메뉴 건너뛰기




Volumn 288, Issue 4, 1999, Pages 659-671

Decreased imino proton exchange and base-pair opening in the IHF-DNA complex measured by NMR

Author keywords

Base pair opening; DNA; Imino proton; NMR; Proton exchange rates

Indexed keywords

DNA; DNA BINDING PROTEIN; DOUBLE STRANDED DNA; INTEGRATION HOST FACTOR; NITROGEN 15; PROTON;

EID: 0033006629     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2690     Document Type: Article
Times cited : (28)

References (33)
  • 1
    • 0029869856 scopus 로고    scopus 로고
    • Solution structure of loop A from the hair pin ribozyme from tobacco ringspot virus satellite
    • Cai Z., Tinoco I. J. Solution structure of loop A from the hair pin ribozyme from tobacco ringspot virus satellite. Biochemistry. 35:1996;6026-6036.
    • (1996) Biochemistry , vol.35 , pp. 6026-6036
    • Cai, Z.1    Tinoco, I.J.2
  • 2
    • 0015223584 scopus 로고
    • Relaxation kinetics of dimer formation by self complementary oligonucleotides
    • Craig M. E., Crothers D. M., Doty P. Relaxation kinetics of dimer formation by self complementary oligonucleotides. J. Mol. Biol. 62:1971;383-401.
    • (1971) J. Mol. Biol. , vol.62 , pp. 383-401
    • Craig, M.E.1    Crothers, D.M.2    Doty, P.3
  • 3
    • 0021710080 scopus 로고
    • E. coli integration host factor binds to specific sites in DNA
    • Craig N. L., Nash H. A. E. coli integration host factor binds to specific sites in DNA. Cell. 3:1984;707-716.
    • (1984) Cell , vol.3 , pp. 707-716
    • Craig, N.L.1    Nash, H.A.2
  • 4
    • 0030037648 scopus 로고    scopus 로고
    • Base-catalysis of imino proton exchange in DNA: Effects of catalyst upon DNA structure and dynamics
    • Folta-Stogniew E., Russua I. M. Base-catalysis of imino proton exchange in DNA: effects of catalyst upon DNA structure and dynamics. Biochemistry. 35:1996;8439-8449.
    • (1996) Biochemistry , vol.35 , pp. 8439-8449
    • Folta-Stogniew, E.1    Russua, I.M.2
  • 5
    • 0023729703 scopus 로고
    • Integration host factor interacts with the DNA replication enhancer of filamentous phage f1
    • Greenstein D., Zinder N. D., Horiuchi K. Integration host factor interacts with the DNA replication enhancer of filamentous phage f1. Proc. Natl Acad. Sci. USA. 85:1988;6262-6266.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 6262-6266
    • Greenstein, D.1    Zinder, N.D.2    Horiuchi, K.3
  • 6
    • 0028864424 scopus 로고
    • Studies of base pair kinetics by NMR measurement of proton exchange
    • Guéron M., Leroy J. L. Studies of base pair kinetics by NMR measurement of proton exchange. Methods Enzymol. 261:1995;383-413.
    • (1995) Methods Enzymol. , vol.261 , pp. 383-413
    • Guéron, M.1    Leroy, J.L.2
  • 7
    • 0028238186 scopus 로고
    • Determining the DNA sequence elements required for binding integration host factor to two different target sites
    • Hales L. M., Gumport R. I., Gardner J. F. Determining the DNA sequence elements required for binding integration host factor to two different target sites. J. Bacteriol. 176:1994;2999-3006.
    • (1994) J. Bacteriol. , vol.176 , pp. 2999-3006
    • Hales, L.M.1    Gumport, R.I.2    Gardner, J.F.3
  • 8
    • 0023645317 scopus 로고
    • Proton exchange and base-pair lifetimes in a deoxy-duplex containing a purine-pyrimidine step and in the duplex of inverse sequence
    • Kochoyan M., Leroy J. L., Guéron M. Proton exchange and base-pair lifetimes in a deoxy-duplex containing a purine-pyrimidine step and in the duplex of inverse sequence. J. Mol. Biol. 196:1987;599-609.
    • (1987) J. Mol. Biol. , vol.196 , pp. 599-609
    • Kochoyan, M.1    Leroy, J.L.2    Guéron, M.3
  • 9
    • 0024284560 scopus 로고
    • Study of structure, base-pair opening kinetics and proton exchange mechanism of the d-(AATTGCAATT) self-complementary oligodeoxynucleotide in solution
    • Kochoyan M., Lancelot G., Leroy J. L. Study of structure, base-pair opening kinetics and proton exchange mechanism of the d-(AATTGCAATT) self-complementary oligodeoxynucleotide in solution. Nucl. Acids Res. 16:1988;7685-7702.
