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Volumn 23, Issue 10, 2002, Pages 1609-1615

Reporter gene transactivation by human p53 is inhibited in thioredoxin reductase null yeast by a mechanism associated with thioredoxin oxidation and independent of changes in the redox state of glutathione

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; GLUTATHIONE; PROTEIN P53; THIOREDOXIN; THIOREDOXIN REDUCTASE;

EID: 0036797413     PISSN: 01433334     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (29)

References (46)
  • 1
    • 0030883143 scopus 로고    scopus 로고
    • SSU1 encodes a plasma membrane protein with a central role in a network of proteins conferring sulfite tolerance in Saccharomyces cerevisiae
    • Avram, D. and Bakalinsky, A.T. (1997) SSU1 encodes a plasma membrane protein with a central role in a network of proteins conferring sulfite tolerance in Saccharomyces cerevisiae. J. Bacteriol., 179, 5971-5974.
    • (1997) J. Bacteriol , vol.179 , pp. 5971-5974
    • Avram, D.1    Bakalinsky, A.T.2
  • 2
    • 0030813617 scopus 로고    scopus 로고
    • Cellular thioredoxin reductase activity is regulated by selenium
    • Berggren, M., Gallegos, A., Gasdaska, J. and Powis, G. (1997) Cellular thioredoxin reductase activity is regulated by selenium. Anticancer Res., 17, 3377-3380.
    • (1997) Anticancer Res , vol.17 , pp. 3377-3380
    • Berggren, M.1    Gallegos, A.2    Gasdaska, J.3    Powis, G.4
  • 3
    • 0036125718 scopus 로고    scopus 로고
    • Protein electrophoretic mobility shift assay to monitor redox state of thioredoxin in cells
    • Bersani, N.A., Merwin, J.R., Lopez, N.I., Pearson, G.D. and Merrill, G.F. (2002) Protein electrophoretic mobility shift assay to monitor redox state of thioredoxin in cells. Meth. Enzymol., 347, 317-326.
    • (2002) Meth. Enzymol , vol.347 , pp. 317-326
    • Bersani, N.A.1    Merwin, J.R.2    Lopez, N.I.3    Pearson, G.D.4    Merrill, G.F.5
  • 4
    • 0030978102 scopus 로고    scopus 로고
    • Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene (Trsp)
    • Bösl, M.R., Takaku, K., Oshima, M., Nishimura, S. and Taketo, M.M. (1997) Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene (Trsp). Proc. Natl Acad. Sci. USA, 94, 5531-5534.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5531-5534
    • Bösl, M.R.1    Takaku, K.2    Oshima, M.3    Nishimura, S.4    Taketo, M.M.5
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 6
    • 0035138443 scopus 로고    scopus 로고
    • Role of thioredoxin reductase in the Yap1p-dependent response to oxidative stress in Saccharomyces cerevisiae
    • Carmel-Harel, O., Stearman, R., Gasch, A.P., Botstein, D., Brown, P.O. and Storz, G. (2001) Role of thioredoxin reductase in the Yap1p-dependent response to oxidative stress in Saccharomyces cerevisiae. Mol. Microbiol., 39, 595-605.
    • (2001) Mol. Microbiol , vol.39 , pp. 595-605
    • Carmel-Harel, O.1    Stearman, R.2    Gasch, A.P.3    Botstein, D.4    Brown, P.O.5    Storz, G.6
  • 7
    • 0029994196 scopus 로고    scopus 로고
    • A mutation in a thioredoxin reductase homolog suppresses p53-induced growth inhibition in the fission yeast Schizosaccharomyces pombe
    • Casso, D. and Beach, D. (1996) A mutation in a thioredoxin reductase homolog suppresses p53-induced growth inhibition in the fission yeast Schizosaccharomyces pombe. Mol. Gen. Genet., 252, 518-529.
    • (1996) Mol. Gen. Genet , vol.252 , pp. 518-529
    • Casso, D.1    Beach, D.2
  • 8
    • 0028072911 scopus 로고
    • Thioredoxin dependent peroxide reductase from yeast
    • Chae, H.Z., Chung, S.J. and Rhee, S.G. (1994) Thioredoxin dependent peroxide reductase from yeast. J. Biol. Chem., 269, 27670-27678.
