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Volumn 46, Issue 10, 2007, Pages 2630-2639

Zn2+-dependent misfolding of the p53 DNA binding domain

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; MOLECULAR STRUCTURE; PROTEINS; REACTION KINETICS; STOICHIOMETRY; ZINC COMPOUNDS;

EID: 33947241339     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi062106y     Document Type: Article
Times cited : (50)

References (40)
  • 1
    • 0034676455 scopus 로고    scopus 로고
    • Surfing the p53 network
    • Vogelstein, B., Lane, D., and Levine, A. J. (2000) Surfing the p53 network, Nature 408, 307-310.
    • (2000) Nature , vol.408 , pp. 307-310
    • Vogelstein, B.1    Lane, D.2    Levine, A.J.3
  • 2
    • 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 Hainault, P. (2002) The IARC TP53 database: new online mutation analysis and recommendations to users, Hum. Mutat. 19, 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    Hainault, P.6
  • 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
  • 5
    • 0034594995 scopus 로고    scopus 로고
    • Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: Definition of mutant states for rescue in cancer therapy
    • Bullock, A. N., Henckel, J., and Fersht, A. R. (2000) Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy, Oncogene 19, 1245-1256.
    • (2000) Oncogene , vol.19 , pp. 1245-1256
    • Bullock, A.N.1    Henckel, J.2    Fersht, A.R.3
  • 7
    • 21744437903 scopus 로고    scopus 로고
    • Kinetic partitioning during folding of the p53 DNA binding domain
    • Butler, J. S., and Loh, S. N. (2005) Kinetic partitioning during folding of the p53 DNA binding domain, J. Mol. Biol. 350, 906-918.
    • (2005) J. Mol. Biol , vol.350 , pp. 906-918
    • Butler, J.S.1    Loh, S.N.2
  • 8
  • 9
    • 28944441575 scopus 로고    scopus 로고
    • The major outer membrane protein of Fusobacterium nucleatum (FomA) folds and inserts into lipid bilayers via parallel folding pathways
    • Pocanschi, C. L., Apell, H. J., Puntervoll, P., Hogh, B., Jensen, H. B., Welte, W., and Kleinschmidt, J. H. (2006) The major outer membrane protein of Fusobacterium nucleatum (FomA) folds and inserts into lipid bilayers via parallel folding pathways, J. Mol. Biol. 355, 548-561.
    • (2006) J. Mol. Biol , vol.355 , pp. 548-561
    • Pocanschi, C.L.1    Apell, H.J.2    Puntervoll, P.3    Hogh, B.4    Jensen, H.B.5    Welte, W.6    Kleinschmidt, J.H.7
  • 10
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
    • Wildegger, G., and Kiefhaber, T. (1997) Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate, J. Mol. Biol. 270, 294-304.
    • (1997) J. Mol. Biol , vol.270 , pp. 294-304
    • Wildegger, G.1    Kiefhaber, T.2
  • 12
    • 0035191642 scopus 로고    scopus 로고
    • Engineered metal binding sites map the heterogeneous folding landscape of a coiled coil
    • Krantz, B., and Sosnick, T. R. (2001) Engineered metal binding sites map the heterogeneous folding landscape of a coiled coil, Nat. Struct. Biol. 8, 1042-1047.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 1042-1047
    • Krantz, B.1    Sosnick, T.R.2
  • 13
    • 0037058950 scopus 로고    scopus 로고
    • Sequential vs. parallel protein-folding mechanisms: Experimental tests for complex folding reactions
    • Wallace, L. A., and Matthews, C. R. (2002) Sequential vs. parallel protein-folding mechanisms: experimental tests for complex folding reactions, Biophys. Chem. 101-102, 113-131.
    • (2002) Biophys. Chem , vol.101-102 , pp. 113-131
    • Wallace, L.A.1    Matthews, C.R.2
  • 14
    • 0016711868 scopus 로고
    • Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
    • Brandts, J. F., Halvorson, H. R., and Brennan, M. (1975) Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues, Biochemistry 14, 4953-4963.
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 15
    • 33947209608 scopus 로고
    • Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding
    • Kiefhaber, T., Grunert, H. P., Hahn, U., and Schmid, F. X. (1990) Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding, Biochemistry 35, 1548-1559.
    • (1990) Biochemistry , vol.35 , pp. 1548-1559
    • Kiefhaber, T.1    Grunert, H.P.2    Hahn, U.3    Schmid, F.X.4
  • 16
    • 0027049568 scopus 로고
    • Cis proline mutants of ribonuclease A. 11. Elimination of the slow-folding forms by mutation
    • Schultz, D. A., Schmid, F. X., and Baldwin, R. L. (1992) Cis proline mutants of ribonuclease A. 11. Elimination of the slow-folding forms by mutation, Protein Sci. 1, 917-924.