    • (1988) Nucl. Acids Res. , vol.16 , pp. 7685-7702
    • Kochoyan, M.1    Lancelot, G.2    Leroy, J.L.3
  • 11
    • 0024292414 scopus 로고
    • Characterization of base-pair opening in deoxynucleotide duplexes using catalyzed exchange of the imino proton
    • Leroy J. L., Kochoyan M., Huynh-Dinh T., Guéron M. Characterization of base-pair opening in deoxynucleotide duplexes using catalyzed exchange of the imino proton. J. Mol. Biol. 200:1988;223-238.
    • (1988) J. Mol. Biol. , vol.200 , pp. 223-238
    • Leroy, J.L.1    Kochoyan, M.2    Huynh-Dinh, T.3    Guéron, M.4
  • 12
    • 0026598551 scopus 로고
    • Proton exchange in DNA-luxopeptin and DNA-echinomycin bisintercalation complexes: Rates and processes of base-pair opening
    • Leroy J. L., Gao X., Misra V., Guéon M., Patel D. J. Proton exchange in DNA-luxopeptin and DNA-echinomycin bisintercalation complexes: rates and processes of base-pair opening. Biochemistry. 31:1992;1407-1415.
    • (1992) Biochemistry , vol.31 , pp. 1407-1415
    • Leroy, J.L.1    Gao, X.2    Misra, V.3    Guéon, M.4    Patel, D.J.5
  • 13
    • 0027159426 scopus 로고
    • Acid multimers of oligodeoxycytidine strands: Stoichiometry, base-pair characterization, and proton exchange properties
    • Leroy J. L., Gehring K., Kettani A., Guéron M. Acid multimers of oligodeoxycytidine strands: stoichiometry, base-pair characterization, and proton exchange properties. Biochemistry. 32:1993;6019-6031.
    • (1993) Biochemistry , vol.32 , pp. 6019-6031
    • Leroy, J.L.1    Gehring, K.2    Kettani, A.3    Guéron, M.4
  • 14
    • 0000389264 scopus 로고
    • Use of a water flip-back pulse in the homonuclear NOESY experiment
    • Lippens G., Dhalluin C., Wieruszeski J.-M. Use of a water flip-back pulse in the homonuclear NOESY experiment. J. Biomol. NMR. 5:1995;327-331.
    • (1995) J. Biomol. NMR , vol.5 , pp. 327-331
    • Lippens, G.1    Dhalluin, C.2    Wieruszeski, J.-M.3
  • 15
    • 0022885153 scopus 로고
    • The DNA binding domain and bending angle of E. coli CAP protein
    • Liu-Johnson H., Gartenberg M. R., Crothers D. M. The DNA binding domain and bending angle of E. coli CAP protein. Cell. 47:1986;995-1005.
    • (1986) Cell , vol.47 , pp. 995-1005
    • Liu-Johnson, H.1    Gartenberg, M.R.2    Crothers, D.M.3
  • 16
    • 0019783899 scopus 로고
    • Purification and properties of the Escherichia coli protein factor required for lambda integrative recombination
    • Nash H. A., Robertson C. A. Purification and properties of the Escherichia coli protein factor required for lambda integrative recombination. J. Biol. Chem. 256:1981;9246-9253.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9246-9253
    • Nash, H.A.1    Robertson, C.A.2
  • 17
    • 0025252231 scopus 로고
    • Heteronuclear filters in two-dimensional (1H, 1H) NMR spectroscopy: Combined use with isotope labeling for studies of macromolecular conformation and intermolecular interactions
    • Otting G., Wüthrich K. Heteronuclear filters in two-dimensional (1H, 1H) NMR spectroscopy: combined use with isotope labeling for studies of macromolecular conformation and intermolecular interactions. Quart. Rev. Biophys. 23:1990;39-96.
    • (1990) Quart. Rev. Biophys. , vol.23 , pp. 39-96
    • Otting, G.1    Wüthrich, K.2
  • 18
    • 0024997404 scopus 로고
    • Protein-DNa contacts in the structure of a homeodomain-DNA complex determined by nuclear magnetic resonance spectroscopy in solution
    • Otting G., Qian Y. Q., Billeter M., Muler M., Affolter M., Gehring W. J., Wüthrich K. Protein-DNa contacts in the structure of a homeodomain-DNA complex determined by nuclear magnetic resonance spectroscopy in solution. EMBO J. 9:1990;3085-3092.
    • (1990) EMBO J. , vol.9 , pp. 3085-3092
    • Otting, G.1    Qian, Y.Q.2    Billeter, M.3    Muler, M.4    Affolter, M.5    Gehring, W.J.6    Wüthrich, K.7
  • 19
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 2:1992;661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 20
