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Volumn 35, Issue 6, 2000, Pages 1394-1404

Mutational analysis of MarR, the negative regulator of marRAB expression in Escherichia coli, suggests the presence of two regions required for DNA binding

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; REGULATOR PROTEIN; REPRESSOR PROTEIN;

EID: 0034107895     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2000.01802.x     Document Type: Article
Times cited : (82)

References (50)
  • 2
    • 0000148162 scopus 로고    scopus 로고
    • Regulation of chromosomally mediated multiple antibiotic resistance: The mar regulon
    • Alekshun, M.N., and Levy, S.B. (1997) Regulation of chromosomally mediated multiple antibiotic resistance: the mar regulon. Antimicrob Agents Chemother 10: 2067-2075.
    • (1997) Antimicrob Agents Chemother , vol.10 , pp. 2067-2075
    • Alekshun, M.N.1    Levy, S.B.2
  • 3
    • 0032792553 scopus 로고    scopus 로고
    • Alteration of the repressor activity of MarR, the negative regulator of the Escherichia coli mar locus, by multiple chemicals in vitro
    • Alekshun, M.N., and Levy, S.B. (1999a) Alteration of the repressor activity of MarR, the negative regulator of the Escherichia coli mar locus, by multiple chemicals in vitro. J Bacteriol 181: 4669-4672.
    • (1999) J Bacteriol , vol.181 , pp. 4669-4672
    • Alekshun, M.N.1    Levy, S.B.2
  • 4
    • 0032955054 scopus 로고    scopus 로고
    • Characterization of MarR superrepressor mutants
    • Alekshun, M.N., and Levy, S.B. (1999b) Characterization of MarR superrepressor mutants. J Bacteriol 181: 3303-3306.
    • (1999) J Bacteriol , vol.181 , pp. 3303-3306
    • Alekshun, M.N.1    Levy, S.B.2
  • 5
    • 0027954601 scopus 로고
    • Repressor mutations in the marRAB operon that activate oxidative stress genes and multiple antibiotic resistance in Escherichia coli
    • Ariza, R.R., Cohen, S.P., Bachhawat, N., Levy, S.B., and Demple, B. (1994) Repressor mutations in the marRAB operon that activate oxidative stress genes and multiple antibiotic resistance in Escherichia coli. J Bacteriol 176: 143-148.
    • (1994) J Bacteriol , vol.176 , pp. 143-148
    • Ariza, R.R.1    Cohen, S.P.2    Bachhawat, N.3    Levy, S.B.4    Demple, B.5
  • 6
    • 0031003863 scopus 로고    scopus 로고
    • Organic solvent tolerance and antibiotic resistance increased by overexpression of marA in Escherichia coli
    • Asako, H., Nakajima, H., Kobayashi, K., Kobayashi, M., and Aono, R. (1997) Organic solvent tolerance and antibiotic resistance increased by overexpression of marA in Escherichia coli. Appl Environ Microbiol 63: 1428-1433.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 1428-1433
    • Asako, H.1    Nakajima, H.2    Kobayashi, K.3    Kobayashi, M.4    Aono, R.5
  • 7
    • 0023644937 scopus 로고
    • Affinities of tight-binding lactose repressors for wild-type and pseudo-operators
    • Betz, J. L. (1987) Affinities of tight-binding lactose repressors for wild-type and pseudo-operators. J Mol Biol 195: 495-504.
    • (1987) J Mol Biol , vol.195 , pp. 495-504
    • Betz, J.L.1
  • 8
    • 0004204457 scopus 로고
    • DNA recognition by proteins with the helix-turn-helix motif
    • Branden, C., and Tooze, J. (eds). New York: Garland Publishing
    • Branden, C., and Tooze, J. (1991) DNA recognition by proteins with the helix-turn-helix motif. In Introduction to Protein Structure. Branden, C., and Tooze, J. (eds). New York: Garland Publishing, pp. 85-110.
    • (1991) Introduction to Protein Structure , pp. 85-110
    • Branden, C.1    Tooze, J.2
  • 9
    • 0025336625 scopus 로고
    • Structure of Arc repressor in solution: Evidence for a family of β-sheet proteins
    • Breg, J.N., van Opheusden, J.H.J., Burgering, M.J.M., Boelens, R., and Kaptein, R. (1990) Structure of Arc repressor in solution: evidence for a family of β-sheet proteins. Nature 346: 586-589.
