메뉴 건너뛰기




Volumn 265, Issue 3, 1999, Pages 919-928

Studies of the Escherichia coli Trp repressor binding to its five operators and to variant operator sequences

Author keywords

DNA binding; Tandem binding; Trp operator; Trp repressor

Indexed keywords

ARTICLE; DNA BINDING; ESCHERICHIA COLI; GENE SEQUENCE; NONHUMAN; OPERATOR GENE; PRIORITY JOURNAL; REPRESSOR GENE; SEQUENCE ANALYSIS; STOICHIOMETRY;

EID: 0012099926     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00792.x     Document Type: Article
Times cited : (22)

References (48)
  • 1
    • 0026466672 scopus 로고
    • The trp repressor, a ligand activated regulatory protein
    • 1. Somerville, R. (1992) The trp repressor, a ligand activated regulatory protein. Prog. Nucleic Acid Res. Mol. Biol. 42, 1-38.
    • (1992) Prog. Nucleic Acid Res. Mol. Biol. , vol.42 , pp. 1-38
    • Somerville, R.1
  • 2
    • 0015901225 scopus 로고
    • Regulation of in vitro transcription of the tryptophan operon by purified RNA polymerase in the presence of partially purified repressor and tryptophan
    • 2. Rose, J.K., Squires, C.L., Yanofsky, C., Yang, H. & Zubay, G. (1973) Regulation of in vitro transcription of the tryptophan operon by purified RNA polymerase in the presence of partially purified repressor and tryptophan. Nature New Biol. 245, 133-137.
    • (1973) Nature New Biol. , vol.245 , pp. 133-137
    • Rose, J.K.1    Squires, C.L.2    Yanofsky, C.3    Yang, H.4    Zubay, G.5
  • 3
    • 0017185637 scopus 로고
    • Nucleotide sequence of region preceding trp mRNA initiation site and its role in promoter and operator function
    • 3. Bennett, G.N., Schweingruber, M.E., Brown, K.D., Squires, C. & Yanofsky, C. (1976) Nucleotide sequence of region preceding trp mRNA initiation site and its role in promoter and operator function. Proc. Natl Acad. Sci. USA 73, 2351-2355.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 2351-2355
    • Bennett, G.N.1    Schweingruber, M.E.2    Brown, K.D.3    Squires, C.4    Yanofsky, C.5
  • 4
    • 0011023559 scopus 로고
    • Nucleotide sequence and expression of Escherichia coli Trp repressor, the structural gene for the Trp aporepressor
    • 4. Gunsalus, R.P. & Yanofsky, C. (1980) Nucleotide sequence and expression of Escherichia coli Trp repressor, the structural gene for the Trp aporepressor. Proc. Natl. Acad. Sci. USA 77, 7117-71221.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 7117-71221
    • Gunsalus, R.P.1    Yanofsky, C.2
  • 5
    • 0019933970 scopus 로고
    • Trp aporepresor production is controlled by autogenous regulation and inefficient translation
    • 5. Kelley, R.L. & Yanofsky, C. (1982) Trp aporepresor production is controlled by autogenous regulation and inefficient translation. Proc. Natl. Acad. Sci. USA 79, 3120-3124.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3120-3124
    • Kelley, R.L.1    Yanofsky, C.2
  • 6
    • 0019382235 scopus 로고
    • Structure and regulation of aroH, the structural gene for the tryptophan-repressible 3-deoxy-D-arabino-heptulosonic acid-7-phosphate synthetase of Escherichia coli
    • 6. Zurawski, G., Gunsalus, R.P., Brown, K.D. & Yanofsky, C. (1981) Structure and regulation of aroH, the structural gene for the tryptophan-repressible 3-deoxy-D-arabino-heptulosonic acid-7-phosphate synthetase of Escherichia coli. J. Mol. Biol. 145, 47-73.
    • (1981) J. Mol. Biol. , vol.145 , pp. 47-73
    • Zurawski, G.1    Gunsalus, R.P.2    Brown, K.D.3    Yanofsky, C.4
  • 7
    • 0023237755 scopus 로고
    • Regulation of the aroH operon of Escherichia coli by the Tryptophan repressor
    • 7. Grove, C.L. & Gunsalus, R.P. (1987) Regulation of the aroH operon of Escherichia coli by the Tryptophan repressor. J. Bacterial. 169, 2158-2164.
    • (1987) J. Bacterial. , vol.169 , pp. 2158-2164
    • Grove, C.L.1    Gunsalus, R.P.2
  • 8
    • 0025833020 scopus 로고
    • The tryptophan-specific permease gene, mtr, is differentially regulated by the tryptophan and tyrosine repressors in E. coli K12
