메뉴 건너뛰기




Volumn 340, Issue 3, 2004, Pages 445-457

Monovalent cations regulate DNA sequence recognition by 434 repressor

Author keywords

bacteriophage; DNA binding; DNA flexibility; DNA structure; gene expression

Indexed keywords

HYDROXYL GROUP; MONOVALENT CATION; REPRESSOR PROTEIN;

EID: 2942711644     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.04.065     Document Type: Article
Times cited : (11)

References (60)
  • 1
    • 0025816853 scopus 로고
    • The structure of B-helical C-G-A-T-C-G-A-T-C-G and comparison with C-C-A-A-C-G-T-T-G-G. The effect of base pair reversals
    • Grzeskowiak K., Yanagi K., Prive G.G., Dickerson R.E. The structure of B-helical C-G-A-T-C-G-A-T-C-G and comparison with C-C-A-A-C-G-T-T-G-G. The effect of base pair reversals. J. Biol. Chem. 266:1991;8861-8883
    • (1991) J. Biol. Chem. , vol.266 , pp. 8861-8883
    • Grzeskowiak, K.1    Yanagi, K.2    Prive, G.G.3    Dickerson, R.E.4
  • 2
    • 0033600794 scopus 로고    scopus 로고
    • Absence of minor groove monovalent cations in the crosslinked dodecamer C-G-C-G-A-A-T-T-C-G-C-G
    • Chiu T.K., Kaczor-Grzeskowiak M., Dickerson R.E. Absence of minor groove monovalent cations in the crosslinked dodecamer C-G-C-G-A-A-T-T-C-G-C-G. J. Mol. Biol. 292:1999;589-608
    • (1999) J. Mol. Biol. , vol.292 , pp. 589-608
    • Chiu, T.K.1    Kaczor-Grzeskowiak, M.2    Dickerson, R.E.3
  • 3
    • 0032499635 scopus 로고    scopus 로고
    • The B-DNA dodecamer at high resolution reveals a spine of water on sodium
    • Shui X., McFail-Isom L., Hu G.G., Williams L.D. The B-DNA dodecamer at high resolution reveals a spine of water on sodium. Biochemistry. 37:1998;8341-8355
    • (1998) Biochemistry , vol.37 , pp. 8341-8355
    • Shui, X.1    McFail-Isom, L.2    Hu, G.G.3    Williams, L.D.4
  • 4
    • 0024284650 scopus 로고
    • Recognition of a DNA operator by the repressor of phage 434: A view at high resolution
    • Aggarwal A., Rodgers D.W., Drottar M., Ptashne M., Harrison S.C. Recognition of a DNA operator by the repressor of phage 434: a view at high resolution. Science. 242:1988;899-907
    • (1988) Science , vol.242 , pp. 899-907
    • Aggarwal, A.1    Rodgers, D.W.2    Drottar, M.3    Ptashne, M.4    Harrison, S.C.5
  • 6
    • 0027918646 scopus 로고
    • The complex between phage 434 repressor DNA-binding domain and operator site OR3: Structural differences between consensus and non-consensus half-sites
    • Rodgers D.W., Harrison S.C. The complex between phage 434 repressor DNA-binding domain and operator site OR3: structural differences between consensus and non-consensus half-sites. Structure. 1:1993;227-240
    • (1993) Structure , vol.1 , pp. 227-240
    • Rodgers, D.W.1    Harrison, S.C.2
  • 7
    • 0023187152 scopus 로고
    • Effect of non-contacted bases on the affinity of 434 operator for 434 repressor and Cro
    • Koudelka G.B., Harrison S.C., Ptashne M. Effect of non-contacted bases on the affinity of 434 operator for 434 repressor and Cro. Nature. 326:1987;886-888
    • (1987) Nature , vol.326 , pp. 886-888
    • Koudelka, G.B.1    Harrison, S.C.2    Ptashne, M.3
  • 8
    • 0023202898 scopus 로고
    • Structure of the repressor-operator complex of bacteriophage 434
    • Anderson J.E., Ptashne M., Harrison S.C. Structure of the repressor-operator complex of bacteriophage 434. Nature. 326:1987;846-852
    • (1987) Nature , vol.326 , pp. 846-852
    • Anderson, J.E.1    Ptashne, M.2    Harrison, S.C.3
  • 9
    • 0026595235 scopus 로고
    • DNA twisting and the effects of non-contacted bases on affinity of 434 operator for 434 repressor
    • Koudelka G.B., Carlson P. DNA twisting and the effects of non-contacted bases on affinity of 434 operator for 434 repressor. Nature. 355:1992;89-91
    • (1992) Nature , vol.355 , pp. 89-91
