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Volumn 276, Issue 4, 1998, Pages 809-818

DNA structure and flexibility in the sequence-specific binding of papillomavirus E2 proteins

Author keywords

DNA conformation; DNA flexibility; DNA binding; E2; Papillomavirus

Indexed keywords

CURVED DNA; SPACER DNA; VIRUS DNA; VIRUS PROTEIN;

EID: 0032489497     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1578     Document Type: Article
Times cited : (65)

References (32)
  • 1
    • 0029764661 scopus 로고    scopus 로고
    • A fluorescence anisotropy study of DNA binding by HPV-11 E2C protein: A hierarchy of of E2-binding sites
    • Alexander K.A., Phelps W.C. A fluorescence anisotropy study of DNA binding by HPV-11 E2C protein A hierarchy of of E2-binding sites. Biochemistry. 35:1996;9864-9872
    • (1996) Biochemistry , vol.35 , pp. 9864-9872
    • Alexander, K.A.1    Phelps, W.C.2
  • 3
    • 0023144684 scopus 로고
    • Structural and transcriptional analysis of human papillomavirus type 16 sequences in cervical carcinoma cell lines
    • Baker C.C., Phelps W.C., Lindgren V., Braun M.J., Gonda M.A., Howley P.M. Structural and transcriptional analysis of human papillomavirus type 16 sequences in cervical carcinoma cell lines. J. Virol. 61:1987;962-971
    • (1987) J. Virol. , vol.61 , pp. 962-971
    • Baker, C.C.1    Phelps, W.C.2    Lindgren, V.3    Braun, M.J.4    Gonda, M.A.5    Howley, P.M.6
  • 4
    • 0025166415 scopus 로고
    • The DNA-binding domain of HPV-16 E2 protein interaction with the viral enhancer: Protein-induced DNA bending and role of the nonconserved core sequence in binding site affinity
    • Bedrosian C.L., Bastia D. The DNA-binding domain of HPV-16 E2 protein interaction with the viral enhancer protein-induced DNA bending and role of the nonconserved core sequence in binding site affinity. Virology. 174:1990;557-575
    • (1990) Virology , vol.174 , pp. 557-575
    • Bedrosian, C.L.1    Bastia, D.2
  • 5
    • 0027497767 scopus 로고
    • Influence of defects on the electrophoretic, thermodynamic and dielectric properties of a 21 base pair DNA in solution
    • Bonincontro A., Matzeu M., Mazzei F., Minoprio A., Pedone F. Influence of defects on the electrophoretic, thermodynamic and dielectric properties of a 21 base pair DNA in solution. Biochim. Biophys. Acta. 1171:1993;288-293
    • (1993) Biochim. Biophys. Acta , vol.1171 , pp. 288-293
    • Bonincontro, A.1    Matzeu, M.2    Mazzei, F.3    Minoprio, A.4    Pedone, F.5
  • 6
    • 0020359857 scopus 로고
    • Reversible bending and helix geometry in a B-DNA dodecamer: CGCGAATTBrCGCG
    • Fratini A.V., Kopka M.L., Drew H.R., Dickerson R.E. Reversible bending and helix geometry in a B-DNA dodecamer CGCGAATTBrCGCG. J. Biol. Chem. 257:(24):1982;14686-14707
    • (1982) J. Biol. Chem. , vol.257 , Issue.24 , pp. 14686-14707
    • Fratini, A.V.1    Kopka, M.L.2    Drew, H.R.3    Dickerson, R.E.4
  • 7
    • 84985667623 scopus 로고
    • Stabilities of nearest neighbour doublets in double-helical DNA determined by fitting calculated melting profiles to observed profiles
    • Gotoh O., Tagashira Y. Stabilities of nearest neighbour doublets in double-helical DNA determined by fitting calculated melting profiles to observed profiles. Biopolymers. 20:1981;1033-1042
    • (1981) Biopolymers , vol.20 , pp. 1033-1042
    • Gotoh, O.1    Tagashira, Y.2
  • 8
    • 0023958472 scopus 로고
    • The Specific DNA recognition sequence of the bovine papillomavirus E2 protein is an E2-dependent enhancer
    • Hawley-Nelson P., Androphy E.J., Lowy D.R., Schiller J.T. The Specific DNA recognition sequence of the bovine papillomavirus E2 protein is an E2-dependent enhancer. EMBO J. 7:(2):1988;525-531
    • (1988) EMBO J. , vol.7 , Issue.2 , pp. 525-531
    • Hawley-Nelson, P.1    Androphy, E.J.2    Lowy, D.R.3    Schiller, J.T.4
  • 10
    • 13144305254 scopus 로고    scopus 로고
    • Protein-DNA Interactions: The papillomavirus E2 proteins as a model system
    • Bush A.C. Greenwich, CT: JAI Press
    • Hegde R.S. Protein-DNA Interactions the papillomavirus E2 proteins as a model system. Bush A.C. Advances in Biophysical Chemistry. 6:1997;JAI Press, Greenwich, CT
    • (1997) Advances in Biophysical Chemistry , vol.6
    • Hegde, R.S.1
  • 11
    • 0026656038 scopus 로고