    • (1990) Nature , vol.346 , pp. 586-589
    • Breg, J.N.1    Van Opheusden, J.H.J.2    Burgering, M.J.M.3    Boelens, R.4    Kaptein, R.5
  • 10
    • 0032839007 scopus 로고    scopus 로고
    • Purification and ligand binding of EmrR, a regulator of a multidrug transporter
    • Brooun, A., Tomashek, J.J., and Lewis, K. (1999) Purification and ligand binding of EmrR, a regulator of a multidrug transporter. J Bacteriol 181: 5131-5133.
    • (1999) J Bacteriol , vol.181 , pp. 5131-5133
    • Brooun, A.1    Tomashek, J.J.2    Lewis, K.3
  • 11
    • 0025834270 scopus 로고
    • Nucleotide sequence of the Escherichia coli regulatory gene mprA and construction and characterization of mprA-deficient mutants
    • del Castillo, I., González-Pastor, J.E., San Millán, J.L., and Moreno, F. (1991) Nucleotide sequence of the Escherichia coli regulatory gene mprA and construction and characterization of mprA-deficient mutants. J Bacteriol 173: 3924-3929.
    • (1991) J Bacteriol , vol.173 , pp. 3924-3929
    • Del Castillo, I.1    González-Pastor, J.E.2    San Millán, J.L.3    Moreno, F.4
  • 12
    • 0028294881 scopus 로고
    • Role of the purine repressor hinge sequence in repressor function
    • Choi, K.Y., and Zalkin, H. (1994) Role of the purine repressor hinge sequence in repressor function. J Bacteriol 176: 1767-1772.
    • (1994) J Bacteriol , vol.176 , pp. 1767-1772
    • Choi, K.Y.1    Zalkin, H.2
  • 13
    • 0027419613 scopus 로고
    • Genetic and functional analysis of the multiple antibiotic resistance (mar) locus in Escherichia coli
    • Cohen, S.P., Hächler, H., and Levy, S.B. (1993) Genetic and functional analysis of the multiple antibiotic resistance (mar) locus in Escherichia coli. J Bacteriol 175: 1484-1492.
    • (1993) J Bacteriol , vol.175 , pp. 1484-1492
    • Cohen, S.P.1    Hächler, H.2    Levy, S.B.3
  • 14
    • 0027131605 scopus 로고
    • Salicylate induction of antibiotic resistance in Escherichia coli: Activation of the mar operon and a mar-independent pathway
    • Cohen, S.P., Levy, S.B., Foulds, J., and Rosner, J.L. (1993) Salicylate induction of antibiotic resistance in Escherichia coli: activation of the mar operon and a mar-independent pathway. J Bacteriol 175: 7856-7862.
    • (1993) J Bacteriol , vol.175 , pp. 7856-7862
    • Cohen, S.P.1    Levy, S.B.2    Foulds, J.3    Rosner, J.L.4
  • 15
    • 0030927036 scopus 로고    scopus 로고
    • Expression of a Butyrivibrio fibrisolvens E14 gene (cinB) encoding an enzyme with cinnamoyl ester hydrolase activity is negatively regulated by the product of an adjacent gene (cinR)
    • Dalrymple, B.P., and Swadling, Y. (1997) Expression of a Butyrivibrio fibrisolvens E14 gene (cinB) encoding an enzyme with cinnamoyl ester hydrolase activity is negatively regulated by the product of an adjacent gene (cinR). Microbiology 143: 1203-1210.
    • (1997) Microbiology , vol.143 , pp. 1203-1210
    • Dalrymple, B.P.1    Swadling, Y.2
  • 16
    • 0023935178 scopus 로고
    • AraC protein with altered DNA sequence specificity which activate a mutant promoter in Escherichia coli
    • Francklyn, C.S., and Lee, N. (1988) AraC protein with altered DNA sequence specificity which activate a mutant promoter in Escherichia coli. J Biol Chem 263: 4400-4407.
