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Volumn 18, Issue 3, 1999, Pages 763-770

p53 DNA binding can be modulated by factors that alter the conformational equilibrium

Author keywords

Conformational states; DNA binding; p53; p53 DNA complex; pAb240

Indexed keywords

DIMER; DNA; MUTANT PROTEIN; PROTEIN P53; REGULATOR PROTEIN; TETRAMER;

EID: 0033081465     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.3.763     Document Type: Article
Times cited : (37)

References (33)
  • 1
    • 0029737509 scopus 로고    scopus 로고
    • Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90
    • Blagosklonny, M.V., Toretsky, J., Bohen, S. and Neckers, L. (1996) Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90. Proc. Natl Acad. Sci. USA, 93, 8379-8383.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8379-8383
    • Blagosklonny, M.V.1    Toretsky, J.2    Bohen, S.3    Neckers, L.4
  • 2
    • 0027969234 scopus 로고
    • Hot-spot p53 mutants interact specifically with two cellular proteins during progression of the cell cycle
    • Chen, Y., Chen, P.-L. and Lee, W.H. (1994) Hot-spot p53 mutants interact specifically with two cellular proteins during progression of the cell cycle. Mol. Cell. Biol., 14, 6764-6772.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6764-6772
    • Chen, Y.1    Chen, P.-L.2    Lee, W.H.3
  • 3
    • 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. (1994) Crystal structure of a p53 tumor suppressor -DNA complex: understanding tumorigenic mutations. Science, 265, 346-355.
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 4
    • 0025214277 scopus 로고
    • Evidence for allosteric variants of wild-type p53, a tumour suppressor protein
    • Cook, A. and Milner, J. (1990) Evidence for allosteric variants of wild-type p53, a tumour suppressor protein. Br. J. Cancer, 61, 548-552.
    • (1990) Br. J. Cancer , vol.61 , pp. 548-552
    • Cook, A.1    Milner, J.2
  • 5
    • 0028137084 scopus 로고
    • p53: A glimpse at the puppet behind the shadow play
    • Friend, S. (1994) p53: a glimpse at the puppet behind the shadow play. Science, 265, 334-335.
    • (1994) Science , vol.265 , pp. 334-335
    • Friend, S.1
  • 6
    • 0025248598 scopus 로고
    • Activating mutations in p53 produce a common conformational effect - A monoclonal antibody specific for the mutant form
    • Gannon, J.V., Greaves, R., Iggo, R. and Lane, D.P. (1990) Activating mutations in p53 produce a common conformational effect - a monoclonal antibody specific for the mutant form. EMBO J., 9, 1595-1602.
    • (1990) EMBO J. , vol.9 , pp. 1595-1602
    • Gannon, J.V.1    Greaves, R.2    Iggo, R.3    Lane, D.P.4
  • 7
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor hound to the ankyrin and SH3 domains of 53BP2
    • Gorina, S. and Pavletich, N.P. (1996) Structure of the p53 tumor suppressor hound to the ankyrin and SH3 domains of 53BP2. Science, 274, 1001-1005.
    • (1996) Science , vol.274 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 8
    • 0026779422 scopus 로고
    • Interaction of heat-shock protein 70 with p53 translated in vitro: Evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation
    • Hainaut, P. and Milner, J. (1992) Interaction of heat-shock protein 70 with p53 translated in vitro: evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation. EMBO J., 11, 3513-20.
    • (1992) EMBO J. , vol.11 , pp. 3513-3520
    • Hainaut, P.1    Milner, J.2
  • 9
    • 0027361046 scopus 로고
    • Redox modulation of p53 conformation and sequence-specific DNA binding in vitro
    • Hainaut P. and Milner J. (1993) Redox modulation of p53 conformation and sequence-specific DNA binding in vitro. Cancer Res., 53, 4469-4473.
    • (1993) Cancer Res. , vol.53 , pp. 4469-4473
    • Hainaut, P.1    Milner, J.2
  • 10
    • 0028830748 scopus 로고
    • Modulation by copper of p53 conformation and sequence-specific DNA binding: Role for Cu (II)/Cu (I) redox mechanism