    • Crystal structure at 1.7 Å of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target
    • Hegde R.S., Grossman S.R., Laimins L.A., Sigler P.B. Crystal structure at 1.7 Å of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target. Nature. 359:1992;505-512
    • (1992) Nature , vol.359 , pp. 505-512
    • Hegde, R.S.1    Grossman, S.R.2    Laimins, L.A.3    Sigler, P.B.4
  • 12
    • 0032489427 scopus 로고    scopus 로고
    • Quaternary structural rearrangement accompanies the sequence-specific DNA-binding of the bovine papillomavirus-1 E2 protein
    • Hegde R.S., Wang A.-F., Kim S.-S., Schapira M. Quaternary structural rearrangement accompanies the sequence-specific DNA-binding of the bovine papillomavirus-1 E2 protein. J. Mol. Biol. 276:1998;797-808
    • (1998) J. Mol. Biol. , vol.276 , pp. 797-808
    • Hegde, R.S.1    Wang, A.-F.2    Kim, S.-S.3    Schapira, M.4
  • 13
    • 0018791736 scopus 로고
    • A hypothesis on a specific sequence-dependent conformation of DNA and its relation to the binding of the lac-repressor protein
    • Klug A., Jack A., Viswamitra M.A., Kennard O., Shakked Z., Steitz T.A. A hypothesis on a specific sequence-dependent conformation of DNA and its relation to the binding of the lac-repressor protein. J.Mol. Biol. 131:1979;669-680
    • (1979) J.Mol. Biol. , vol.131 , pp. 669-680
    • Klug, A.1    Jack, A.2    Viswamitra, M.A.3    Kennard, O.4    Shakked, Z.5    Steitz, T.A.6
  • 14
    • 0023187152 scopus 로고
    • Effect of non-contacted bases on the affinity of 434 operator for 434 repressor and cro
    • Koudelka C.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;886-889
    • (1987) Nature , vol.326 , pp. 886-889
    • Koudelka, C.B.1    Harrison, S.C.2    Ptashne, M.3
  • 15
    • 0026595235 scopus 로고
    • DNA twisting and the effects of non-contacted bases on the affinity of 434 repressor for 434 operator
    • Koudelka G.B., Carlson P. DNA twisting and the effects of non-contacted bases on the affinity of 434 repressor for 434 operator. Nature. 355:1992;89-91
    • (1992) Nature , vol.355 , pp. 89-91
    • Koudelka, G.B.1    Carlson, P.2
  • 16
    • 0024654340 scopus 로고
    • Specific recognition nucleotides and their DNA context determine the affinity of E2 protein for 17 binding sites in the BPV-1 genome
    • Li R., Knight J., Bream G., Stenlund A., Botchan M. Specific recognition nucleotides and their DNA context determine the affinity of E2 protein for 17 binding sites in the BPV-1 genome. Genes Dev. 3:1989;510-526
    • (1989) Genes Dev. , vol.3 , pp. 510-526
    • Li, R.1    Knight, J.2    Bream, G.3    Stenlund, A.4    Botchan, M.5
  • 17
    • 0023958594 scopus 로고
    • The carboxy-terminal domain shared by the bovine papillomavirus E2 transactivator and repressor proteins contains a specific DNA binding activity
    • McBride A.A., Schlegel R., Howley P.M. The carboxy-terminal domain shared by the bovine papillomavirus E2 transactivator and repressor proteins contains a specific DNA binding activity. EMBO J. 7:1988;533-539
    • (1988) EMBO J. , vol.7 , pp. 533-539
    • McBride, A.A.1    Schlegel, R.2    Howley, P.M.3
  • 18
    • 0030064186 scopus 로고    scopus 로고
    • Equilibrium dissociation and unfolding of the dimeric human papillomavirus strain-16 E2 DNA-binding domain
    • Mok Y.-K., Gay G.D.P., Jonathan B.P., Bycroft M. Equilibrium dissociation and unfolding of the dimeric human papillomavirus strain-16 E2 DNA-binding domain. Protein Sci. 5:1996;310-319
    • (1996) Protein Sci. , vol.5 , pp. 310-319
    • Mok, Y.-K.1    Gay, G.D.P.2    Jonathan, B.P.3    Bycroft, M.4
  • 19
    • 0024434513 scopus 로고
    • Trans activation by the bovine papillomavirus E2 protein in Saccharomyces cerevisae
    • Morrissey L.C., Barsoum J., Androphy E.J. Trans activation by the bovine papillomavirus E2 protein in Saccharomyces cerevisae. J. Virol. 63:1989;4422-4425
    • (1989) J. Virol. , vol.63 , pp. 4422-4425
    • Morrissey, L.C.1    Barsoum, J.2    Androphy, E.J.3
  • 20
    • 0023892684 scopus 로고
    • Interaction of the bovine papillomavirus type I E2 transcriptional control protein with the viral Enhancer: Purification of the DNA-Binding domain and analysis of its contact points with DNA
