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Volumn 22, Issue 6, 2006, Pages 741-753

Structural Basis of DNA Recognition by p53 Tetramers

Author keywords

CELLCYCLE; DNA

Indexed keywords

DIMER; DNA; PROTEIN P53; TETRAMER;

EID: 33745209412     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2006.05.015     Document Type: Article
Times cited : (330)

References (61)
  • 1
    • 0034862475 scopus 로고    scopus 로고
    • The C-terminus of p53: the more you learn the less you know
    • Ahn J., and Prives C. The C-terminus of p53: the more you learn the less you know. Nat. Struct. Biol. 8 (2001) 730-732
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 730-732
    • Ahn, J.1    Prives, C.2
  • 2
    • 2942612843 scopus 로고    scopus 로고
    • Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53
    • An W., Kim J., and Roeder R.G. Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. Cell 117 (2004) 735-748
    • (2004) Cell , vol.117 , pp. 735-748
    • An, W.1    Kim, J.2    Roeder, R.G.3
  • 3
    • 0036415663 scopus 로고    scopus 로고
    • p53 contains large unstructured regions in its native state
    • Bell S., Klein C., Muller L., Hansen S., and Buchner J. p53 contains large unstructured regions in its native state. J. Mol. Biol. 322 (2002) 917-927
    • (2002) J. Mol. Biol. , vol.322 , pp. 917-927
    • Bell, S.1    Klein, C.2    Muller, L.3    Hansen, S.4    Buchner, J.5
  • 6
    • 0035496607 scopus 로고    scopus 로고
    • Rescuing the function of mutant p53
    • Bullock A.N., and Fersht A.R. Rescuing the function of mutant p53. Nat. Rev. Cancer 1 (2001) 68-76
    • (2001) Nat. Rev. Cancer , vol.1 , pp. 68-76
    • Bullock, A.N.1    Fersht, A.R.2
  • 7
    • 0034704175 scopus 로고    scopus 로고
    • The N terminus of p53 regulates its dissociation from DNA
    • Cain C., Miller S., Ahn J., and Prives C. The N terminus of p53 regulates its dissociation from DNA. J. Biol. Chem. 275 (2000) 39944-39953
    • (2000) J. Biol. Chem. , vol.275 , pp. 39944-39953
    • Cain, C.1    Miller, S.2    Ahn, J.3    Prives, C.4
  • 8
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations
    • Cho Y., Gorina S., Jeffrey P.D., and Pavletich N.P. Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 265 (1994) 346-355
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 14
    • 0034881964 scopus 로고    scopus 로고
    • Transcriptional regulation by p53 through intrinsic DNA/chromatin binding and site-directed cofactor recruitment
    • Espinosa J.M., and Emerson B.M. Transcriptional regulation by p53 through intrinsic DNA/chromatin binding and site-directed cofactor recruitment. Mol. Cell 8 (2001) 57-69
    • (2001) Mol. Cell , vol.8 , pp. 57-69
    • Espinosa, J.M.1    Emerson, B.M.2
  • 15
    • 0027522365 scopus 로고
    • The p53 protein is an unusually shaped tetramer that binds directly to DNA
    • Friedman P.N., Chen X., Bargonetti J., and Prives C. The p53 protein is an unusually shaped tetramer that binds directly to DNA. Proc. Natl. Acad. Sci. USA 90 (1993) 3319-3323
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3319-3323
    • Friedman, P.N.1    Chen, X.2    Bargonetti, J.3    Prives, C.4
  • 16
    • 0026650531 scopus 로고
    • A transcriptionally active DNA binding site for human p53 protein complexes
    • Funk W.D., Pak D.T., Karas R.H., Wright W.E., and Shay J.W. A transcriptionally active DNA binding site for human p53 protein complexes. Mol. Cell. Biol. 12 (1992) 2866-2871
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2866-2871
    • Funk, W.D.1    Pak, D.T.2    Karas, R.H.3    Wright, W.E.4    Shay, J.W.5
  • 17
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2