    • Koudelka, G.B.1    Carlson, P.2
  • 10
    • 0032518220 scopus 로고    scopus 로고
    • Recognition of DNA structure by 434 repressor
    • Koudelka G.B. Recognition of DNA structure by 434 repressor. Nucl. Acids Res. 26:1998;669-675
    • (1998) Nucl. Acids Res. , vol.26 , pp. 669-675
    • Koudelka, G.B.1
  • 11
    • 0023687419 scopus 로고
    • DNA twisting and the affinity of bacteriophage 434 operator for bacteriophage 434 repressor
    • Koudelka G.B., Harbury P.H., Harrison S.C., Ptashne M. DNA twisting and the affinity of bacteriophage 434 operator for bacteriophage 434 repressor. Proc. Natl Acad. Sci. USA. 85:1988;4633-4637
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4633-4637
    • Koudelka, G.B.1    Harbury, P.H.2    Harrison, S.C.3    Ptashne, M.4
  • 12
    • 0037968651 scopus 로고    scopus 로고
    • The role of the minor groove substituents in indirect readout of DNA sequence by 434 repressor
    • Mauro S.A., Pawlowski D., Koudelka G.B. The role of the minor groove substituents in indirect readout of DNA sequence by 434 repressor. J. Biol. Chem. 278:2004;12955-12960
    • (2004) J. Biol. Chem. , vol.278 , pp. 12955-12960
    • Mauro, S.A.1    Pawlowski, D.2    Koudelka, G.B.3
  • 13
    • 0027146277 scopus 로고
    • Operator sequence context influences amino acid-base-pair interactions in 434 repressor-operator complexes
    • Bell A.C., Koudelka G.B. Operator sequence context influences amino acid-base-pair interactions in 434 repressor-operator complexes. J. Mol. Biol. 234:1993;542-553
    • (1993) J. Mol. Biol. , vol.234 , pp. 542-553
    • Bell, A.C.1    Koudelka, G.B.2
  • 14
    • 0028890298 scopus 로고
    • R3. The influence of contacted and noncontacted base pairs
    • R3. The influence of contacted and noncontacted base pairs. J. Biol. Chem. 270:1995;1205-1212
    • (1995) J. Biol. Chem. , vol.270 , pp. 1205-1212
    • Bell, A.C.1    Koudelka, G.B.2
  • 16
    • 0017701075 scopus 로고
    • Non-specific interaction of lac repressor with DNA: An association reaction driven by counterion release
    • DeHaseth P.L., Lohman T.M., Record M.T. Non-specific interaction of lac repressor with DNA: an association reaction driven by counterion release. Biochemistry. 16:1977;4783-4790
    • (1977) Biochemistry , vol.16 , pp. 4783-4790
    • Dehaseth, P.L.1    Lohman, T.M.2    Record, M.T.3
  • 17
    • 0031576995 scopus 로고    scopus 로고
    • Thermodynamics of the interactions of lac repressor with variants of the symmetric lac operator: Effects of converting a consensus site to a non-specific site
    • Frank D.E., Saecker R.M., Bond J.P., Capp M.W., Tsodikov O.V., Melcher S.E., et al. Thermodynamics of the interactions of lac repressor with variants of the symmetric lac operator: effects of converting a consensus site to a non-specific site. J. Mol. Biol. 267:1997;1186-1206
    • (1997) J. Mol. Biol. , vol.267 , pp. 1186-1206
    • Frank, D.E.1    Saecker, R.M.2    Bond, J.P.3    Capp, M.W.4    Tsodikov, O.V.5    Melcher, S.E.6
  • 18
    • 0035957083 scopus 로고    scopus 로고
    • Site-specific cation binding mediates TATA binding protein-DNA interaction from a hyperthermophilic archaeon
    • Bergqvist S., O'Brien R., Ladbury J.E. Site-specific cation binding mediates TATA binding protein-DNA interaction from a hyperthermophilic archaeon. Biochemistry. 40:2001;2419-2425
    • (2001) Biochemistry , vol.40 , pp. 2419-2425
    • Bergqvist, S.1    O'Brien, R.2    Ladbury, J.E.3
  • 19
    • 0037143629 scopus 로고    scopus 로고
    • DNA-dependent divalent cation binding in the nucleosome core particle
    • Davey C.A., Richmond T.J. DNA-dependent divalent cation binding in the nucleosome core particle. Proc. Natl Acad. Sci. USA. 20:2002;11169-11174
    • (2002) Proc. Natl Acad. Sci. USA , vol.20 , pp. 11169-11174
