메뉴 건너뛰기




Volumn 256, Issue 5, 1996, Pages 889-896

In vivo interaction between mutated tryptophan repressors of Escherichia coli

Author keywords

Corepressor binding pocket; In vivo properties of amino acids; Intragenic complementation; Site directed mutagenesis; Tryptophan analogues

Indexed keywords

AMINO ACID; REPRESSOR PROTEIN; TRYPTOPHAN;

EID: 0029983551     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0135     Document Type: Article
Times cited : (2)

References (50)
  • 1
    • 0026015213 scopus 로고
    • The solution structures of Escherichia coli trp repressor and trp aporepressor at an intermediate resolution
    • Arrowsmith, C., Pachter, R., Altman, R. & Jardetzky, O. (1991). The solution structures of Escherichia coli trp repressor and trp aporepressor at an intermediate resolution. Eur. J. Biochem. 202, 53-66.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 53-66
    • Arrowsmith, C.1    Pachter, R.2    Altman, R.3    Jardetzky, O.4
  • 2
    • 0025825019 scopus 로고
    • Mutant tryptophan aporepressors with altered specificities of corepressor recognition
    • Arvidson, D. N., Shapiro, M. & Youderian, P. (1991). Mutant tryptophan aporepressors with altered specificities of corepressor recognition. Genetics, 128, 29-35.
    • (1991) Genetics , vol.128 , pp. 29-35
    • Arvidson, D.N.1    Shapiro, M.2    Youderian, P.3
  • 5
    • 0024286247 scopus 로고
    • Mutant trp repressors with new DNA-binding specificities
    • Bass, S., Sorrells, V. & Youderian, P (1988). Mutant trp repressors with new DNA-binding specificities. Science, 242, 240-245.
    • (1988) Science , vol.242 , pp. 240-245
    • Bass, S.1    Sorrells, V.2    Youderian, P.3
  • 6
    • 0027236794 scopus 로고
    • Structural basis of amino acid α helix propensity
    • Blaber, M., Zhang, X.-J. & Matthews, B. W. (1993). Structural basis of amino acid α helix propensity. Science, 260, 1637-1640.
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zhang, X.-J.2    Matthews, B.W.3
  • 7
    • 85030194389 scopus 로고
    • Boehringer Mannheim, Germany
    • Boehringer Mannheim (1994). Biochemical Catalogue. pp. 205 and 453, Boehringer Mannheim, Germany.
    • (1994) Biochemical Catalogue , pp. 205
    • Mannheim, B.1
  • 9
    • 0026042785 scopus 로고
    • Determination of the orientations of tryptophan analogues bound to the trp repressor and the relationship to activation. (1991)
    • Borden, K. L. B., Beckman, P. & Lane, A. N. (1991). Determination of the orientations of tryptophan analogues bound to the trp repressor and the relationship to activation. (1991). Eur. J. Biochem. 202, 459-470.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 459-470
    • Borden, K.L.B.1    Beckman, P.2    Lane, A.N.3
  • 10
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
    • Chang, A. C. Y. & Cohen, S. N. (1978). Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J. Bacteriol. 134, 1141-1166.
    • (1978) J. Bacteriol. , vol.134 , pp. 1141-1166
    • Chang, A.C.Y.1    Cohen, S.N.2
  • 11
    • 0024418115 scopus 로고
    • Serine to cysteine mutations in Trp repressor protein alter tryptophan and operator binding
    • Chou, W.-Y. & Matthews, K. S. (1989). Serine to cysteine mutations in Trp repressor protein alter tryptophan and operator binding. J. Biol. Chem. 264, 18314-18319.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18314-18319
    • Chou, W.-Y.1    Matthews, K.S.2
  • 12
    • 0025249285 scopus 로고
    • Conversion of a helix-turn-helix motif sequence-specific DNA binding into a site-specific DNA cleavage agent
    • Ebright, R. H., Ebright, Y. W., Pendergast, P. S. & Gunasekera, A. (1990). Conversion of a helix-turn-helix motif sequence-specific DNA binding into a site-specific DNA cleavage agent. Proc. Natl Acad. Sci. USA, 87, 2882-2886.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 2882-2886