    • Gorina S., and Pavletich N.P. Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science 274 (1996) 1001-1005
    • (1996) Science , vol.274 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 18
    • 0026652596 scopus 로고
    • The DNA target of the trp repressor
    • Haran T.E., Joachimiak A., and Sigler P.B. The DNA target of the trp repressor. EMBO J. 11 (1992) 3021-3030
    • (1992) EMBO J. , vol.11 , pp. 3021-3030
    • Haran, T.E.1    Joachimiak, A.2    Sigler, P.B.3
  • 19
    • 0036892060 scopus 로고    scopus 로고
    • Differential transactivation by the p53 transcription factor is highly dependent on p53 level and promoter target sequence
    • Inga A., Storici F., Darden T.A., and Resnick M.A. Differential transactivation by the p53 transcription factor is highly dependent on p53 level and promoter target sequence. Mol. Cell. Biol. 22 (2002) 8612-8625
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8612-8625
    • Inga, A.1    Storici, F.2    Darden, T.A.3    Resnick, M.A.4
  • 20
    • 0033027346 scopus 로고    scopus 로고
    • Covalent and noncovalent modifiers of the p53 protein
    • Jayaraman L., and Prives C. Covalent and noncovalent modifiers of the p53 protein. Cell. Mol. Life Sci. 55 (1999) 76-87
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 76-87
    • Jayaraman, L.1    Prives, C.2
  • 21
    • 0028952841 scopus 로고
    • Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms
    • Jeffrey P.D., Gorina S., and Pavletich N.P. Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms. Science 267 (1995) 1498-1502
    • (1995) Science , vol.267 , pp. 1498-1502
    • Jeffrey, P.D.1    Gorina, S.2    Pavletich, N.P.3
  • 22
    • 0036500691 scopus 로고    scopus 로고
    • Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure
    • Joo W.S., Jeffrey P.D., Cantor S.B., Finnin M.S., Livingston D.M., and Pavletich N.P. Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure. Genes Dev. 16 (2002) 583-593
    • (2002) Genes Dev. , vol.16 , pp. 583-593
    • Joo, W.S.1    Jeffrey, P.D.2    Cantor, S.B.3    Finnin, M.S.4    Livingston, D.M.5    Pavletich, N.P.6
  • 23
    • 0037039319 scopus 로고    scopus 로고
    • Chromatin immunoprecipitation analysis fails to support the latency model for regulation of p53 DNA binding activity in vivo
    • Kaeser M.D., and Iggo R.D. Chromatin immunoprecipitation analysis fails to support the latency model for regulation of p53 DNA binding activity in vivo. Proc. Natl. Acad. Sci. USA 99 (2002) 95-100
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 95-100
    • Kaeser, M.D.1    Iggo, R.D.2
  • 24
    • 33646809388 scopus 로고    scopus 로고
    • The versatile interactions of p53 with DNA: when flexibility serves specificity
    • Kim E., and Deppert W. The versatile interactions of p53 with DNA: when flexibility serves specificity. Cell Death Differ. 13 (2006) 885-889
    • (2006) Cell Death Differ. , vol.13 , pp. 885-889
    • Kim, E.1    Deppert, W.2
  • 25
    • 0035966083 scopus 로고    scopus 로고
    • NMR spectroscopy reveals the solution dimerization interface of p53 core domains bound to their consensus DNA
    • Klein C., Planker E., Diercks T., Kessler H., Kunkele K.P., Lang K., Hansen S., and Schwaiger M. NMR spectroscopy reveals the solution dimerization interface of p53 core domains bound to their consensus DNA. J. Biol. Chem. 276 (2001) 49020-49027
    • (2001) J. Biol. Chem. , vol.276 , pp. 49020-49027
    • Klein, C.1    Planker, E.2    Diercks, T.3    Kessler, H.4    Kunkele, K.P.5    Lang, K.6    Hansen, S.7    Schwaiger, M.8
  • 26
    • 0029972806 scopus 로고    scopus 로고
    • p53: puzzle and paradigm
    • Ko J., and Prives C. p53: puzzle and paradigm. Genes Dev. 10 (1996) 1054-1072