    • 0030782227 scopus 로고    scopus 로고
    • Role of architectural elements in combinatorial regulation of initiation of DNA replication in Escherichia coli
    • Polaczek P., Kwan K., Liberies D. A., Campbell J. L. Role of architectural elements in combinatorial regulation of initiation of DNA replication in Escherichia coli. Mol. Microbiol. 26:1997;261-275.
    • (1997) Mol. Microbiol. , vol.26 , pp. 261-275
    • Polaczek, P.1    Kwan, K.2    Liberies, D.A.3    Campbell, J.L.4
  • 21
    • 0015223587 scopus 로고
    • Co-operative non-enzymic base recognition. III. Kinetics of the helix-coil transition of the oligoribouridylic oligoriboadenylic acid system and of oligoriboadenylic acid alone at acid pH
    • Pörschke D., Eigen M. Co-operative non-enzymic base recognition. III. Kinetics of the helix-coil transition of the oligoribouridylic oligoriboadenylic acid system and of oligoriboadenylic acid alone at acid pH. J. Mol. Biol. 62:1971;361-381.
    • (1971) J. Mol. Biol. , vol.62 , pp. 361-381
    • Pörschke, D.1    Eigen, M.2
  • 22
    • 0030451819 scopus 로고    scopus 로고
    • Crystal structure of an IHF-DNA complex: A protein-induced DNA U-turn
    • Rice P. A., Yang S., Mizuuchi K., Nash H. A. Crystal structure of an IHF-DNA complex: a protein-induced DNA U-turn. Cell. 87:1996;1295-1306.
    • (1996) Cell , vol.87 , pp. 1295-1306
    • Rice, P.A.1    Yang, S.2    Mizuuchi, K.3    Nash, H.A.4
  • 23
    • 0023833241 scopus 로고
    • Bending of the bacteriophage 1 attachment site by Escherichia coli integration host factor
    • Robertson C. A., Nash H. A. Bending of the bacteriophage 1 attachment site by Escherichia coli integration host factor. J. Biol. Chem. 263:1988;3554-3557.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3554-3557
    • Robertson, C.A.1    Nash, H.A.2
  • 25
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • Shaka A. J., Barker P. B., Freeman R. Computer-optimized decoupling scheme for wideband applications and low-level operation. J. Magn. Reson. 64:1985;547-552.
    • (1985) J. Magn. Reson. , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 26
    • 0000521134 scopus 로고
    • Spin-echo water suppression for the generation of pure-phase two-dimensional NMR spectra
    • Sklenar V., Bax A. Spin-echo water suppression for the generation of pure-phase two-dimensional NMR spectra. J. Magn. Reson. 74:1987;469-479.
    • (1987) J. Magn. Reson. , vol.74 , pp. 469-479
    • Sklenar, V.1    Bax, A.2
  • 28
    • 2642628181 scopus 로고
    • A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants
    • States D. J. A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J. Magn. Reson. 48:1982;286-292.
    • (1982) J. Magn. Reson. , vol.48 , pp. 286-292
    • States, D.J.1
  • 29
    • 0023644961 scopus 로고
    • The integration host factor of Escherichia coli binds to bent DNA at the origin of replication of the plasmid pSC101
    • Stenzel T. T., Patel P., Bastia D. The integration host factor of Escherichia coli binds to bent DNA at the origin of replication of the plasmid pSC101. Cell. 49:1987;709-717.
    • (1987) Cell , vol.49 , pp. 709-717
    • Stenzel, T.T.1    Patel, P.2    Bastia, D.3
  • 30
  • 31
    • 0023771741 scopus 로고
    • Empirical estimation of protein-induced DNA bending angles: Applications to 1 site-specific recombination complexes
    • Thompson J. F., Landy A. Empirical estimation of protein-induced DNA bending angles: applications to 1 site-specific recombination complexes. Nucl. Acids Res. 16:1988;9687-9705.
    • (1988) Nucl. Acids Res. , vol.16 , pp. 9687-9705
    • Thompson, J.F.1    Landy, A.2
  • 32
    • 0024340266 scopus 로고
    • The interaction of E. coli IHF protein with its specific binding sites
    • Yang C., Nash H. A. The interaction of E. coli IHF protein with its specific binding sites. Cell. 57:1989;869-880.
    • (1989) Cell , vol.57 , pp. 869-880
    • Yang, C.1    Nash, H.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.