    • (1988) J Biol Chem , vol.263 , pp. 4400-4407
    • Francklyn, C.S.1    Lee, N.2
  • 17
    • 0013680573 scopus 로고
    • The lactose repressor
    • Beckwith, J.R., and Zipser, D. (eds). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • Gilbert, W., and Müller-Hill, B. (1970) The lactose repressor. In The Lactose Operon. Beckwith, J.R., and Zipser, D. (eds). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, pp. 93-109.
    • (1970) The Lactose Operon. , pp. 93-109
    • Gilbert, W.1    Müller-Hill, B.2
  • 18
    • 0025833517 scopus 로고
    • Activation of oxidative stress genes by mutations at the soxQ/cfxB1/marA locus of Escherichia coli
    • Greenberg, J.T., Chou, J.H., Monach, P.A., and Demple, B. (1991) Activation of oxidative stress genes by mutations at the soxQ/cfxB1/marA locus of Escherichia coli. J Bacteriol 173: 4433-4439.
    • (1991) J Bacteriol , vol.173 , pp. 4433-4439
    • Greenberg, J.T.1    Chou, J.H.2    Monach, P.A.3    Demple, B.4
  • 19
    • 0025310356 scopus 로고
    • DNA recognition by proteins with the helix-turn-helix motif
    • Harrison, S.C., and Aggarwal, A.K. (1990) DNA recognition by proteins with the helix-turn-helix motif. Ann Rev Biochem 59: 933-969.
    • (1990) Ann Rev Biochem , vol.59 , pp. 933-969
    • Harrison, S.C.1    Aggarwal, A.K.2
  • 20
    • 0025371603 scopus 로고
    • Enhanced operator binding by trp superrepressors of Escherichia coli
    • Hurlburt, B.K., and Yanofsky, C. (1990) Enhanced operator binding by trp superrepressors of Escherichia coli. J Biol Chem 265: 7853-7858.
    • (1990) J Biol Chem , vol.265 , pp. 7853-7858
    • Hurlburt, B.K.1    Yanofsky, C.2
  • 21
    • 0021988066 scopus 로고
    • Mutational analysis with the trp repressor of Escherichia coli support the helix-turn-helix model of repressor recognition of operator DNA
    • Kelley, R.L., and Yanofsky, C. (1985) Mutational analysis with the trp repressor of 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
  • 22
    • 0025304132 scopus 로고
    • Genetic studies of the lac repressor. XIII. Extensive amino acid replacements generated by the use of natural and synthetic nonsense suppressors
    • Kleina, L.G., and Miller, J.H. (1990) Genetic studies of the lac repressor. XIII. Extensive amino acid replacements generated by the use of natural and synthetic nonsense suppressors. J Mol Biol 212: 295-318.
    • (1990) J Mol Biol , vol.212 , pp. 295-318
    • Kleina, L.G.1    Miller, J.H.2
  • 23
    • 0023945429 scopus 로고
    • Increased binding of operator DNA by trp superrepressor EK49
    • Klig, L.S., and Yanofsky, C. (1988) Increased binding of operator DNA by trp superrepressor EK49. J Biol Chem 263: 243-246.
    • (1988) J Biol Chem , vol.263 , pp. 243-246
    • Klig, L.S.1    Yanofsky, C.2
  • 24
    • 0029938053 scopus 로고    scopus 로고
    • Crystal structure of the lactose operon repressor and its complexes with DNA and inducer
    • Lewis, M., Chang, G., Horton, N.C., Kercher, M.A., Pace, H.C., Schumacher, M.A., et al. (1996) Crystal structure of the lactose operon repressor and its complexes with DNA and inducer. Science 271: 1247-1254.
    • (1996) Science , vol.271 , pp. 1247-1254
    • Lewis, M.1    Chang, G.2    Horton, N.C.3    Kercher, M.A.4    Pace, H.C.5    Schumacher, M.A.6
  • 25
    • 0026686805 scopus 로고
    • emr, an Escherichia coli locus for multidrug resistance
    • Lomovskaya, O., and Lewis, K. (1992) emr, an Escherichia coli locus for multidrug resistance. Proc Natl Acad Sci 89: 8938-8942.