    • (1996) Genes Dev. , vol.10 , pp. 1054-1072
    • Ko, J.1    Prives, C.2
  • 27
    • 0024539180 scopus 로고
    • Defining the structure of irregular nucleic acids: conventions and principles
    • Lavery R., and Sklenar H. Defining the structure of irregular nucleic acids: conventions and principles. J. Biomol. Struct. Dyn. 6 (1989) 655-667
    • (1989) J. Biomol. Struct. Dyn. , vol.6 , pp. 655-667
    • Lavery, R.1    Sklenar, H.2
  • 29
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine A.J. p53, the cellular gatekeeper for growth and division. Cell 88 (1997) 323-331
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 30
    • 22144452221 scopus 로고    scopus 로고
    • Facilitated search for specific genomic targets by p53 C-terminal basic DNA binding domain
    • Liu Y., Lagowski J.P., Vanderbeek G.E., and Kulesz-Martin M.F. Facilitated search for specific genomic targets by p53 C-terminal basic DNA binding domain. Cancer Biol. Ther. 3 (2004) 1102-1108
    • (2004) Cancer Biol. Ther. , vol.3 , pp. 1102-1108
    • Liu, Y.1    Lagowski, J.P.2    Vanderbeek, G.E.3    Kulesz-Martin, M.F.4
  • 31
    • 0035393302 scopus 로고    scopus 로고
    • Amino acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level
    • Luscombe N.M., Laskowski R.A., and Thornton J.M. Amino acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level. Nucleic Acids Res. 29 (2001) 2860-2874
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2860-2874
    • Luscombe, N.M.1    Laskowski, R.A.2    Thornton, J.M.3
  • 32
    • 0033552638 scopus 로고    scopus 로고
    • Twenty years of p53 research: structural and functional aspects of the p53 protein
    • May P., and May E. Twenty years of p53 research: structural and functional aspects of the p53 protein. Oncogene 18 (1999) 7621-7636
    • (1999) Oncogene , vol.18 , pp. 7621-7636
    • May, P.1    May, E.2
  • 33
    • 8644241631 scopus 로고    scopus 로고
    • p53 linear diffusion along DNA requires its C terminus
    • McKinney K., Mattia M., Gottifredi V., and Prives C. p53 linear diffusion along DNA requires its C terminus. Mol. Cell 16 (2004) 413-424
    • (2004) Mol. Cell , vol.16 , pp. 413-424
    • McKinney, K.1    Mattia, M.2    Gottifredi, V.3    Prives, C.4
  • 34
    • 0032526426 scopus 로고    scopus 로고
    • How p53 binds DNA as a tetramer
    • McLure K.G., and Lee P.W.K. How p53 binds DNA as a tetramer. EMBO J. 17 (1998) 3342-3350
    • (1998) EMBO J. , vol.17 , pp. 3342-3350
    • McLure, K.G.1    Lee, P.W.K.2
  • 35
    • 0031951844 scopus 로고    scopus 로고
    • Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template
    • Mittl P.R., Chene P., and Grutter M.G. Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template. Acta Crystallogr. D Biol. Crystallogr. 54 (1998) 86-89
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 86-89
    • Mittl, P.R.1    Chene, P.2    Grutter, M.G.3
  • 37
    • 0033515035 scopus 로고    scopus 로고
    • p53-induced DNA bending and twisting: p53 tetramer binds on the outer side of a DNA loop and increses DNA twisting
    • Nagaich A., Zhurkin V.B., Durrel S.R., Jernigan R.L., Appella E., and Harrington R.E. p53-induced DNA bending and twisting: p53 tetramer binds on the outer side of a DNA loop and increses DNA twisting. Proc. Natl. Acad. Sci. USA 96 (1999) 1875-1880
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1875-1880
    • Nagaich, A.1    Zhurkin, V.B.2    Durrel, S.R.3    Jernigan, R.L.4    Appella, E.5    Harrington, R.E.6
  • 38
    • 0036258111 scopus 로고    scopus 로고
    • The IARC TP53 database: new online mutation analysis and recommendations to users