    • 8. Heatwole, V.M. & Somerville, R.L. (1991). The tryptophan-specific permease gene, mtr, is differentially regulated by the tryptophan and tyrosine repressors in E. coli K12. J. Bacteriol. 174, 3601-3604.
    • (1991) J. Bacteriol. , vol.174 , pp. 3601-3604
    • Heatwole, V.M.1    Somerville, R.L.2
  • 9
    • 0025768436 scopus 로고
    • Regulation of the expression of Escherichia coli K12 mtr gene by TyrR protein and trp repressor
    • 9. Sarsero, J.P., Wookey, P.J. & Pittard, A.J. (1991) Regulation of the expression of Escherichia coli K12 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
  • 10
    • 0026525555 scopus 로고
    • Synergism between the trp repressor and tyr repressor in repression of the arol promoter of Escherichia coli K12
    • 10. Heatwole, V.M. & Somerville, R.L. (1992). Synergism between the trp repressor and tyr repressor in repression of the aroL promoter of Escherichia coli K12. J. Bacteriol 174, 331-335.
    • (1992) J. Bacteriol , vol.174 , pp. 331-335
    • Heatwole, V.M.1    Somerville, R.L.2
  • 11
    • 0027987492 scopus 로고
    • Regulation of aroL expression by TyrR protein and Trp repressor in E. coli K12
    • 11. Lawley, B. & Pittard, A.J. (1994) Regulation of aroL expression by TyrR protein and Trp repressor in E. coli K12. J. Bacteriol. 176, 6921-6930.
    • (1994) J. Bacteriol. , vol.176 , pp. 6921-6930
    • Lawley, B.1    Pittard, A.J.2
  • 12
    • 0023811599 scopus 로고
    • Trp repressor interactions with the trp, aroH, and trpR operators
    • 12. Klig, L.S., Carey, J. & Yanofsky, C. (1988) Trp repressor interactions with the trp, aroH, and trpR operators. J. Mol. Biol. 202, 769-777.
    • (1988) J. Mol. Biol. , vol.202 , pp. 769-777
    • Klig, L.S.1    Carey, J.2    Yanofsky, C.3
  • 15
    • 0027528411 scopus 로고
    • Refined solution structures of the Escherichai coli trp holo-and aporepressor
    • 15. Zhao, D., Arrowsmith, C.H., Jia, X. & Jardetzky, O. (1993) Refined solution structures of the Escherichai coli trp holo-and aporepressor. J. Mol. Biol. 229, 735-746.
    • (1993) J. Mol. Biol. , vol.229 , pp. 735-746
    • Zhao, D.1    Arrowsmith, C.H.2    Jia, X.3    Jardetzky, O.4
  • 16
    • 0023256884 scopus 로고
    • The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA specificity
    • 16. Zhang, R.-G., Joachimiak, A., Lawson, C.L., Schevitz, R.W., Otwinowski, Z. & Sigler, P.B. (1987) The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA specificity. Nature (London) 327, 591-597.
    • (1987) Nature (London) , vol.327 , pp. 591-597
    • Zhang, R.-G.1    Joachimiak, A.2    Lawson, C.L.3    Schevitz, R.W.4    Otwinowski, Z.5    Sigler, P.B.6
  • 21
    • 0023389549 scopus 로고
    • DNA specificity determinants of Escherichia coli trytophan repressor binding
    • 21. Bass, S., Sugiono, P., Arvidson, D.N., Gunsalus, R.P. & Youderian, P. (1987). DNA specificity determinants of Escherichia coli trytophan repressor binding. Genes Dev. 1, 565-572.
    • (1987) Genes Dev. , vol.1 , pp. 565-572
    • Bass, S.1    Sugiono, P.2    Arvidson, D.N.3    Gunsalus, R.P.4    Youderian, P.5
  • 23
    • 0026343607 scopus 로고
    • How does trp repressor bind to its operator?
    • 23. Carey, J., Lewis, D.E.A., Lavoie, T.A. & Yang, J. (1991). How does trp repressor bind to its operator? J. Biol. Chem. 266, 24509-24513.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24509-24513
    • Carey, J.1    Lewis, D.E.A.2    Lavoie, T.A.3    Yang, J.4
  • 24
    • 0026652596 scopus 로고
    • The DNA target of the trp repressor
    • 24. Haran, T.E., Joachimiak, A. & Sigler, P.B. (1992). The DNA target of the trp repressor. EMBO J. 11, 3021-3030.
    • (1992) EMBO J. , vol.11 , pp. 3021-3030
    • Haran, T.E.1    Joachimiak, A.2    Sigler, P.B.3
  • 25
    • 0027370156 scopus 로고
    • Dependence of trp repressor-operator affinity, stoichiometry, and apparent cooperativity on DNA sequence and size
    • 25. Liu, Y.-C. & Matthews, K.S. (1993) Dependence of trp repressor-operator affinity, stoichiometry, and apparent cooperativity on DNA sequence and size. J. Biol. Chem. 268, 23239-23249.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23239-23249