    • (1992) Protein Sci , vol.1 , pp. 917-924
    • Schultz, D.A.1    Schmid, F.X.2    Baldwin, R.L.3
  • 17
    • 0037126686 scopus 로고    scopus 로고
    • Proline cis-trans isomerization and protein folding
    • Wedermeyer, W. J., Welker, E., and Scheraga, H. A. (2002) Proline cis-trans isomerization and protein folding, Biochemistry 451, 14637-14644.
    • (2002) Biochemistry , vol.451 , pp. 14637-14644
    • Wedermeyer, W.J.1    Welker, E.2    Scheraga, H.A.3
  • 18
    • 0033573854 scopus 로고    scopus 로고
    • Effects of proline mutations on the folding of staphylococcal nuclease
    • Maki, K., Ikura, T., Hayano, T., Takaliashi, N., and Kuwajima, K. (1999) Effects of proline mutations on the folding of staphylococcal nuclease, Biochemistry 38, 2213-2223.
    • (1999) Biochemistry , vol.38 , pp. 2213-2223
    • Maki, K.1    Ikura, T.2    Hayano, T.3    Takaliashi, N.4    Kuwajima, K.5
  • 19
    • 0038690118 scopus 로고    scopus 로고
    • Proline replacements and the simplification of the complex, parallel channel folding mechanism for the alpha subunit fo Tip synthase, a TIM barrel protein
    • Wu, Y., and Matthews, C. R. (2003) Proline replacements and the simplification of the complex, parallel channel folding mechanism for the alpha subunit fo Tip synthase, a TIM barrel protein, J. Mol. Biol. 330, 1131-1144.
    • (2003) J. Mol. Biol , vol.330 , pp. 1131-1144
    • Wu, Y.1    Matthews, C.R.2
  • 20
    • 0037418548 scopus 로고    scopus 로고
    • Structure, function, and aggregation of the zinc-free form of the p53 DNA binding domain
    • Butler, J. S., and Loh, S. N. (2003) Structure, function, and aggregation of the zinc-free form of the p53 DNA binding domain, Biochemistry 42, 2396-2403.
    • (2003) Biochemistry , vol.42 , pp. 2396-2403
    • Butler, J.S.1    Loh, S.N.2
  • 21
    • 33745170683 scopus 로고    scopus 로고
    • 2+ on DNA recognition and stability of the p53 DNA binding domain
    • 2+ on DNA recognition and stability of the p53 DNA binding domain, Biochemistry 45, 7483-7492.
    • (2006) Biochemistry , vol.45 , pp. 7483-7492
    • Duan, J.1    Nilsson, L.2
  • 22
    • 0030816577 scopus 로고    scopus 로고
    • Identification of the predominant non-native histidine ligand in unfolded cytochrome c
    • Colón, W., Wakem, L. P., Sherman, F., and Roder, H. (1997) Identification of the predominant non-native histidine ligand in unfolded cytochrome c, Biochemistry 36, 12535-12541.
    • (1997) Biochemistry , vol.36 , pp. 12535-12541
    • Colón, W.1    Wakem, L.P.2    Sherman, F.3    Roder, H.4
  • 23
    • 0024596024 scopus 로고
    • 2+ binding on the folding kinetics of α-lactalbumin
    • 2+ binding on the folding kinetics of α-lactalbumin, J. Mol. Biol. 206, 547-561.
    • (1989) J. Mol. Biol , vol.206 , pp. 547-561
    • Kuwajima, K.1    Mitani, M.2    Sugai, S.3
  • 24
    • 33645506272 scopus 로고    scopus 로고
    • Cofactor effects on the protein folding reaction: Acceleration of α-lactalbumin refolding by metal ions
    • Bushmarina, N. A., Blanchet, C. E., Vernier, G., and Forge, V. (2006) Cofactor effects on the protein folding reaction: acceleration of α-lactalbumin refolding by metal ions, Protein Sci. 15, 659-671.
    • (2006) Protein Sci , vol.15 , pp. 659-671
    • Bushmarina, N.A.1    Blanchet, C.E.2    Vernier, G.3    Forge, V.4
  • 25
    • 0036228152 scopus 로고    scopus 로고
    • Presence of the cofactor speeds up folding of Desulfovibrio desulfuricans flavodoxin
    • Apiyo, D., and Wittung-Stafshede, P. (2002) Presence of the cofactor speeds up folding of Desulfovibrio desulfuricans flavodoxin, Protein Sci. 11, 1129-1135.
    • (2002) Protein Sci , vol.11 , pp. 1129-1135
    • Apiyo, D.1    Wittung-Stafshede, P.2
  • 26
    • 0025911196 scopus 로고
    • Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra
    • Sugawara, T., Kuwajima, K., and Sugai, S. (1991) Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra, Biochemistry 30, 2698-2706.