    • Davey, C.A.1    Richmond, T.J.2
  • 20
    • 0036307707 scopus 로고    scopus 로고
    • Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution
    • Davey C.A., Sargent D.F., Luger K., Maeder A.W., Richmond T.J. Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution. J. Mol. Biol. 319:2002;1097-1113
    • (2002) J. Mol. Biol. , vol.319 , pp. 1097-1113
    • Davey, C.A.1    Sargent, D.F.2    Luger, K.3    Maeder, A.W.4    Richmond, T.J.5
  • 21
    • 0024378717 scopus 로고
    • Role of the hydrophobic effect in stability of site-specific protein-DNA complexes
    • Ha J.H., Spolar R.S., Record M.T. Role of the hydrophobic effect in stability of site-specific protein-DNA complexes. J. Mol. Biol. 209:1989;801-816
    • (1989) J. Mol. Biol. , vol.209 , pp. 801-816
    • Ha, J.H.1    Spolar, R.S.2    Record, M.T.3
  • 22
    • 0026498015 scopus 로고
    • Thermodynamic stoichiometries of participation of water, cations and anions in specific and nonspecific-binding of lac repressor to DNA: Possible thermodynamic origins of the glutamate effect on protein-DNA interactions
    • Ha J.H., Capp M.W., Hohenwalter M.D., Baskerville M., Record M.T. Thermodynamic stoichiometries of participation of water, cations and anions in specific and nonspecific-binding of lac repressor to DNA: possible thermodynamic origins of the glutamate effect on protein-DNA interactions. J. Mol. Biol. 228:1992;252-264
    • (1992) J. Mol. Biol. , vol.228 , pp. 252-264
    • Ha, J.H.1    Capp, M.W.2    Hohenwalter, M.D.3    Baskerville, M.4    Record, M.T.5
  • 23
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • Manning G.S. The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Quart. Rev. Biophys. 11:1978;176-246
    • (1978) Quart. Rev. Biophys. , vol.11 , pp. 176-246
    • Manning, G.S.1
  • 25
    • 0242668713 scopus 로고    scopus 로고
    • DNA stimulated assembly of oligomeric bacteriophage 434 repressor: Evidence for cooperative binding by recruitment
    • Ciubotaru M., Koudelka G.B. DNA stimulated assembly of oligomeric bacteriophage 434 repressor: evidence for cooperative binding by recruitment. Biochemistry. 42:2003;4253-4264
    • (2003) Biochemistry , vol.42 , pp. 4253-4264
    • Ciubotaru, M.1    Koudelka, G.B.2
  • 26
    • 0032515104 scopus 로고    scopus 로고
    • Carboxyl-teminal domain dimer interface mutant 434 repressors have altered dimerization and DNA binding specificities
    • Donner A.L., Koudelka G.B. Carboxyl-teminal domain dimer interface mutant 434 repressors have altered dimerization and DNA binding specificities. J. Mol. Biol. 283:1998;931-946
    • (1998) J. Mol. Biol. , vol.283 , pp. 931-946
    • Donner, A.L.1    Koudelka, G.B.2
  • 27
    • 0021130173 scopus 로고
    • Substituting an α-helix switches the sequence specific DNA interactions of a repressor
    • Wharton R.P., Brown E.L., Ptashne M. Substituting an α-helix switches the sequence specific DNA interactions of a repressor. Cell. 38:1985;361-369
    • (1985) Cell , vol.38 , pp. 361-369
    • Wharton, R.P.1    Brown, E.L.2    Ptashne, M.3
  • 28
    • 0026547676 scopus 로고
    • Determination of the nuclear magnetic resonance solution structure of the DNA-binding domain (residues 1-69) of the 434 repressor and comparison with the X-ray crystal structure
    • Neri D., Billeter M., Wüthrich K. Determination of the nuclear magnetic resonance solution structure of the DNA-binding domain (residues 1-69) of the 434 repressor and comparison with the X-ray crystal structure. J. Mol. Biol. 223:1992;743-767
    • (1992) J. Mol. Biol. , vol.223 , pp. 743-767
    • Neri, D.1    Billeter, M.2    Wüthrich, K.3
  • 29
    • 0024961628 scopus 로고
    • Structure of the amino-terminal domain of phage 434 repressor at 2.0 Å resolution