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 8938-8942
    • Lomovskaya, O.1    Lewis, K.2
  • 26
    • 0028999706 scopus 로고
    • EmrR is a negative regulator of the Escherichia coli multidrug resistance pump EmrAB
    • Lomovskaya, O., Lewis, K., and Matin, A. (1995) EmrR is a negative regulator of the Escherichia coli multidrug resistance pump EmrAB. J Bacteriol 177: 2328-2334.
    • (1995) J Bacteriol , vol.177 , pp. 2328-2334
    • Lomovskaya, O.1    Lewis, K.2    Matin, A.3
  • 27
    • 0029589218 scopus 로고
    • SlyA, a regulatory protein from Salmonella typhimurium, induces a haemolytic and poreforming protein in Escherichia coli
    • Ludwig, A., Tengel, C., Bauer, S., Bubert, A., Benz, R., Mollenkopf, H.J., et al. (1995) SlyA, a regulatory protein from Salmonella typhimurium, induces a haemolytic and poreforming protein in Escherichia coli. Mol Gen Genet 249: 474-486.
    • (1995) Mol Gen Genet , vol.249 , pp. 474-486
    • Ludwig, A.1    Tengel, C.2    Bauer, S.3    Bubert, A.4    Benz, R.5    Mollenkopf, H.J.6
  • 28
    • 0026738339 scopus 로고
    • Sequence alterations affecting F plasmid transfer gene expression: A conjugation system dependent on transcription by the RNA polymerase of phage T7
    • Maneewannakul, K., Maneewannakul, S., and Ippen-Ihler, K. (1992) Sequence alterations affecting F plasmid transfer gene expression: a conjugation system dependent on transcription by the RNA polymerase of phage T7. Mol Microbiol 6: 2961-2973.
    • (1992) Mol Microbiol , vol.6 , pp. 2961-2973
    • Maneewannakul, K.1    Maneewannakul, S.2    Ippen-Ihler, K.3
  • 29
    • 0026732868 scopus 로고
    • Horizontal gene transfer of the Escherichia coli pap and prs pili operons as a mechanism for the development of tissue-specific adhesive properties
    • Marklund, B.-I., Tennent, J.M., Garcia, E., Hamers, A., Baga, M., Lindberg, F., et al. (1992) Horizontal gene transfer of the Escherichia coli pap and prs pili operons as a mechanism for the development of tissue-specific adhesive properties. Mol Microbiol 6: 2225-2242.
    • (1992) Mol Microbiol , vol.6 , pp. 2225-2242
    • Marklund, B.-I.1    Tennent, J.M.2    Garcia, E.3    Hamers, A.4    Baga, M.5    Lindberg, F.6
  • 30
    • 0029079304 scopus 로고
    • Binding of purified multiple antibiotic-resistance repressor protein (MarR) to mar operator sequences
    • Martin, R.G., and Rosner, J.L. (1995) Binding of purified multiple antibiotic-resistance repressor protein (MarR) to mar operator sequences. Proc Natl Acad Sci USA 92: 5456-5460.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5456-5460
    • Martin, R.G.1    Rosner, J.L.2
  • 31
    • 0032462726 scopus 로고    scopus 로고
    • Multidrug resistance following expression of the Escherichia coli marA gene in Mycobacterium smegmatis
    • McDermott, P.F., White, D.G., Podglajen, I., Alekshun, M.N., and Levy, S.B. (1998) Multidrug resistance following expression of the Escherichia coli marA gene in Mycobacterium smegmatis. J Bacteriol 180: 2995-2998.
    • (1998) J Bacteriol , vol.180 , pp. 2995-2998
    • McDermott, P.F.1    White, D.G.2    Podglajen, I.3    Alekshun, M.N.4    Levy, S.B.5
  • 32
    • 0003785155 scopus 로고
    • Miller, J.H. (ed.). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Miller, J.H. (ed.). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, pp. 125-129, 138-139.
    • (1972) Experiments in Molecular Genetics , pp. 125-129
    • Miller, J.H.1
  • 33
    • 0002271229 scopus 로고
    • The lacl gene: Its role in lac operon control and its use as a genetic selection
    • Miller, J.H., and Reznikoff, W.S. (eds). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • Miller, J.H. (1980) The lacl gene: its role in lac operon control and its use as a genetic selection. In The Operon. Miller, J.H., and Reznikoff, W.S. (eds). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, pp. 31-88.
