 54 bacterial enhancer-binding family: Mechanism of action and phylogenetic relationship of their functional domains
    • 54 bacterial enhancer-binding family: mechanism of action and phylogenetic relationship of their functional domains. J. Bacteriol. 175, 6067-6074.
    • (1993) J. Bacteriol. , vol.175 , pp. 6067-6074
    • Morett, E.1    Segovia, L.2
  • 28
    • 0025835584 scopus 로고
    • The tyrosine repressor negatively regulates aroH expression in Escherichia coli
    • Muday, G. K., Johnson, D. I., Somerville, R. L. & Herrmann, K. M. (1991). The tyrosine repressor negatively regulates aroH expression in Escherichia coli. J. Bacteriol. 173, 3930-3932.
    • (1991) J. Bacteriol. , pp. 3930-3932
    • Muday, G.K.1    Johnson, D.I.2    Somerville, R.L.3    Herrmann, K.M.4
  • 29
    • 0019977222 scopus 로고
    • The operator-binding domain of λ repressor: Structure and DNA recognition
    • Pabo, C. O. & Lewis, M. (1982). The operator-binding domain of λ repressor: structure and DNA recognition. Nature, 298, 443-447.
    • (1982) Nature , vol.298 , pp. 443-447
    • Pabo, C.O.1    Lewis, M.2
  • 30
    • 0003796799 scopus 로고
    • Biosynthesis of the aromatic amino acids
    • (Neidhardt, F. C., Ingraham, J. L., Brooks-Low, K., Magasanik, B., Schaechter, M. & Umbarger, H. E., eds), American Society for Microbiology, Washington, DC
    • Pittard, A. J. (1987). Biosynthesis of the aromatic amino acids. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology (Neidhardt, F. C., Ingraham, J. L., Brooks-Low, K., Magasanik, B., Schaechter, M. & Umbarger, H. E., eds), pp. 368-394, American Society for Microbiology, Washington, DC.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 368-394
    • Pittard, A.J.1
  • 31
    • 0025740385 scopus 로고
    • TyrR protein of Escherichia coli and its role as repressor and activator
    • Pittard, A. J. & Davidson, B. E. (1991). TyrR protein of Escherichia coli and its role as repressor and activator. Mol. Microbiol. 5, 1585-1592.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1585-1592
    • Pittard, A.J.1    Davidson, B.E.2
  • 32
    • 0029147295 scopus 로고
    • A structural model for the Escherichia coli DnaB helicase based on electron microscopy data
    • San Martin, M. C., Stamford, N. P. J., Dammerova, N., Dixon, N. E. & Carazo, J. M. (1995). A structural model for the Escherichia coli DnaB helicase based on electron microscopy data. J. Struct. Biol. 114, 167-176.
    • (1995) J. Struct. Biol. , vol.114 , pp. 167-176
    • San Martin, M.C.1    Stamford, N.P.J.2    Dammerova, N.3    Dixon, N.E.4    Carazo, J.M.5
  • 33
    • 0025836978 scopus 로고
    • Molecular analysis of the TyrR protein-mediated activation of mtr gene expression in Escherichia coli K-12
    • Sarsero, J. P. & Pittard, A. J. (1991). Molecular analysis of the TyrR protein-mediated activation of mtr gene expression in Escherichia coli K-12. J. Bacteriol. 173, 7701-7704.
    • (1991) J. Bacteriol. , vol.173 , pp. 7701-7704
    • Sarsero, J.P.1    Pittard, A.J.2
  • 34
    • 0025768436 scopus 로고
    • Regulation of expression of the Escherichia coli K-12 mtr gene by TyrR protein and Trp repressor
    • Sarsero, J. P., Wookey, P. J. & Pittard, A. J. (1991). Regulation of expression of the Escherichia coli K-12 mtr gene by TyrR protein and Trp repressor. J. Bacteriol. 173, 4133-4143.
    • (1991) J. Bacteriol. , vol.173 , pp. 4133-4143
    • Sarsero, J.P.1    Wookey, P.J.2    Pittard, A.J.3
  • 35
    • 0001607723 scopus 로고
    • Distantly related sequences in the α-and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J. & Gay, N. J. (1982). Distantly related sequences in the α-and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO. J. 8, 945-951.
    • (1982) EMBO. J. , vol.8 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 36
    • 0028263372 scopus 로고
    • Ligand-induced self-association of the Escherichia coli regulatory protein TyrR
    • Wilson, T. J., Maroudas, P., Howlett, G. J. & Davidson, B. E. (1994). Ligand-induced self-association of the Escherichia coli regulatory protein TyrR. J. Mol. Biol. 238, 309-318.
    • (1994) J. Mol. Biol. , vol.238 , pp. 309-318
    • Wilson, T.J.1    Maroudas, P.2    Howlett, G.J.3    Davidson, B.E.4
  • 37
    • 0029144438 scopus 로고
    • Evidence for two aromatic amino acid binding sites, one ATP-dependent and the other ATP-independent, in the Escherichia coli regulatory protein TyrR
    • Wilson, T. J., Argaet, V. P., Howlett, G. J. & Davidson, B. E. (1995). Evidence for two aromatic amino acid binding sites, one ATP-dependent and the other ATP-independent, in the Escherichia coli regulatory protein TyrR. Mol. Microbiol. 17, 483-492.
    • (1995) Mol. Microbiol. , vol.17 , pp. 483-492
    • Wilson, T.J.1    Argaet, V.P.2    Howlett, G.J.3    Davidson, B.E.4
  • 38
    • 0002368922 scopus 로고
    • Concentrative properties of aqueous solutions: Conversion tables
    • (Weast, R. C., Astle, M. J. & Beyer, W. H., eds), CRC Press, Inc, Boca Raton, Florida
    • Wolf, A. V., Brown, M. G. & Prentiss, P. G. (1988). Concentrative properties of aqueous solutions: conversion tables. In CRC Handbook of Chemistry and Physics (Weast, R. C., Astle, M. J. & Beyer, W. H., eds), pp. D-219-D-269, CRC Press, Inc, Boca Raton, Florida.
    • (1988) CRC Handbook of Chemistry and Physics
    • Wolf, A.V.1    Brown, M.G.2    Prentiss, P.G.3
  • 39
    • 0027493444 scopus 로고
    • Mutations in the tyrR gene of Escherichia coli which affect TyrR-mediated activation but not TyrR-mediated repression
    • Yang, J., Camakaris, H. & Pittard, A. J. (1993a). Mutations in the tyrR gene of Escherichia coli which affect TyrR-mediated activation but not TyrR-mediated repression. J. Bacteriol. 175, 6372-6375.
    • (1993) J. Bacteriol. , vol.175 , pp. 6372-6375
    • Yang, J.1    Camakaris, H.2    Pittard, A.J.3
  • 40
    • 0027408011 scopus 로고
    • A genetic analysis of various functions of the TyrR protein of Escherichia coli
    • Yang, J., Ganesan, S., Sarsero, J. & Pittard, A. J. (1993b). A genetic analysis of various functions of the TyrR protein of Escherichia coli. J. Bacteriol. 175, 1767-1776.
    • (1993) J. Bacteriol. , vol.175 , pp. 1767-1776
    • Yang, J.1    Ganesan, S.2    Sarsero, J.3    Pittard, A.J.4


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