    • Mondragon A., Subbiah S., Almo S.C., Drottar M., Harrison S.C. Structure of the amino-terminal domain of phage 434 repressor at 2.0 Å resolution. J. Mol. Biol. 205:1989;189-200
    • (1989) J. Mol. Biol. , vol.205 , pp. 189-200
    • Mondragon, A.1    Subbiah, S.2    Almo, S.C.3    Drottar, M.4    Harrison, S.C.5
  • 30
    • 0026807036 scopus 로고
    • Using hydroxyl radical to probe DNA structure
    • Price M.A., Tullius T.D. Using hydroxyl radical to probe DNA structure. Methods Enzymol. 212:1992;194-219
    • (1992) Methods Enzymol. , vol.212 , pp. 194-219
    • Price, M.A.1    Tullius, T.D.2
  • 31
    • 0033527737 scopus 로고    scopus 로고
    • Nucleosome structural features and intrinsic properties of the TATAAACGCC repeat sequence
    • Widlund H.R., Kuduvalli P.N., Bengtsson M., Cao H., Tullius T.D., Kubista M. Nucleosome structural features and intrinsic properties of the TATAAACGCC repeat sequence. J. Biol. Chem. 274:1999;31847-31852
    • (1999) J. Biol. Chem. , vol.274 , pp. 31847-31852
    • Widlund, H.R.1    Kuduvalli, P.N.2    Bengtsson, M.3    Cao, H.4    Tullius, T.D.5    Kubista, M.6
  • 32
    • 0022360001 scopus 로고
    • Ethylation interference and X-ray crystallography identify similar interactions between 434 repressor and operator
    • Bushman F.D., Anderson J.E., Harrison S.C., Ptashne M. Ethylation interference and X-ray crystallography identify similar interactions between 434 repressor and operator. Nature. 316:1985;651-653
    • (1985) Nature , vol.316 , pp. 651-653
    • Bushman, F.D.1    Anderson, J.E.2    Harrison, S.C.3    Ptashne, M.4
  • 33
    • 0022872214 scopus 로고
    • Activation of transcription by the bacteriophage 434 repressor
    • Bushman F.D., Ptashne M. Activation of transcription by the bacteriophage 434 repressor. Proc. Natl Acad. Sci. USA. 83:1986;9353-9357
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 9353-9357
    • Bushman, F.D.1    Ptashne, M.2
  • 35
    • 0036106350 scopus 로고    scopus 로고
    • Reversal of halophilicity in a protein-DNA interaction by limited mutation strategy
    • Bergqvist S., Williams M.A., O'Brien R., Ladbury J.E. Reversal of halophilicity in a protein-DNA interaction by limited mutation strategy. Structure (Camb.). 10:2002;629-637
    • (2002) Structure (Camb.) , vol.10 , pp. 629-637
    • Bergqvist, S.1    Williams, M.A.2    O'Brien, R.3    Ladbury, J.E.4
  • 36
    • 0032577337 scopus 로고    scopus 로고
    • The effects of salt on the TATA binding protein-DNA interaction from a hyperthermophilic archaeon
    • O'Brien R., DeDecker B., Fleming K.G., Sigler P.B., Ladbury J.E. The effects of salt on the TATA binding protein-DNA interaction from a hyperthermophilic archaeon. J. Mol. Biol. 279:1998;117-125
    • (1998) J. Mol. Biol. , vol.279 , pp. 117-125
    • O'Brien, R.1    Dedecker, B.2    Fleming, K.G.3    Sigler, P.B.4    Ladbury, J.E.5
  • 37
    • 0007703108 scopus 로고
    • A phage repressor-operator complex at 7 Å resolution
    • Anderson J.E., Harrison S.C., Ptashne M. A phage repressor-operator complex at 7 Å resolution. Nature. 326:1987;888-891
    • (1987) Nature , vol.326 , pp. 888-891
    • Anderson, J.E.1    Harrison, S.C.2    Ptashne, M.3
  • 39
    • 0032387836 scopus 로고    scopus 로고
    • Structure of the potassium form of CGCGAATTCGCG: DNA deformation by electrostatic collapse around inorganic cations
    • Shui X., Sines C.C., McFail-Isom L., VanDerveer D., Williams L.D. Structure of the potassium form of CGCGAATTCGCG: DNA deformation by electrostatic collapse around inorganic cations. Biochemistry. 37:1998;16877-16887
    • (1998) Biochemistry , vol.37 , pp. 16877-16887
    • Shui, X.1    Sines, C.C.2    McFail-Isom, L.3    Vanderveer, D.4    Williams, L.D.5
  • 43
    • 0036009329 scopus 로고    scopus 로고
    • DNA-cation interactions. Quo vadis?