    • (1980) The Operon. , pp. 31-88
    • Miller, J.H.1
  • 34
    • 0029831354 scopus 로고    scopus 로고
    • Overlaps and parallels in the regulation of intrinsic multiple-antibiotic resistance in Escherichia coli
    • Miller, P.F., and Sulavik, M.C. (1996) Overlaps and parallels in the regulation of intrinsic multiple-antibiotic resistance in Escherichia coli. Mol Microbiol 21: 441-448.
    • (1996) Mol Microbiol , vol.21 , pp. 441-448
    • Miller, P.F.1    Sulavik, M.C.2
  • 35
    • 0030582731 scopus 로고    scopus 로고
    • How AraC interacts specifically with its target DNAs
    • Niland, P., Hühne, R., and Müller-Hill, B. (1996) How AraC interacts specifically with its target DNAs. J Mol Biol 264: 667-674.
    • (1996) J Mol Biol , vol.264 , pp. 667-674
    • Niland, P.1    Hühne, R.2    Müller-Hill, B.3
  • 36
    • 0019431405 scopus 로고
    • Determination of the ligand-binding characteristics of several tight-binding mutants of the lactose repressor protein
    • O'Gorman, R.B., Ferguson, L., Betz, J.L., Sadler, J.R., and Matthews, K.S. (1981) Determination of the ligand-binding characteristics of several tight-binding mutants of the lactose repressor protein. Biochim Biophys Acta 653: 236-247.
    • (1981) Biochim Biophys Acta , vol.653 , pp. 236-247
    • O'Gorman, R.B.1    Ferguson, L.2    Betz, J.L.3    Sadler, J.R.4    Matthews, K.S.5
  • 37
    • 0021196998 scopus 로고
    • Protein-DNA recognition
    • Pabo, C.O., and Sauer, R.T. (1984) Protein-DNA recognition. Ann Rev Biochem 53: 293-321.
    • (1984) Ann Rev Biochem , vol.53 , pp. 293-321
    • Pabo, C.O.1    Sauer, R.T.2
  • 38
    • 0026682657 scopus 로고
    • Transcription factors: Structural families and principals of DNA recognition
    • Pabo, C.O., and Sauer, R.T. (1992) Transcription factors: structural families and principals 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
    • 0024026228 scopus 로고
    • Sequence analysis and regulation of the hpr locus, a regulatory gene for protease production and sporulation in Bacillus subtilis
    • Perego, M., and Hoch, J.A. (1988) Sequence analysis and regulation of the hpr locus, a regulatory gene for protease production and sporulation in Bacillus subtilis. J Bacteriol 170: 2560-2567.
    • (1988) J Bacteriol , vol.170 , pp. 2560-2567
    • Perego, M.1    Hoch, J.A.2
  • 40
    • 0018377472 scopus 로고
    • Tight-binding repressors of the lac operon: Selection system and in vitro analysis
    • Pfahl, M. (1979) Tight-binding repressors of the lac operon: selection system and in vitro analysis. J Bacteriol 137: 137-145.
    • (1979) J Bacteriol , vol.137 , pp. 137-145
    • Pfahl, M.1
  • 41
    • 0029815432 scopus 로고    scopus 로고
    • Expression of the multidrug resistance operon mexA-mexB-oprM in Pseudomonas aeruginosa: MexR encodes a regulator of operon expression
    • Poole, K., Tetro, K., Zhao, Q., Neshat, S., Heinrichs, D.E., and Bianco, N. (1996) Expression of the multidrug resistance operon mexA-mexB-oprM in Pseudomonas aeruginosa: mexR encodes a regulator of operon expression. Antimicrob Agents Chemother 40: 2021-2028.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 2021-2028
    • Poole, K.1    Tetro, K.2    Zhao, Q.3    Neshat, S.4    Heinrichs, D.E.5    Bianco, N.6
  • 42
    • 0024462909 scopus 로고
    • Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor
    • Rafferty, J.B., Somers, W.S., Saint-Girons, I., and Phillips, S.E.V. (1989) Three-dimensional crystal structures of Escherichia coli met repressor with and without corepressor. Nature 341: 705-710.