    • Liu, Y.-C.1    Matthews, K.S.2
  • 26
    • 0027374430 scopus 로고
    • Trp repressor interaction with bromodeoxyuridine-substituted operators alters UV-induced perturbation pattern in a sequence dependent manner
    • 26. Liu, Y.-C. & Matthews, K.S. (1993) Trp repressor interaction with bromodeoxyuridine-substituted operators alters UV-induced perturbation pattern in a sequence dependent manner. Biochemistry 32, 10532-10542.
    • (1993) Biochemistry , vol.32 , pp. 10532-10542
    • Liu, Y.-C.1    Matthews, K.S.2
  • 27
    • 0028175286 scopus 로고
    • Trp repressor mutations alter DNA complex stoichiometry
    • 27. Liu, Y.-C. & Matthews, K.S. (1994) Trp repressor mutations alter DNA complex stoichiometry. J. Biol. Chem. 269, 1692-1698.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1692-1698
    • Liu, Y.-C.1    Matthews, K.S.2
  • 28
    • 0028283502 scopus 로고
    • A thermodynamic study of the trp repressor-operator interaction
    • 28. Ladbury, J.E., Wright, J.G., Sturtevant, J.M. & Sigler, P.B. (1994) A thermodynamic study of the trp repressor-operator interaction. J. Mol. Biol. 238, 669-681.
    • (1994) J. Mol. Biol. , vol.238 , pp. 669-681
    • Ladbury, J.E.1    Wright, J.G.2    Sturtevant, J.M.3    Sigler, P.B.4
  • 29
    • 0029988059 scopus 로고    scopus 로고
    • Co-operative binding of two trp repressor dimers to α-or β-centered trp operators
    • 29. Gunes, C., von Staake, D., Wilken-Bergman, B. & Muller-Hill, B. (1996) Co-operative binding of two Trp repressor dimers to α-or β-centered trp operators. Mol. Microbiol. 20, 375-384.
    • (1996) Mol. Microbiol. , vol.20 , pp. 375-384
    • Gunes, C.1    Von Staake, D.2    Wilken-Bergman, B.3    Muller-Hill, B.4
  • 30
    • 0031582053 scopus 로고    scopus 로고
    • Repressor assembly at trp binding sites is dependent on the identity of the intervening dinucleotide between the binding half sites
    • 30. Bareket-Samish, A., Cohen, I. & Haran, T.E. (1997) Repressor assembly at trp binding sites is dependent on the identity of the intervening dinucleotide between the binding half sites. J. Mol. Biol. 267, 103-117.
    • (1997) J. Mol. Biol. , vol.267 , pp. 103-117
    • Bareket-Samish, A.1    Cohen, I.2    Haran, T.E.3
  • 31
    • 0032540302 scopus 로고    scopus 로고
    • Direct versus indirect readout in the interaction of the trp repressor with non-canonical sites
    • 31. Bareket-Samish, A., Cohen, I. & Haran, T.E. (1998) Direct versus indirect readout in the interaction of the trp repressor with non-canonical sites. J. Mol. Biol. 277, 1071-1080.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1071-1080
    • Bareket-Samish, A.1    Cohen, I.2    Haran, T.E.3
  • 32
    • 0031592940 scopus 로고    scopus 로고
    • Affinity and specificity of trp repressor-DNA interactions studied with fluorescent oligonucleotides
    • 32. Reedstrom, R.J., Brown, M.P., Grillo, A., Roen, D. & Royer, C.A. (1997) Affinity and specificity of trp repressor-DNA interactions studied with fluorescent oligonucleotides. J. Mol. Biol. 2773, 572-585.
    • (1997) J. Mol. Biol. , vol.2773 , pp. 572-585
    • Reedstrom, R.J.1    Brown, M.P.2    Grillo, A.3    Roen, D.4    Royer, C.A.5
  • 33
    • 0030922055 scopus 로고    scopus 로고
    • Probing contacts to the DNA backbone in the trp repressor-operator sequence-specific protein-nucleic acid complex using diastereomic methylphosphonate analogues
    • 33. Smith, S.A. & McLaughlin, L.W. (1997) Probing contacts to the DNA backbone in the trp repressor-operator sequence-specific protein-nucleic acid complex using diastereomic methylphosphonate analogues. Biochemistry 36, 6046-6058.
    • (1997) Biochemistry , vol.36 , pp. 6046-6058
    • Smith, S.A.1    McLaughlin, L.W.2
  • 34
    • 0033515527 scopus 로고    scopus 로고
    • Probing the physical basis for trp repressor-operator recognition
    • 34. Grillo, A.O., Brown, M.P. & Royer, C.A. (1999) Probing the physical basis for trp repressor-operator recognition. J. Mol. Biol. 287, 539-554.
    • (1999) J. Mol. Biol. , vol.287 , pp. 539-554