    • (1991) Biochemistry , vol.30 , pp. 2698-2706
    • Sugawara, T.1    Kuwajima, K.2    Sugai, S.3
  • 27
    • 0035370848 scopus 로고    scopus 로고
    • Copper stabilizes azurin by decreasing the unfolding rate
    • Pozdnyakova, I., and Wittung-Stafshede, P. (2001) Copper stabilizes azurin by decreasing the unfolding rate, Arch. Biochem. Biophys. 290, 146-148.
    • (2001) Arch. Biochem. Biophys , vol.290 , pp. 146-148
    • Pozdnyakova, I.1    Wittung-Stafshede, P.2
  • 28
    • 0033769529 scopus 로고    scopus 로고
    • Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease H1
    • Goedken, E. R., Keck, J. L., Berger, J. M., and Marqusee, S. (2000) Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease H1, Protein Sci. 9, 1914-1921.
    • (2000) Protein Sci , vol.9 , pp. 1914-1921
    • Goedken, E.R.1    Keck, J.L.2    Berger, J.M.3    Marqusee, S.4
  • 29
    • 0022051541 scopus 로고
    • The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase
    • Hunt, J. B., Neece, S. H., and Ginsburg, A. (1985) The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase, Anal. Biochem. 146, 150-157.
    • (1985) Anal. Biochem , vol.146 , pp. 150-157
    • Hunt, J.B.1    Neece, S.H.2    Ginsburg, A.3
  • 30
    • 0037066755 scopus 로고    scopus 로고
    • Biogenesis of p53 involves cotranslational dimerization of monomers and posttranslational dimerization of dimers. Implications on the dominant negative effect
    • Nicholls, C. D., McLure, K. G., Shields, M. A., and Lee, P. (2002) Biogenesis of p53 involves cotranslational dimerization of monomers and posttranslational dimerization of dimers. Implications on the dominant negative effect, J. Biol. Chem. 277, 12937-12945.
    • (2002) J. Biol. Chem , vol.277 , pp. 12937-12945
    • Nicholls, C.D.1    McLure, K.G.2    Shields, M.A.3    Lee, P.4
  • 32
    • 33751094082 scopus 로고    scopus 로고
    • Folding and misfolding mechanisms of the p53 DNA binding domain at physiological temperature
    • in press
    • Butler, J. S., and Loh, S. N. (2006) Folding and misfolding mechanisms of the p53 DNA binding domain at physiological temperature, Protein Sci. (in press).
    • (2006) Protein Sci
    • Butler, J.S.1    Loh, S.N.2
  • 36
    • 0039136305 scopus 로고    scopus 로고
    • Cadmium induces conformational modifications of wild-type p53 and supresses p53 response to DNA damage in cultured cells
    • Meplan, C., Mann, K., and Hainaut, P. (1999) Cadmium induces conformational modifications of wild-type p53 and supresses p53 response to DNA damage in cultured cells, J. Biol. Chem. 274, 31663-31670.
    • (1999) J. Biol. Chem , vol.274 , pp. 31663-31670
    • Meplan, C.1    Mann, K.2    Hainaut, P.3
  • 37
  • 38
    • 0025785257 scopus 로고
    • Intracellular free zinc and zinc buffering in human red blood cells
    • Simons, T. J. B. (1991) Intracellular free zinc and zinc buffering in human red blood cells, J. Membr. Biol. 123, 63-71.
    • (1991) J. Membr. Biol , vol.123 , pp. 63-71
    • Simons, T.J.B.1
  • 39
    • 0034597536 scopus 로고    scopus 로고
    • Metallogregulation of the tumor supressor protein p53: Zinc mediates the renaturation of p53 after exposure to metal chelators in vitro and in intact cells
    • Meplan, C., Richard, M.-J., and Hainaut, P. (2000) Metallogregulation of the tumor supressor protein p53: zinc mediates the renaturation of p53 after exposure to metal chelators in vitro and in intact cells, Oncogene 19, 5227-5236.
    • (2000) Oncogene , vol.19 , pp. 5227-5236
    • Meplan, C.1    Richard, M.-J.2    Hainaut, P.3
  • 40
    • 0037168653 scopus 로고    scopus 로고
    • Low intracellular zinc induces oxidative DNA damage, disrupts p53, NFkB, and AP1 DNA binding, and affects DNA repair in a rat glioma cell line
    • Ho, E., and Ames, B. N. (2002) Low intracellular zinc induces oxidative DNA damage, disrupts p53, NFkB, and AP1 DNA binding, and affects DNA repair in a rat glioma cell line, Proc. Natl. Acad. Sci. U.S.A. 99, 16770-16775.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 16770-16775
    • Ho, E.1    Ames, B.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.