    • (1994) J. Biol. Chem , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 9
    • 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
  • 10
    • 0031819215 scopus 로고    scopus 로고
    • Decreased incidence of prostate cancer with selenium supplementation: Results of a double-blind cancer prevention trial
    • Clark, L.C., Dalkin, B.A. Krongrad, G.F., et al. 1998. Decreased incidence of prostate cancer with selenium supplementation: results of a double-blind cancer prevention trial. Br. J. Urol., 81, 730-734.
    • (1998) Br. J. Urol , vol.81 , pp. 730-734
    • Clark, L.C.1    Dalkin, B.A.2    Krongrad, G.F.3
  • 11
    • 0028016446 scopus 로고
    • Characterization of baculovirus recombinant wild-type p53. Dimerization of p53 is required for high-affinity DNA binding and cysteine oxidation inhibits p53 DNA binding
    • Delphin, C., Cahen, P., Lawrence, J.J. and Baudier, J. (1994) Characterization of baculovirus recombinant wild-type p53. Dimerization of p53 is required for high-affinity DNA binding and cysteine oxidation inhibits p53 DNA binding. Eur. J. Biochem., 223, 683-692.
    • (1994) Eur. J. Biochem , vol.223 , pp. 683-692
    • Delphin, C.1    Cahen, P.2    Lawrence, J.J.3    Baudier, J.4
  • 12
    • 0023079953 scopus 로고
    • High-performance liquid chromatography of thiols and disulfides: Dinitrophenol derivatives
    • Fariss, M.W. and Reed, D.J. (1987) High-performance liquid chromatography of thiols and disulfides: dinitrophenol derivatives. Meth. Enzymol., 143, 101-109.
    • (1987) Meth. Enzymol , vol.143 , pp. 101-109
    • Fariss, M.W.1    Reed, D.J.2
  • 13
    • 0024266139 scopus 로고
    • New yeast-Escherischia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Geitz, R.D. and Sugino, A. (1988) New yeast-Escherischia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene, 74, 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Geitz, R.D.1    Sugino, A.2
  • 14
    • 0032935722 scopus 로고    scopus 로고
    • Selenocysteine-containing proteins in mammals
    • Gladyshev, V.N. and Hatfield, D.L. (1999) Selenocysteine-containing proteins in mammals. J. Biomed. Sci., 6, 151-160.
    • (1999) J. Biomed. Sci , vol.6 , pp. 151-160
    • Gladyshev, V.N.1    Hatfield, D.L.2
  • 15
    • 0029973142 scopus 로고    scopus 로고
    • Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene
    • Gladyshev, V.N., Jeang, K.T. and Stadtman, T.C. (1996) Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. Proc. Natl Acad. Sci. USA, 93, 6146-6151.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6146-6151
    • Gladyshev, V.N.1    Jeang, K.T.2    Stadtman, T.C.3
  • 16
    • 0030025773 scopus 로고    scopus 로고
    • Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours
    • Graeber, T.G., Osmanian, C., Jacks, T., Housman, D.E., Koch, C.J., Lowe, S.W. and Giaccia, A.J. (1996) Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours. Nature, 379, 88-91.
    • (1996) Nature , vol.379 , pp. 88-91
    • Graeber, T.G.1    Osmanian, C.2    Jacks, T.3    Housman, D.E.4    Koch, C.J.5    Lowe, S.W.6    Giaccia, A.J.7
  • 17
    • 0030016469 scopus 로고    scopus 로고
    • Yeast glutathione reductase is required for protection against oxidative stress and is a target for yAP-1 transcriptional regulation
    • Grant, C.M., Collinson, L.P., Roe, J.-H. and Dawes, I.W. (1996) Yeast glutathione reductase is required for protection against oxidative stress and is a target for yAP-1 transcriptional regulation. Mol. Microbiol., 21, 171-179.
    • (1996) Mol. Microbiol , vol.21 , pp. 171-179
    • Grant, C.M.1    Collinson, L.P.2    Roe, J.-H.3    Dawes, I.W.4
  • 18
    • 0030996361 scopus 로고    scopus 로고
    • Synergistic activation of transcription by CBP and p53
    • Gu, W., Shi, X.L. and Roeder, R.G. (1997) Synergistic activation of transcription by CBP and p53. Nature, 387, 819-823.