    • Olivier M., Eeles R., Hollstein M., Khan M.A., Harris C.C., and Hainaut P. The IARC TP53 database: new online mutation analysis and recommendations to users. Hum. Mutat. 19 (2002) 607-614
    • (2002) Hum. Mutat. , vol.19 , pp. 607-614
    • Olivier, M.1    Eeles, R.2    Hollstein, M.3    Khan, M.A.4    Harris, C.C.5    Hainaut, P.6
  • 39
    • 0038075338 scopus 로고    scopus 로고
    • Decision making by p53: life, death and cancer
    • Oren M. Decision making by p53: life, death and cancer. Cell Death Differ. 10 (2003) 431-442
    • (2003) Cell Death Differ. , vol.10 , pp. 431-442
    • Oren, M.1
  • 40
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carter Jr. C.W., and Sweet M. (Eds), Academic Press, New York
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. In: Carter Jr. C.W., and Sweet M. (Eds). Methods in Enzymology (1997), Academic Press, New York 307-326
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 41
    • 0032931517 scopus 로고    scopus 로고
    • The p53 pathway
    • Prives C., and Hall P.A. The p53 pathway. J. Pathol. 187 (1999) 112-126
    • (1999) J. Pathol. , vol.187 , pp. 112-126
    • Prives, C.1    Hall, P.A.2
  • 42
    • 0037038699 scopus 로고    scopus 로고
    • Groups of p53 target genes involved in specific p53 downstream effects cluster into different classes of DNA binding sites
    • Qian H., Wang T., Naumovski L., Lopez C.D., and Brachmann R.K. Groups of p53 target genes involved in specific p53 downstream effects cluster into different classes of DNA binding sites. Oncogene 21 (2002) 7901-7911
    • (2002) Oncogene , vol.21 , pp. 7901-7911
    • Qian, H.1    Wang, T.2    Naumovski, L.3    Lopez, C.D.4    Brachmann, R.K.5
  • 43
    • 0032528245 scopus 로고    scopus 로고
    • Identification of a novel class of genomic DNA-binding sites suggests a mechanism for selectivity in target gene activation by the tumor suppressor protein p53
    • Resnick-Silverman L., St Clair S., Maurer M., Zhao K., and Manfredi J.J. Identification of a novel class of genomic DNA-binding sites suggests a mechanism for selectivity in target gene activation by the tumor suppressor protein p53. Genes Dev. 12 (1998) 2102-2107
    • (1998) Genes Dev. , vol.12 , pp. 2102-2107
    • Resnick-Silverman, L.1    St Clair, S.2    Maurer, M.3    Zhao, K.4    Manfredi, J.J.5
  • 44
    • 0036301402 scopus 로고    scopus 로고
    • Recognition of DNA by p53 core domain and location of intermolecular contacts of cooperative binding
    • Rippin T.M., Freund S.M., Veprintsev D.B., and Fersht A.R. Recognition of DNA by p53 core domain and location of intermolecular contacts of cooperative binding. J. Mol. Biol. 319 (2002) 351-358
    • (2002) J. Mol. Biol. , vol.319 , pp. 351-358
    • Rippin, T.M.1    Freund, S.M.2    Veprintsev, D.B.3    Fersht, A.R.4
  • 47
    • 0031854480 scopus 로고    scopus 로고
    • Molecular modelling and footprinting studies of DNA minor groove binders: bisquaternary ammonium heterocyclic compounds
    • Slickers P., Hillebrand M., Kittler L., Lober G., and Suhnel J. Molecular modelling and footprinting studies of DNA minor groove binders: bisquaternary ammonium heterocyclic compounds. Anticancer Drug Des. 13 (1998) 463-488
    • (1998) Anticancer Drug Des. , vol.13 , pp. 463-488
    • Slickers, P.1    Hillebrand, M.2    Kittler, L.3    Lober, G.4    Suhnel, J.5
  • 48
    • 0035028599 scopus 로고    scopus 로고
    • Kinetics of p53 binding to promoter sites in vivo
    • Szak S.T., Mays D., and Pietenpol J.A. Kinetics of p53 binding to promoter sites in vivo. Mol. Cell. Biol. 21 (2001) 3375-3386
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3375-3386
    • Szak, S.T.1    Mays, D.2    Pietenpol, J.A.3
  • 49
    • 0033584842 scopus 로고    scopus 로고