    • Egli M. DNA-cation interactions. Quo vadis? Chem. Biol. 9:2002;277-286
    • (2002) Chem. Biol. , vol.9 , pp. 277-286
    • Egli, M.1
  • 44
    • 0038713237 scopus 로고    scopus 로고
    • A unified model for the origin of DNA sequence-directed curvature
    • Hud N.V., Plavec J. A unified model for the origin of DNA sequence-directed curvature. Biopolymers. 69:2003;144-158
    • (2003) Biopolymers , vol.69 , pp. 144-158
    • Hud, N.V.1    Plavec, J.2
  • 45
    • 0034802485 scopus 로고    scopus 로고
    • Influence of the dynamic positions of cations on the structure of the DNA minor groove: Sequence-dependent effects
    • Hamelberg D., Williams L.D., Wilson W.D. Influence of the dynamic positions of cations on the structure of the DNA minor groove: sequence-dependent effects. J. Am. Chem. Soc. 123:2001;7745-7755
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7745-7755
    • Hamelberg, D.1    Williams, L.D.2    Wilson, W.D.3
  • 46
    • 0033605083 scopus 로고    scopus 로고
    • Localization of ammonium ions in the minor groove of DNA duplexes in solution and the origin of DNA A-tract bending
    • Hud N.V., Sklenar V., Feigon J. Localization of ammonium ions in the minor groove of DNA duplexes in solution and the origin of DNA A-tract bending. J. Mol. Biol. 286:1999;651-660
    • (1999) J. Mol. Biol. , vol.286 , pp. 651-660
    • Hud, N.V.1    Sklenar, V.2    Feigon, J.3
  • 47
    • 0023664450 scopus 로고
    • Variability of the intracellular ionic environment of Escherichia coli-differences between in vitro and in vivo effects of ion concentrations on protein-DNA interactions and gene-expression
    • Richey B., Cayley D.S., Mossing M.C., Kolka C., Anderson C.F., Farrar T.C., Record M.T. Variability of the intracellular ionic environment of Escherichia coli-differences between in vitro and in vivo effects of ion concentrations on protein-DNA interactions and gene-expression. J. Biol. Chem. 262:1987;7157-7164
    • (1987) J. Biol. Chem. , vol.262 , pp. 7157-7164
    • Richey, B.1    Cayley, D.S.2    Mossing, M.C.3    Kolka, C.4    Anderson, C.F.5    Farrar, T.C.6    Record, M.T.7
  • 49
    • 0022000993 scopus 로고
    • Productive phage infection in Escherichia coli with reduced internal levels of the major cations
    • Kuhn A., Kellenberger E. Productive phage infection in Escherichia coli with reduced internal levels of the major cations. J. Bacteriol. 163:1985;906-912
    • (1985) J. Bacteriol. , vol.163 , pp. 906-912
    • Kuhn, A.1    Kellenberger, E.2
  • 50
    • 0034630237 scopus 로고    scopus 로고
    • Characterization of Streptococcus thermophilus strains that undergo lysis under unfavourable environmental conditions
    • Husson-Kao C., Mengaud J., Gripon J.C., Benbadis L., Chapot-Chartier M.P. Characterization of Streptococcus thermophilus strains that undergo lysis under unfavourable environmental conditions. Int. J. Food Microbiol. 55:2000;209-213
    • (2000) Int. J. Food Microbiol. , vol.55 , pp. 209-213
    • Husson-Kao, C.1    Mengaud, J.2    Gripon, J.C.3    Benbadis, L.4    Chapot-Chartier, M.P.5
  • 52
    • 0032981401 scopus 로고    scopus 로고
    • Effects of changes in membrane sodium flux on virulence gene expression in Vibrio cholerae
    • Hase C.C., Mekalanos J.J. Effects of changes in membrane sodium flux on virulence gene expression in Vibrio cholerae. Proc. Natl Acad. Sci. USA. 96:1999;3183-3187