    • Ebright, R.H.1    Ebright, Y.W.2    Pendergast, P.S.3    Gunasekera, A.4
  • 13
    • 0342464061 scopus 로고
    • European Division, Glasgow, Scotland
    • Gibco BRL (1992). Product Catalog, p. 62, European Division, Glasgow, Scotland.
    • (1992) Product Catalog , pp. 62
    • Gibco, B.R.L.1
  • 14
    • 0024238064 scopus 로고
    • Formation of heterodimers between wild-type and mutant trp aporepressor polypeptides of Escherichia coli
    • Graddis, T. J., Klig, L. S., Yanofsky, C. & Oxender, D. L. (1988). Formation of heterodimers between wild-type and mutant trp aporepressor polypeptides of Escherichia coli. Proteins: Struct. Funct. Genet. 4, 173-181.
    • (1988) Proteins: Struct. Funct. Genet. , vol.4 , pp. 173-181
    • Graddis, T.J.1    Klig, L.S.2    Yanofsky, C.3    Oxender, D.L.4
  • 15
    • 0023237755 scopus 로고
    • Regulation of the aroh operon of Escherichia coli by tryptophan repressor
    • Grove, C. L. & Gunsalus, R. P. (1987). Regulation of the aroH operon of Escherichia coli by tryptophan repressor. J. Bacteriol. 169, 2158-2164.
    • (1987) J. Bacteriol. , vol.169 , pp. 2158-2164
    • Grove, C.L.1    Gunsalus, R.P.2
  • 16
    • 0011023559 scopus 로고
    • Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor
    • Gunsalus, R. P. & Yanofsky, C. (1980). Nucleotide sequence and expression of Escherichia coli trpR, the structural gene for the trp aporepressor. Proc. Natl Acad. Sci. USA, 77, 7117-7121.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 7117-7121
    • Gunsalus, R.P.1    Yanofsky, C.2
  • 17
    • 0025016918 scopus 로고
    • Effect of amino acid alterations in the tryptophan-binding site of the Trp repressor
    • He, J.-J. & Matthews, K. S. (1990). Effect of amino acid alterations in the tryptophan-binding site of the Trp repressor. J. Biol. Chem. 265, 731-737.
    • (1990) J. Biol. Chem. , vol.265 , pp. 731-737
    • He, J.-J.1    Matthews, K.S.2
  • 18
    • 0025957686 scopus 로고
    • Cloning, nucleotide sequence and characterization of mtr, the structural gene for a tryptophan-specific permease of Escherichia coli K12
    • Heatwole, V. M. & Somerville, R. L. (1991). Cloning, nucleotide sequence and characterization of mtr, the structural gene for a tryptophan-specific permease of Escherichia coli K12. J. Bacteriol. 173, 108-115.
    • (1991) J. Bacteriol. , vol.173 , pp. 108-115
    • Heatwole, V.M.1    Somerville, R.L.2
  • 19
    • 0026525555 scopus 로고
    • Synergism between the Trp repressor and Tyr repressor in repression of the aroL promoter of Escherichia coli K-12
    • Heatwole, V. M. & Somerville, R. L. (1992). Synergism between the Trp repressor and Tyr repressor in repression of the aroL promoter of Escherichia coli K-12. J. Bacteriol. 174, 331-335.
    • (1992) J. Bacteriol. , vol.174 , pp. 331-335
    • Heatwole, V.M.1    Somerville, R.L.2
  • 20
    • 0027168732 scopus 로고
    • Analysis of heterodimer formation by the Eschericha coli trp repressor
    • Hurlburt, B. K. & Yanofsky, C. (1993). Analysis of heterodimer formation by the Eschericha coli trp repressor. J. Biol. Chem. 268, 14794-14798.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14794-14798
    • Hurlburt, B.K.1    Yanofsky, C.2
  • 21
    • 0025675856 scopus 로고
    • High efficiency transformation of E. coli with plasmids
    • Inoue, H., Nojima, H. & Okayama, H. (1990). High efficiency transformation of E. coli with plasmids. Gene, 26, 23-28.
    • (1990) Gene , vol.26 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 22
    • 0028157348 scopus 로고
    • Mutagenesis supports water mediated recognition in the trp repressor-operator system
    • 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
  • 23
    • 0019933970 scopus 로고
    • Trp aporepressor production is controlled by autogenous regulation and inefficient translation