    • Grillo, A.O.1    Brown, M.P.2    Royer, C.A.3
  • 35
    • 0026710960 scopus 로고
    • Interactions between the trp repressor and its operator sequence as studies by base analogue substitution
    • 35. Mazzarelli, J.M., Rajur, S.B., Iadarola, P.L. & McLaughlin, L.W. (1992) Interactions between the trp repressor and its operator sequence as studies by base analogue substitution. Biochemistry 31, 5926-5935.
    • (1992) Biochemistry , vol.31 , pp. 5926-5935
    • Mazzarelli, J.M.1    Rajur, S.B.2    Iadarola, P.L.3    McLaughlin, L.W.4
  • 37
    • 0027998091 scopus 로고
    • Functional selection and characterisation of DNA binding sites for trp repressor of Escherichia coli
    • 37. Czernick, P., Shin, D.S. & Hurlburt, B.K. (1994). Functional selection and characterisation of DNA binding sites for trp repressor of Escherichia coli. J. Biol. Chem. 269, 227869-227875.
    • (1994) J. Biol. Chem. , vol.269 , pp. 227869-227875
    • Czernick, P.1    Shin, D.S.2    Hurlburt, B.K.3
  • 38
    • 0027372621 scopus 로고
    • Tandem binding in crystals of a trp repressor/operator half site complex
    • 38. Lawson, C.L. & Carey, J. (1993). Tandem binding in crystals of a trp repressor/operator half site complex. Nature (London) 366, 178-182.
    • (1993) Nature (London) , vol.366 , pp. 178-182
    • Lawson, C.L.1    Carey, J.2
  • 39
    • 0023056195 scopus 로고
    • High level production and rapid purification of the E. Coli trp repressor
    • 39. Paluh, J.L. & Yanofsky, C. (1986) High level production and rapid purification of the E. coli trp repressor. Nucleic Acids Res. 14, 7851-7860.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 7851-7860
    • Paluh, J.L.1    Yanofsky, C.2
  • 42
    • 0023955176 scopus 로고
    • Gel retardation at low pH resolves trp repressor-DNA complexes for quantitative study
    • 42. Carey, J. (1988) Gel retardation at low pH resolves trp repressor-DNA complexes for quantitative study. Proc. Natl Acad. Sci. USA 85, 975-979.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 975-979
    • Carey, J.1
  • 43
    • 0026035470 scopus 로고
    • An alkaline phosphatase protection assay to investigate trp repressor/operator interactions
    • 43. Marmorstein, R.Q., Sprinzl, M. & Sigler, P.B. (1991) An alkaline phosphatase protection assay to investigate trp repressor/operator interactions. Biochemistry 30, 1141 -1148.
    • (1991) Biochemistry , vol.30 , pp. 1141-1148
    • Marmorstein, R.Q.1    Sprinzl, M.2    Sigler, P.B.3
  • 44
    • 0027973633 scopus 로고
    • Direct recognition of the trp operator by the trp holorepressor: A review
    • 44. Youderian, Y. & Arvidson, D.N. (1994) Direct recognition of the trp operator by the trp holorepressor: a review. Gene 150, 1-8.
    • (1994) Gene , vol.150 , pp. 1-8
    • Youderian, Y.1    Arvidson, D.N.2
  • 46
    • 0023389847 scopus 로고
    • E. Coli tryptophan repressor binds multiple sites within the aroH and trp operators
    • 46. Kumamoto, A., Miller, W. & Gunsalus, R.P. (1987) E. coli tryptophan repressor binds multiple sites within the aroH and trp operators. Genes Dev. 1, 556-564.
    • (1987) Genes Dev. , vol.1 , pp. 556-564
    • Kumamoto, A.1    Miller, W.2    Gunsalus, R.P.3
  • 47
    • 0027269748 scopus 로고
    • Transforming the Escherichia coli Trp repressor into a site-specific nuclease
    • 47. Sutton, C.L., Mazumder, A., Chen, C.-H.B. & Sigman, D.S. (1993) Transforming the Escherichia coli Trp repressor into a site-specific nuclease. Biochemistry 32, 4225-4230.
    • (1993) Biochemistry , vol.32 , pp. 4225-4230
    • Sutton, C.L.1    Mazumder, A.2    Chen, C.-H.B.3    Sigman, D.S.4
  • 48
    • 0028157348 scopus 로고
    • Mutagenesis supports water-mediated recognition in the trp repressor-operator system
    • 48. Joachimiak, A., Haran, T.E. & Sigler, P.B. (1994). Mutagenesis supports water-mediated recognition in the trp repressor-operator system. EMBO J. 13, 367-372.
    • (1994) EMBO J. , vol.13 , pp. 367-372
    • Joachimiak, A.1    Haran, T.E.2    Sigler, P.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.