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3183-3187
    • Hase, C.C.1    Mekalanos, J.J.2
  • 53
    • 0026802487 scopus 로고
    • Non-contacted bases affect the affinity of synthetic P22 operators for P22 repressor
    • Wu L., Vertino A., Koudelka G.B. Non-contacted bases affect the affinity of synthetic P22 operators for P22 repressor. J. Biol. Chem. 267:1992;9134-9135
    • (1992) J. Biol. Chem. , vol.267 , pp. 9134-9135
    • Wu, L.1    Vertino, A.2    Koudelka, G.B.3
  • 54
    • 0031027295 scopus 로고    scopus 로고
    • DNA-based loss of specificity mutations
    • Hilchey S.P., Koudelka G.B. DNA-based loss of specificity mutations. J. Biol. Chem. 272:1997;1646-1653
    • (1997) J. Biol. Chem. , vol.272 , pp. 1646-1653
    • Hilchey, S.P.1    Koudelka, G.B.2
  • 55
    • 0026409841 scopus 로고
    • Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein-DNA interactions in vivo
    • Cayley S., Lewis B.A., Guttman H.J., Record M.T. Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein-DNA interactions in vivo. J. Mol. Biol. 222:1991;281-300
    • (1991) J. Mol. Biol. , vol.222 , pp. 281-300
    • Cayley, S.1    Lewis, B.A.2    Guttman, H.J.3    Record, M.T.4
  • 56
    • 0344653612 scopus 로고    scopus 로고
    • Responses of E. coli to osmotic stress: Large changes in amounts of cytoplasmic solutes and water
    • Record M.T., Courtenay E.S., Cayley D.S., Guttman H.J. Responses of E. coli to osmotic stress: large changes in amounts of cytoplasmic solutes and water. Trends Biochem. Sci. 23:1998;143-148
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 143-148
    • Record, M.T.1    Courtenay, E.S.2    Cayley, D.S.3    Guttman, H.J.4
  • 57
    • 0004253967 scopus 로고
    • Co-crystals of the DNA-binding domain of phage 434 repressor and a synthetic 434 operator
    • Anderson J.E., Ptashne M., Harrison S.C. Co-crystals of the DNA-binding domain of phage 434 repressor and a synthetic 434 operator. Proc. Natl Acad. Sci. USA. 81:1984;1307-1311
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 1307-1311
    • Anderson, J.E.1    Ptashne, M.2    Harrison, S.C.3
  • 58
    • 0015530179 scopus 로고
    • Lac repressor binding to non-operator DNA: Detailed studies and a comparison of equilibrium and rate competition methods
    • Lin S., Riggs A.D. Lac repressor binding to non-operator DNA: detailed studies and a comparison of equilibrium and rate competition methods. J. Mol. Biol. 72:1972;671-690
    • (1972) J. Mol. Biol. , vol.72 , pp. 671-690
    • Lin, S.1    Riggs, A.D.2
  • 59
    • 0027172789 scopus 로고
    • A double-filter method for nitrocellulose-filter binding: Application to protein-nucleic acid interactions
    • Wong I., Lohman T.M. A double-filter method for nitrocellulose-filter binding: application to protein-nucleic acid interactions. Proc. Natl Acad. Sci. USA. 90:1993;5428-5432
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5428-5432
    • Wong, I.1    Lohman, T.M.2
  • 60
    • 0018867360 scopus 로고
    • E. coli RNA polymerase interacts homologously with two different promoters
    • Siebenlist U., Simpson R.B., Gilbert W. E. coli RNA polymerase interacts homologously with two different promoters. Cell. 20:1980;269-281
    • (1980) Cell , vol.20 , pp. 269-281
    • Siebenlist, U.1    Simpson, R.B.2    Gilbert, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.