    • One mechanism for cell type-specific regulation of the bax promoter by the tumor suppressor p53 is dictated by the p53 response element
    • Thornborrow E.C., and Manfredi J.J. One mechanism for cell type-specific regulation of the bax promoter by the tumor suppressor p53 is dictated by the p53 response element. J. Biol. Chem. 274 (1999) 33747-33756
    • (1999) J. Biol. Chem. , vol.274 , pp. 33747-33756
    • Thornborrow, E.C.1    Manfredi, J.J.2
  • 52
    • 0024531901 scopus 로고
    • Facilitated target location in biological systems
    • von Hippel P.H., and Berg O.G. Facilitated target location in biological systems. J. Biol. Chem. 264 (1989) 675-678
    • (1989) J. Biol. Chem. , vol.264 , pp. 675-678
    • von Hippel, P.H.1    Berg, O.G.2
  • 53
    • 0036674617 scopus 로고    scopus 로고
    • Live or let die: the cell's response to p53
    • Vousden K.H., and Lu X. Live or let die: the cell's response to p53. Nat. Rev. Cancer 2 (2002) 594-604
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 594-604
    • Vousden, K.H.1    Lu, X.2
  • 54
    • 0033531266 scopus 로고    scopus 로고
    • Evolutionary conservation and somatic mutation hotspot maps of p53: correlation with p53 protein structural and functional features
    • Walker D.R., Bond J.P., Tarone R.E., Harris C.C., Makalowski W., Boguski M.S., and Greenblatt M.S. Evolutionary conservation and somatic mutation hotspot maps of p53: correlation with p53 protein structural and functional features. Oncogene 18 (1999) 211-218
    • (1999) Oncogene , vol.18 , pp. 211-218
    • Walker, D.R.1    Bond, J.P.2    Tarone, R.E.3    Harris, C.C.4    Makalowski, W.5    Boguski, M.S.6    Greenblatt, M.S.7
  • 56
    • 0028888020 scopus 로고
    • The dihedral symmetry of the p53 tetramerization domain mandates a conformational switch upon DNA binding
    • Waterman J.L., Shenk J.L., and Halazonetis T.D. The dihedral symmetry of the p53 tetramerization domain mandates a conformational switch upon DNA binding. EMBO J. 14 (1995) 512-519
    • (1995) EMBO J. , vol.14 , pp. 512-519
    • Waterman, J.L.1    Shenk, J.L.2    Halazonetis, T.D.3
  • 58
  • 59
    • 17144399973 scopus 로고    scopus 로고
    • Comparative binding of p53 to its promoter and DNA recognition elements
    • Weinberg R.L., Veprintsev D.B., Bycroft M., and Fersht A.R. Comparative binding of p53 to its promoter and DNA recognition elements. J. Mol. Biol. 348 (2005) 589-596
    • (2005) J. Mol. Biol. , vol.348 , pp. 589-596
    • Weinberg, R.L.1    Veprintsev, D.B.2    Bycroft, M.3    Fersht, A.R.4
  • 60
    • 0042358627 scopus 로고    scopus 로고
    • Analysis of p53 "latency" and "activation" by fluorescence correlation spectroscopy. Evidence for different modes of high affinity DNA binding
    • Wolcke J., Reimann M., Klumpp M., Gohler T., Kim E., and Deppert W. Analysis of p53 "latency" and "activation" by fluorescence correlation spectroscopy. Evidence for different modes of high affinity DNA binding. J. Biol. Chem. 278 (2003) 32587-32595
    • (2003) J. Biol. Chem. , vol.278 , pp. 32587-32595
    • Wolcke, J.1    Reimann, M.2    Klumpp, M.3    Gohler, T.4    Kim, E.5    Deppert, W.6
  • 61
    • 0035853734 scopus 로고    scopus 로고
    • Crystal structure of the mouse p53 core DNA-binding domain at 2.7 A resolution
    • Zhao K., Chai X., Johnston K., Clements A., and Marmorstein R. Crystal structure of the mouse p53 core DNA-binding domain at 2.7 A resolution. J. Biol. Chem. 276 (2001) 12120-12127
    • (2001) J. Biol. Chem. , vol.276 , pp. 12120-12127
    • Zhao, K.1    Chai, X.2    Johnston, K.3    Clements, A.4    Marmorstein, R.5


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