    • Moskaluk C., Bastia D. Interaction of the bovine papillomavirus type I E2 transcriptional control protein with the viral Enhancer purification of the DNA-Binding domain and analysis of its contact points with DNA. J. Virol. 62:(8):1988;1925-1931
    • (1988) J. Virol. , vol.62 , Issue.8 , pp. 1925-1931
    • Moskaluk, C.1    Bastia, D.2
  • 21
    • 0023513912 scopus 로고
    • The structure of an oligo(dA)-oligo(dT) tract and its biological implications
    • Nelson H.C.M., Finch J.T., Luisi B.F., Klug A. The structure of an oligo(dA)-oligo(dT) tract and its biological implications. Nature. 330:1987;221-226
    • (1987) Nature , vol.330 , pp. 221-226
    • Nelson, H.C.M.1    Finch, J.T.2    Luisi, B.F.3    Klug, A.4
  • 22
    • 0004194541 scopus 로고
    • Cambridge, MA: Cell Press/Blackwell Science
    • Ptashne M. A Genetic Switch. 1986;Cell Press/Blackwell Science, Cambridge, MA
    • (1986) A Genetic Switch
    • Ptashne, M.1
  • 24
    • 0028589386 scopus 로고
    • Kinetic and equilibrium studies of the human papillomavirus type-16 transcription regulatory protein E2 interacting with core enhancer elements
    • Sanders C.M., Maitland N.J. Kinetic and equilibrium studies of the human papillomavirus type-16 transcription regulatory protein E2 interacting with core enhancer elements. Nucl. Acids Res. 22:(22):1994;4890-4897
    • (1994) Nucl. Acids Res. , vol.22 , Issue.22 , pp. 4890-4897
    • Sanders, C.M.1    Maitland, N.J.2
  • 26
    • 0025768548 scopus 로고
    • Determination of binding constants for cooperative site-specific Protein-DNA interactions using the Gel-Mobility Shift assay
    • Senear D.F., Brenowitz M. Determination of binding constants for cooperative site-specific Protein-DNA interactions using the Gel-Mobility Shift assay. J. Biol. Chem. 266:1991;13661-13671
    • (1991) J. Biol. Chem. , vol.266 , pp. 13661-13671
    • Senear, D.F.1    Brenowitz, M.2
  • 27
    • 0027308214 scopus 로고
    • Effects of anomalous migration and DNA protein ratios on the resolution of equilibrium constants from gel-mobility shift assays
    • Senear D.F., Dalma-Weishaus D., Brenowitz M. Effects of anomalous migration and DNA protein ratios on the resolution of equilibrium constants from gel-mobility shift assays. Electrophoresis. 14:1993;704-712
    • (1993) Electrophoresis , vol.14 , pp. 704-712
    • Senear, D.F.1    Dalma-Weishaus, D.2    Brenowitz, M.3
  • 28
    • 0025372735 scopus 로고
    • Characterization of the structure and melting of DNAs containing backbone nicks and gaps
    • Snowden-Ifft E.A., Wemmer D.E. Characterization of the structure and melting of DNAs containing backbone nicks and gaps. Biochemistry. 29:(25):1990;6017-6025
    • (1990) Biochemistry , vol.29 , Issue.25 , pp. 6017-6025
    • Snowden-Ifft, E.A.1    Wemmer, D.E.2
  • 29
    • 0022356562 scopus 로고
    • Transactivation of a bovine papillomavirus transcriptional regulatory element by the E2 gene product
    • Spalholz B.A., Yang Y., Howley P.M. Transactivation of a bovine papillomavirus transcriptional regulatory element by the E2 gene product. Cell. 42:1985;183-191
    • (1985) Cell , vol.42 , pp. 183-191
    • Spalholz, B.A.1    Yang, Y.2    Howley, P.M.3
  • 30
    • 0031060198 scopus 로고    scopus 로고
    • Dose-dependent regulation of the early promoter of human papillomavirus type 18 by the viral E2 protein
    • Steger G., Corbach S. Dose-dependent regulation of the early promoter of human papillomavirus type 18 by the viral E2 protein. J. Virol. 71:(1):1997;50-58
    • (1997) J. Virol. , vol.71 , Issue.1 , pp. 50-58
    • Steger, G.1    Corbach, S.2
  • 31
    • 9544221456 scopus 로고
    • Protein-induced DNA bending
    • F. Eckstein, Lilley D.M.J. Berlin, Heidelberg: Springer-Verlag
    • Travers A.A. Protein-induced DNA bending. Eckstein F., Lilley D.M.J. Nucleic Acids and Molecular Biology. 2:1988;136-148 Springer-Verlag, Berlin, Heidelberg
    • (1988) Nucleic Acids and Molecular Biology , vol.2 , pp. 136-148
    • Travers, A.A.1
  • 32
    • 0026034125 scopus 로고
    • Transient replication of BPV-1 requires two viral polypeptides encoded by the E1 and E2 open reading frames
    • Ustav M., Stenlund A. Transient replication of BPV-1 requires two viral polypeptides encoded by the E1 and E2 open reading frames. EMBO J. 10:1991;449-457
    • (1991) EMBO J. , vol.10 , pp. 449-457
    • Ustav, M.1    Stenlund, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.