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Volumn 89, Issue 4, 2007, Pages 528-533

TBP binding capacity of the TATA box is associated with specific structural properties: AFM study of the IL-2R alpha gene promoter

Author keywords

Atomic Force Microscopy (AFM) in liquid; DNA curvature; DNA flexibility; IL2 R promoter; TATA box

Indexed keywords

CURVED DNA; INTERLEUKIN 2 RECEPTOR ALPHA; TATA BINDING PROTEIN;

EID: 34247357468     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2006.12.004     Document Type: Article
Times cited : (8)

References (23)
  • 1
    • 0029900290 scopus 로고    scopus 로고
    • Common DNA structural features exhibited by eukaryotic ribosomal gene promoters
    • Marilley M., and Pasero P. Common DNA structural features exhibited by eukaryotic ribosomal gene promoters. Nucleic Acids Res. 24 (1996) 2204-2211
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2204-2211
    • Marilley, M.1    Pasero, P.2
  • 2
    • 28544442712 scopus 로고    scopus 로고
    • Fine mapping of inherent flexibility variation along DNA molecules: validation by atomic force microscopy (AFM) in buffer
    • Marilley M., Sanchez-Sevilla A., and Rocca-Serra J. Fine mapping of inherent flexibility variation along DNA molecules: validation by atomic force microscopy (AFM) in buffer. Mol. Genet. Genomics 274 (2005) 658-670
    • (2005) Mol. Genet. Genomics , vol.274 , pp. 658-670
    • Marilley, M.1    Sanchez-Sevilla, A.2    Rocca-Serra, J.3
  • 3
    • 0023649621 scopus 로고
    • Regulation of the human interleukin-2 receptor alpha chain promoter: activation of a non-functional promoter by the transactivator gene of HTLV-I
    • Cross S.L., Feinberg M., Wolf J.B., Holbrook N.J., Wong-Staal F., and Leonard W.J. Regulation of the human interleukin-2 receptor alpha chain promoter: activation of a non-functional promoter by the transactivator gene of HTLV-I. Cell 49 (1987) 47-56
    • (1987) Cell , vol.49 , pp. 47-56
    • Cross, S.L.1    Feinberg, M.2    Wolf, J.B.3    Holbrook, N.J.4    Wong-Staal, F.5    Leonard, W.J.6
  • 4
    • 0025138985 scopus 로고
    • Delineation of an enhancerlike positive regulatory element in the interleukin-2 receptor alpha-chain gene
    • Lin B.B., Cross S.L., Halden N.F., Roman D.G., Toledano M.B., and Leonard W.J. Delineation of an enhancerlike positive regulatory element in the interleukin-2 receptor alpha-chain gene. Mol. Cell Biol. 10 (1990) 850-853
    • (1990) Mol. Cell Biol. , vol.10 , pp. 850-853
    • Lin, B.B.1    Cross, S.L.2    Halden, N.F.3    Roman, D.G.4    Toledano, M.B.5    Leonard, W.J.6
  • 5
    • 0025261347 scopus 로고
    • The same target sequences are differentially important for activation of the interleukin 2 receptor alpha-chain gene in two distinct T-cell lines
    • Toledano M.B., Roman D.G., Halden N.F., Lin B.B., and Leonard W.J. The same target sequences are differentially important for activation of the interleukin 2 receptor alpha-chain gene in two distinct T-cell lines. Proc. Natl. Acad. Sci. USA 87 (1990) 1830-1834
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1830-1834
    • Toledano, M.B.1    Roman, D.G.2    Halden, N.F.3    Lin, B.B.4    Leonard, W.J.5
  • 6
    • 0027499605 scopus 로고
    • Interaction between NF-kappa B- and serum response factor-binding elements activates an interleukin-2 receptor alpha-chain enhancer specifically in T lymphocytes
    • Kuang A.A., Novak K.D., Kang S.M., Bruhn K., and Lenardo M.J. Interaction between NF-kappa B- and serum response factor-binding elements activates an interleukin-2 receptor alpha-chain enhancer specifically in T lymphocytes. Mol. Cell Biol. 13 (1993) 2536-2545
    • (1993) Mol. Cell Biol. , vol.13 , pp. 2536-2545
    • Kuang, A.A.1    Novak, K.D.2    Kang, S.M.3    Bruhn, K.4    Lenardo, M.J.5
  • 7
    • 0028889159 scopus 로고
    • Regulation of cell-type-specific interleukin-2 receptor alpha-chain gene expression: potential role of physical interactions between Elf-1, HMG-I(Y), and NF-kappa B family proteins
    • John S., Reeves R.B., Lin J.X., Child R., Leiden J.M., Thompson C.B., and Leonard W.J. Regulation of cell-type-specific interleukin-2 receptor alpha-chain gene expression: potential role of physical interactions between Elf-1, HMG-I(Y), and NF-kappa B family proteins. Mol. Cell Biol. 15 (1995) 1786-1796
    • (1995) Mol. Cell Biol. , vol.15 , pp. 1786-1796
    • John, S.1    Reeves, R.B.2    Lin, J.X.3    Child, R.4    Leiden, J.M.5    Thompson, C.B.6    Leonard, W.J.7
  • 9
    • 0036290074 scopus 로고    scopus 로고
    • Accuracy of AFM measurements of the contour length of DNA fragments adsorbed on mica in air and in aqueous buffer
    • Sanchez-Sevilla A., Thimonier J., Marilley M., Rocca-Serra J., and Barbet J. Accuracy of AFM measurements of the contour length of DNA fragments adsorbed on mica in air and in aqueous buffer. Ultramicroscopy 92 (2002) 151-158
    • (2002) Ultramicroscopy , vol.92 , pp. 151-158