    • Kelley, R. L. & Yanofsky, C. (1982). Trp aporepressor 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
  • 24
    • 0021988066 scopus 로고
    • Mutational studies with the trp repressor Escherichia coli support the helix-turn-helix model of repressor recognition of operator DNA
    • Kelley, R. L. & Yanofsky, C. (1985). Mutational studies with the trp repressor Escherichia coli support the helix-turn-helix model of repressor recognition of operator DNA. Proc. Natl Acad. Sci. USA, 82, 483-487.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 483-487
    • Kelley, R.L.1    Yanofsky, C.2
  • 25
    • 0023701043 scopus 로고
    • Second site revertants of Escherichia coli Trp repressor mutants
    • Klig, L. S., Oxender, D. L. & Yanofsky, C. (1988). Second site revertants of Escherichia coli Trp repressor mutants. Genetics, 120, 651-655.
    • (1988) Genetics , vol.120 , pp. 651-655
    • Klig, L.S.1    Oxender, D.L.2    Yanofsky, C.3
  • 26
    • 0028173096 scopus 로고
    • Glycine 85 of the trp-repressor of E. coli is important in forming the hydrophobic tryptophan binding pocket: Experimental and computational approaches
    • Komeiji, K., Izumi, F., Honda, N., Tsutsui, M., Tamura, T. & Yamato, I. (1994). Glycine 85 of the trp-repressor of E. coli is important in forming the hydrophobic tryptophan binding pocket: experimental and computational approaches. Protein Eng. 7, 1239-1247.
    • (1994) Protein Eng. , vol.7 , pp. 1239-1247
    • Komeiji, K.1    Izumi, F.2    Honda, N.3    Tsutsui, M.4    Tamura, T.5    Yamato, I.6
  • 27
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., Roberts, J. D. & Zakour, R. A. (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.A.3
  • 28
    • 0027372621 scopus 로고
    • Tandem binding in crystals of a trp repressor/operator half-site complex
    • Lawson, C. L. & Carey, J. (1993). Tandem binding in crystals of a trp repressor/operator half-site complex. Nature, 366, 178-182.
    • (1993) Nature , vol.366 , pp. 178-182
    • Lawson, C.L.1    Carey, J.2
  • 29
    • 0024300177 scopus 로고
    • The structure of trp pseudorepressor at 1.65 A shows why indole propionate act as a trp inducer
    • Lawson, C. L. & Sigler, P. B. (1988). The structure of trp pseudorepressor at 1.65 A shows why indole propionate act as a trp inducer. Nature, 333, 869-871.
    • (1988) Nature , vol.333 , pp. 869-871
    • Lawson, C.L.1    Sigler, P.B.2
  • 31
    • 0025363526 scopus 로고
    • The stereochemistry and biochemistry of the trp repressor-operator complex
    • Luisi, B. F. & Sigler, P. B. (1990). The stereochemistry and biochemistry of the trp repressor-operator complex. Biochim. Biophys. Acta, 1048, 113-126.
    • (1990) Biochim. Biophys. Acta , vol.1048 , pp. 113-126
    • Luisi, B.F.1    Sigler, P.B.2
  • 32
    • 0024474711 scopus 로고
    • Stereochemical effects of L-tryptophan and its analogues on trp repressors affinity for operator-DNA
    • Marmorstein, R. Q. & Sigler, P. B. (1989). Stereochemical effects of L-tryptophan and its analogues on trp repressors affinity for operator-DNA. J. Biol. Chem. 264, 9149-9154.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9149-9154
    • Marmorstein, R.Q.1    Sigler, P.B.2
  • 33
    • 0023176802 scopus 로고
    • The structural basis for the interaction between L-tryptophan and the Escherichia coli Trp aporepressor
    • Marmorstein, R. Q., Joachimiak, A., Sprinzl, M. & Sigler, P. B. (1987). The structural basis for the interaction between L-tryptophan and the Escherichia coli Trp aporepressor. J. Biol. Chem. 262, 4922-4927.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4922-4927
    • Marmorstein, R.Q.1    Joachimiak, A.2    Sprinzl, M.3    Sigler, P.B.4
  • 34