    • (1989) Nature , vol.341 , pp. 705-710
    • Rafferty, J.B.1    Somers, W.S.2    Saint-Girons, I.3    Phillips, S.E.V.4
  • 43
    • 0028334118 scopus 로고
    • pecS: A locus controlling pectinase, cellulase and blue pigment production in Erwinia chrysanthemi
    • Reverchon, S., Nasser, W., and Robert-Baudouy, J. (1994) pecS: a locus controlling pectinase, cellulase and blue pigment production in Erwinia chrysanthemi. Mol Microbiol 11: 1127-1139.
    • (1994) Mol Microbiol , vol.11 , pp. 1127-1139
    • Reverchon, S.1    Nasser, W.2    Robert-Baudouy, J.3
  • 44
    • 0032169864 scopus 로고    scopus 로고
    • A novel DNA-binding motif in MarA: The first structure for an AraC family transcriptional activator
    • Rhee, S., Martin, R.G., Rosner, J.L., and Davies, D.R. (1998) A novel DNA-binding motif in MarA: the first structure for an AraC family transcriptional activator. Proc Natl Acad Sci USA 95: 10413-10418.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10413-10418
    • Rhee, S.1    Martin, R.G.2    Rosner, J.L.3    Davies, D.R.4
  • 45
    • 0028173030 scopus 로고
    • Crystal structure of Lacl member, PurR, bound to DNA: Minor groove binding by helices
    • Schumacher, M.A., Choi, K.Y., Zalkin, H., and Brennan, R.G. (1994) Crystal structure of Lacl member, PurR, bound to DNA: minor groove binding by helices. Science 266: 763-770.
    • (1994) Science , vol.266 , pp. 763-770
    • Schumacher, M.A.1    Choi, K.Y.2    Zalkin, H.3    Brennan, R.G.4
  • 46
    • 0029025536 scopus 로고
    • Characterization of MarR, the repressor of the multiple antibiotic resistance (mar) operon of Escherichia coli
    • Seoane, A.S., and Levy, S.B. (1995) Characterization of MarR, the repressor of the multiple antibiotic resistance (mar) operon of Escherichia coli. J Bacteriol 177: 3414-3419.
    • (1995) J Bacteriol , vol.177 , pp. 3414-3419
    • Seoane, A.S.1    Levy, S.B.2
  • 48
    • 0029295437 scopus 로고
    • The MarR repressor of the multiple antibiotic resistance (mar) operon in Escherichia coli: Prototypic member of a family of bacterial regulatory proteins involved in sensing phenolic compounds
    • Sulavik, M.C., Gambino, L.F., and Miller, P.F. (1995) The MarR repressor of the multiple antibiotic resistance (mar) operon in Escherichia coli: prototypic member of a family of bacterial regulatory proteins involved in sensing phenolic compounds. Mol Med 1: 436-446.
    • (1995) Mol Med , vol.1 , pp. 436-446
    • Sulavik, M.C.1    Gambino, L.F.2    Miller, P.F.3
  • 49
    • 0028060315 scopus 로고
    • The optimization of preparations of competent cells for transformation of E. coli
    • Tang, X., Nakata, Y., Li, H.-O., Zhang, M., Gao, H., Fujita, A., et al. (1994) The optimization of preparations of competent cells for transformation of E. coli. Nucleic Acids Res 22: 2857-2858.
    • (1994) Nucleic Acids Res , vol.22 , pp. 2857-2858
    • Tang, X.1    Nakata, Y.2    Li, H.-O.3    Zhang, M.4    Gao, H.5    Fujita, A.6
  • 50
    • 0022952907 scopus 로고
    • Isolation and analysis of Arc repressor mutants: Evidence for an unusual mechanism of DNA binding
    • Vershon, A.K., Bowie, J.U., Karpulus, T.M., and Sauer, R.T. (1986) Isolation and analysis of Arc repressor mutants: evidence for an unusual mechanism of DNA binding. Protein 1: 302-311.
    • (1986) Protein , vol.1 , pp. 302-311
    • Vershon, A.K.1    Bowie, J.U.2    Karpulus, T.M.3    Sauer, R.T.4


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