    • Hainaut, P., Rolley, N., Davies, M. and Milner, J. (1995) Modulation by copper of p53 conformation and sequence-specific DNA binding: role for Cu (II)/Cu (I) redox mechanism. Oncogene, 10, 27-32.
    • (1995) Oncogene , vol.10 , pp. 27-32
    • Hainaut, P.1    Rolley, N.2    Davies, M.3    Milner, J.4
  • 11
    • 0027521114 scopus 로고
    • Conformational shifts propagate from the oligomerization domain of p53 to its tetrameric DNA binding domain and restore DNA binding to select p53 mutants
    • Halazonetis, T.D. and Kandil, A.N. (1993) Conformational shifts propagate from the oligomerization domain of p53 to its tetrameric DNA binding domain and restore DNA binding to select p53 mutants. EMBO J., 12, 5057-5064.
    • (1993) EMBO J. , vol.12 , pp. 5057-5064
    • Halazonetis, T.D.1    Kandil, A.N.2
  • 12
    • 0027407260 scopus 로고
    • Wild-type p53 adopts a 'mutant'-like conformation when bound to DNA
    • Halazonetis, T.D., Davis, L.J. and Kandil, A.N. (1993) Wild-type p53 adopts a 'mutant'-like conformation when bound to DNA. EMBO J., 12, 1021-1028.
    • (1993) EMBO J. , vol.12 , pp. 1021-1028
    • Halazonetis, T.D.1    Davis, L.J.2    Kandil, A.N.3
  • 13
    • 0028804617 scopus 로고
    • Structural and kinetic analysis of p53-DNA complexes and comparison of human and murine p53
    • Hall, A.R. and Milner, J. (1995) Structural and kinetic analysis of p53-DNA complexes and comparison of human and murine p53. Oncogene,. 10, 561-567.
    • (1995) Oncogene , vol.10 , pp. 561-567
    • Hall, A.R.1    Milner, J.2
  • 15
    • 0026448672 scopus 로고
    • Regulation of the specific DNA binding function of p53
    • Hupp, T.R., Meek, D.W., Midgley, C.A. and Lane, D.P. (1992) Regulation of the specific DNA binding function of p53. Cell, 71, 875-886.
    • (1992) Cell , vol.71 , pp. 875-886
    • Hupp, T.R.1    Meek, D.W.2    Midgley, C.A.3    Lane, D.P.4
  • 16
    • 0028845158 scopus 로고
    • Small peptides activated the latent sequence-specific DNA binding function of p53
    • Hupp, T.R., Sparks, A. and Lane, D.P. (1995) Small peptides activated the latent sequence-specific DNA binding function of p53. Cell, 83, 237-245.
    • (1995) Cell , vol.83 , pp. 237-245
    • Hupp, T.R.1    Sparks, A.2    Lane, D.P.3
  • 18
  • 19
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland, D.L., Jr, Nemethy, G. and Filmer, D. (1966) Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry, 5, 365-385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland D.L., Jr.1    Nemethy, G.2    Filmer, D.3
  • 20
    • 0028130284 scopus 로고
    • Mutations in p53 produce a common conformational effect that can be detected with a panel of monoclonal antibodies directed toward the central part of the p53 protein
    • Legros, Y., Meyer, A., Ory, K. and Soussi, T. (1994) Mutations in p53 produce a common conformational effect that can be detected with a panel of monoclonal antibodies directed toward the central part of the p53 protein. Oncogene, 9, 3689-3694.
    • (1994) Oncogene , vol.9 , pp. 3689-3694
    • Legros, Y.1    Meyer, A.2    Ory, K.3    Soussi, T.4
  • 21
    • 0029853272 scopus 로고    scopus 로고
    • + conformation of wild type p53 binds DNA
    • + conformation of wild type p53 binds DNA. Oncogene, 13, 1297-1303.
    • (1996) Oncogene , vol.13 , pp. 1297-1303
    • McLure, K.G.1    Lee, P.W.K.2
  • 22
    • 0032526426 scopus 로고    scopus 로고
    • How p53 binds DNA as a tetramer
    • McLure, K.G. and Lee, P.W.K. (1998) How p53 binds DNA as a tetramer. EMBO J., 17, 3342-3350.
    • (1998) EMBO J. , vol.17 , pp. 3342-3350
    • McLure, K.G.1    Lee, P.W.K.2
  • 23
    • 0028877982 scopus 로고
    • Flexibility: The key to p53 function?
    • Milner, J. (1995) Flexibility: the key to p53 function? Trends Biochem. Sci., 20, 49-51.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 49-51