    • Sanchez-Sevilla, A.1    Thimonier, J.2    Marilley, M.3    Rocca-Serra, J.4    Barbet, J.5
  • 10
    • 0029619641 scopus 로고
    • Reversal of intrinsic DNA bends in the IFN beta gene enhancer by transcription factors and the architectural protein HMG I(Y)
    • Falvo J.V., Thanos D., and Maniatis T. Reversal of intrinsic DNA bends in the IFN beta gene enhancer by transcription factors and the architectural protein HMG I(Y). Cell 83 (1995) 1101-1111
    • (1995) Cell , vol.83 , pp. 1101-1111
    • Falvo, J.V.1    Thanos, D.2    Maniatis, T.3
  • 11
    • 0344505734 scopus 로고    scopus 로고
    • A sequence based computational identification of a Drosophila developmentally regulated TATA-less RNA polymerase II promoter and its experimental validation
    • Santoni M.J., Ait-Ahmed O., and Marilley M. A sequence based computational identification of a Drosophila developmentally regulated TATA-less RNA polymerase II promoter and its experimental validation. Biochim. Biophys. Acta. 1399 (1998) 117-125
    • (1998) Biochim. Biophys. Acta. , vol.1399 , pp. 117-125
    • Santoni, M.J.1    Ait-Ahmed, O.2    Marilley, M.3
  • 12
    • 0032213753 scopus 로고    scopus 로고
    • Inherent DNA curvature and flexibility correlate with TATA box functionality
    • de Souza O.N., and Ornstein R.L. Inherent DNA curvature and flexibility correlate with TATA box functionality. Biopolymers 46 (1998) 403-415
    • (1998) Biopolymers , vol.46 , pp. 403-415
    • de Souza, O.N.1    Ornstein, R.L.2
  • 13
    • 0032812795 scopus 로고    scopus 로고
    • TATA box DNA deformation with and without the TATA box-binding protein
    • Davis N.A., Majee S.S., and Kahn J.D. TATA box DNA deformation with and without the TATA box-binding protein. J. Mol. Biol. 291 (1999) 249-265
    • (1999) J. Mol. Biol. , vol.291 , pp. 249-265
    • Davis, N.A.1    Majee, S.S.2    Kahn, J.D.3
  • 14
    • 7444244495 scopus 로고    scopus 로고
    • Core promoter elements of eukaryotic genes have a highly distinctive mechanical property
    • Fukue Y., Sumida N., Nishikawa J., and Ohyama T. Core promoter elements of eukaryotic genes have a highly distinctive mechanical property. Nucleic Acids Res. 32 (2004) 5834-5840
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5834-5840
    • Fukue, Y.1    Sumida, N.2    Nishikawa, J.3    Ohyama, T.4
  • 15
    • 22444448187 scopus 로고    scopus 로고
    • A highly distinctive mechanical property found in the majority of human promoters and its transcriptional relevance
    • Fukue Y., Sumida N., Tanase J., and Ohyama T. A highly distinctive mechanical property found in the majority of human promoters and its transcriptional relevance. Nucleic Acids Res. 33 (2005) 3821-3827
    • (2005) Nucleic Acids Res. , vol.33 , pp. 3821-3827
    • Fukue, Y.1    Sumida, N.2    Tanase, J.3    Ohyama, T.4
  • 16
    • 0032475962 scopus 로고    scopus 로고
    • Affinity, stability and polarity of binding of the TATA binding protein governed by flexure at the TATA Box
    • Grove A., Galeone A., Yu E., Mayol L., and Geiduschek E.P. Affinity, stability and polarity of binding of the TATA binding protein governed by flexure at the TATA Box. J. Mol. Biol. 282 (1998) 731-739
    • (1998) J. Mol. Biol. , vol.282 , pp. 731-739
    • Grove, A.1    Galeone, A.2    Yu, E.3    Mayol, L.4    Geiduschek, E.P.5
  • 18
    • 0027483012 scopus 로고
    • Co-crystal structure of TBP recognizing the minor groove of a TATA element
    • Kim J.L., Nikolov D.B., and Burley S.K. Co-crystal structure of TBP recognizing the minor groove of a TATA element. Nature 365 (1993) 520-527
    • (1993) Nature , vol.365 , pp. 520-527
    • Kim, J.L.1    Nikolov, D.B.2    Burley, S.K.3
  • 19
    • 0027504913 scopus 로고
    • Crystal structure of a yeast TBP/TATA-box complex
    • Kim Y., Geiger J.H., Hahn S., and Sigler P.B. Crystal structure of a yeast TBP/TATA-box complex. Nature 365 (1993) 512-520
    • (1993) Nature , vol.365 , pp. 512-520
    • Kim, Y.1    Geiger, J.H.2    Hahn, S.3    Sigler, P.B.4
  • 22
    • 0037040419 scopus 로고    scopus 로고
    • A regulated two-step mechanism of TBP binding to DNA: a solvent-exposed surface of TBP inhibits TATA box recognition
    • Zhao X., and Herr W. A regulated two-step mechanism of TBP binding to DNA: a solvent-exposed surface of TBP inhibits TATA box recognition. Cell 108 (2002) 615-627
    • (2002) Cell , vol.108 , pp. 615-627
    • Zhao, X.1    Herr, W.2
  • 23
    • 0037040899 scopus 로고    scopus 로고
    • Comparison of TATA-binding protein recognition of a variant and consensus DNA promoters
    • Powell R.M., Parkhurst K.M., and Parkhurst L.J. Comparison of TATA-binding protein recognition of a variant and consensus DNA promoters. J. Biol. Chem. 277 (2002) 7776-7784
    • (2002) J. Biol. Chem. , vol.277 , pp. 7776-7784
    • Powell, R.M.1    Parkhurst, K.M.2    Parkhurst, L.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.