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. H. (1972). Experiments in Molecular Genetics, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 37
    • 0026682657 scopus 로고
    • Transcription factors: Structural families and principles of DNA recognition
    • Pabo, C. O. & Sauer, R. T. (1992). Transcription factors: structural families and principles of DNA recognition. Annu. Rev. Biochem. 61, 1053-1095.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1053-1095
    • Pabo, C.O.1    Sauer, R.T.2
  • 39
    • 0027248706 scopus 로고
    • Engineering multiple properties of a protein by combinatorial mutagenesis
    • Sandberg, W. S. & Terwilliger, T. C. (1993). Engineering multiple properties of a protein by combinatorial mutagenesis. Proc. Natl Acad. Sci. USA, 90, 8367-8371.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8367-8371
    • Sandberg, W.S.1    Terwilliger, T.C.2
  • 41
    • 0025768436 scopus 로고
    • Regulation of expression of the E. 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 E. 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
  • 43
    • 0026753266 scopus 로고
    • Intragenic complementation between Escherichia coli Trp-repressors with different defects in the tryptophan-binding pocket
    • Storbakk, N., Oxender, D. L. & El-Gewely, M. R. (1992). Intragenic complementation between Escherichia coli Trp-repressors with different defects in the tryptophan-binding pocket. Gene, 117, 23-29.
    • (1992) Gene , vol.117 , pp. 23-29
    • Storbakk, N.1    Oxender, D.L.2    El-Gewely, M.R.3
  • 44
    • 0023785887 scopus 로고
    • A multisite mutagenesis using T7 DNA polymerase: Application for reconstructing a mammalian gene
    • Su, T.-Z. & El-Gewely, M. R. (1988). A multisite mutagenesis using T7 DNA polymerase: application for reconstructing a mammalian gene. Gene, 69, 81-91.
    • (1988) Gene , vol.69 , pp. 81-91
    • Su, T.-Z.1    El-Gewely, M.R.2
  • 45
    • 0027269748 scopus 로고
    • Transforming the Escherichia coli Trp repressor into a site-specific nuclease
    • Sutton, C. L., Mazumder, A., Chen, C. 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.B.3    Sigman, D.S.4
  • 46
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli: Partial purification and some properties
    • Vogel, H. J. & Bonner, D. H. (1956). Acetylornithinase of Escherichia coli: partial purification and some properties. J. Biol. Chem. 218, 97-106.
    • (1956) J. Biol. Chem. , vol.218 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.H.2
  • 47
    • 0026078753 scopus 로고
    • Fast recovery of DNA from agarose gels by centrifugation through blotting paper
    • Weichenhan, D. (1991). Fast recovery of DNA from agarose gels by centrifugation through blotting paper. Trends Genet. 7, 109.
    • (1991) Trends Genet. , vol.7 , pp. 109
    • Weichenhan, D.1
  • 48
    • 0019495739 scopus 로고
    • Rifampicin resistance mutations that alter the efficiency of transcription termination at the tryptophan attenuator
    • Yanofsky, C. & Horn, V. (1981). Rifampicin resistance mutations that alter the efficiency of transcription termination at the tryptophan attenuator. J. Bacteriol. 145, 1334-1341.
    • (1981) J. Bacteriol. , vol.145 , pp. 1334-1341
    • Yanofsky, C.1    Horn, V.2
  • 49
    • 0023256884 scopus 로고
    • The crystal structure of Trp-aporepressor at 1.8 A shows how binding tryptophan enhances DNA affinity
    • 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 A shows how binding tryptophan enhances DNA affinity Nature, 327, 591-597.
    • (1987) Nature , 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
  • 50
    • 0027528411 scopus 로고
    • Refined solution structures of the Escherichia coli trp holo- and aporepressor
    • Zhao, D., Arrowsmith, C. H., Jia, X. & Jardetzky, O. (1993). Refined solution structures of the Escherichia 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.