    • Milner, J.1
  • 24
    • 0022500115 scopus 로고
    • The cellular tumour antigen p53: Evidence for transformation-related, immunological variants of p53
    • Milner, J. and Cook, A. (1986) The cellular tumour antigen p53: evidence for transformation-related, immunological variants of p53. Virology, 154, 21-30.
    • (1986) Virology , vol.154 , pp. 21-30
    • Milner, J.1    Cook, A.2
  • 25
    • 0025605727 scopus 로고
    • Temperature-dependent switching between 'wild-type' and 'mutant' forms of p53-Va1135
    • Milner, J. and Medcalfe, E.A. (1990) Temperature-dependent switching between 'wild-type' and 'mutant' forms of p53-Va1135. J. Mol. Biol., 216, 481-484.
    • (1990) J. Mol. Biol. , vol.216 , pp. 481-484
    • Milner, J.1    Medcalfe, E.A.2
  • 26
    • 0025221676 scopus 로고
    • Addition of fresh medium induces cell cycle and conformation changes in p53, a tumour suppressor protein
    • Milner J. and Watson J.V. (1990) Addition of fresh medium induces cell cycle and conformation changes in p53, a tumour suppressor protein. Oncogene, 5, 1683-1690.
    • (1990) Oncogene , vol.5 , pp. 1683-1690
    • Milner, J.1    Watson, J.V.2
  • 27
    • 0023232266 scopus 로고
    • A new anti-p53 monoclonal antibody, previously reported to be directed against the large T antigen of simian virus 40
    • Milner, J., Cook, A. and Sheldon, M. (1987) A new anti-p53 monoclonal antibody, previously reported to be directed against the large T antigen of simian virus 40. Oncogene, 1, 453-455.
    • (1987) Oncogene , vol.1 , pp. 453-455
    • Milner, J.1    Cook, A.2    Sheldon, M.3
  • 28
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J. and Changeux, J.P. (1965) On the nature of allosteric transitions: a plausible model. J. Mol. Biol., 12, 88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 29
    • 0029125555 scopus 로고
    • Specific DNA binding by different classes of human p53 mutants
    • Rolley, N., Butcher, S. and Milner, J. (1995) Specific DNA binding by different classes of human p53 mutants. Oncogene, 11, 763-770.
    • (1995) Oncogene , vol.11 , pp. 763-770
    • Rolley, N.1    Butcher, S.2    Milner, J.3
  • 30
    • 0028816814 scopus 로고
    • Conformational changes in p53 analysed using new antibodies to the core DNA binding domain of the protein
    • Vojtesek, B. et al. (1995) Conformational changes in p53 analysed using new antibodies to the core DNA binding domain of the protein. Oncogene, 10, 389-393.
    • (1995) Oncogene , vol.10 , pp. 389-393
    • Vojtesek, B.1
  • 31
    • 0028888020 scopus 로고
    • The dihedral symmetry of the p53 tetramerization domain mandates a conformational switch upon DNA binding
    • Waterman, J.L.F., Shenk, J.L. and Halazonetis, T.D. (1995) The dihedral symmetry of the p53 tetramerization domain mandates a conformational switch upon DNA binding. EMBO J., 14, 512-519.
    • (1995) EMBO J. , vol.14 , pp. 512-519
    • Waterman, J.L.F.1    Shenk, J.L.2    Halazonetis, T.D.3
  • 32
    • 0028919075 scopus 로고
    • The DNA binding activity of wild type p53 is modulated by blocking its various antigenic epitopes
    • Wolkowicz, R., Elkind, N.B., Ronen, D. and Rotter, V. (1995) The DNA binding activity of wild type p53 is modulated by blocking its various antigenic epitopes. Oncogene, 10, 1167-1174.
    • (1995) Oncogene , vol.10 , pp. 1167-1174
    • Wolkowicz, R.1    Elkind, N.B.2    Ronen, D.3    Rotter, V.4
  • 33
    • 0027275854 scopus 로고
    • Novel DNA binding of p53 mutants and their role in transcriptional activation
    • Zhang, W., Funk, W.D., Wright, W.E., Shay, J.W. and Deisseroth, A.B. (1993) Novel DNA binding of p53 mutants and their role in transcriptional activation. Oncogene, 8, 2555-2559.
    • (1993) Oncogene , vol.8 , pp. 2555-2559
    • Zhang, W.1    Funk, W.D.2    Wright, W.E.3    Shay, J.W.4    Deisseroth, A.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.