    • (1997) Nature , vol.387 , pp. 819-823
    • Gu, W.1    Shi, X.L.2    Roeder, R.G.3
  • 19
    • 0034859507 scopus 로고    scopus 로고
    • Zinc binding and redox control of p53 structure and function
    • Hainaut, P. and Mann, K. (2001) Zinc binding and redox control of p53 structure and function. Antiox. Redox Signal., 3, 611-623.
    • (2001) Antiox. Redox Signal , vol.3 , pp. 611-623
    • Hainaut, P.1    Mann, K.2
  • 20
    • 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
  • 21
    • 0017653811 scopus 로고
    • Bovine thioredoxin system. Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction
    • Holmgren, A. (1977) Bovine thioredoxin system. Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction. J. Biol. Chem., 252, 4600-4606.
    • (1977) J. Biol. Chem , vol.252 , pp. 4600-4606
    • Holmgren, A.1
  • 22
    • 0030900605 scopus 로고    scopus 로고
    • Identification of redox/repair protein Ref-1 as a potent activator of p53
    • Jayaraman, L., Murthy, K.G., Zhu, C., Curran, T., Xanthoudakis, S. and Prives, C. (1997) Identification of redox/repair protein Ref-1 as a potent activator of p53. Genes Der., 11, 558-570.
    • (1997) Genes Der , vol.11 , pp. 558-570
    • Jayaraman, L.1    Murthy, K.G.2    Zhu, C.3    Curran, T.4    Xanthoudakis, S.5    Prives, C.6
  • 23
    • 0029053005 scopus 로고
    • A rapid permeabilization procedure for accurate quantitative determination of beta-galactosidase activity in yeast cells
    • Kippert, F. (1995) A rapid permeabilization procedure for accurate quantitative determination of beta-galactosidase activity in yeast cells. FEMS Microbiol. Lett., 128, 201-206.
    • (1995) FEMS Microbiol. Lett , vol.128 , pp. 201-206
    • Kippert, F.1
  • 24
    • 0035140981 scopus 로고    scopus 로고
    • Regulation of p53 by hypoxia: Dissociation of transcriptional repression and apoptosis from p53-dependent transactivation
    • Koumenis, C., Alarcon, R.E., Hammond, P., et al. (2001) Regulation of p53 by hypoxia: dissociation of transcriptional repression and apoptosis from p53-dependent transactivation. Mol. Cell. Biol., 21, 1297-1310.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 1297-1310
    • Koumenis, C.1    Alarcon, R.E.2    Hammond, P.3
  • 26
    • 0030841865 scopus 로고    scopus 로고
    • Thioredoxin reductase-dependent inhibition of MCB cell cycle box activity in Saccharomyces cerevisiae
    • Machado, A.K., Morgan, B.A. and Merrill, G.M. (1997) Thioredoxin reductase-dependent inhibition of MCB cell cycle box activity in Saccharomyces cerevisiae. J. Biol. Chem., 272, 17045-17054.
    • (1997) J. Biol. Chem , vol.272 , pp. 17045-17054
    • Machado, A.K.1    Morgan, B.A.2    Merrill, G.M.3
  • 27
    • 2042470971 scopus 로고    scopus 로고
    • Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene
    • Matsui, M., Oshima, M., Oshima, H., Takaku, K., Maruyama, T., Yodoi, J. and Taketo, M.M. (1996) Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene. Dev. Biol., 178, 179-185.
    • (1996) Dev. Biol , vol.178 , pp. 179-185
    • Matsui, M.1    Oshima, M.2    Oshima, H.3    Takaku, K.4    Maruyama, T.5    Yodoi, J.6    Taketo, M.M.7
  • 28
    • 0026715172 scopus 로고
    • Thioredoxin regulates the DNA binding activity of NF-kB by reduction of a disulfide bond involving cysteine 62
    • Matthews, J.R., Wakasugi, N., Virelizier J.-L.V., Yodoi, J. and Hay, R.T. (1992) Thioredoxin regulates the DNA binding activity of NF-kB by reduction of a disulfide bond involving cysteine 62. Nucleic Acids Res., 20, 3821-3830.
    • (1992) Nucleic Acids Res , vol.20 , pp. 3821-3830
    • Matthews, J.R.1    Wakasugi, N.2    Virelizier, J.-L.V.3    Yodoi, J.4    Hay, R.T.5
  • 29
    • 0033168514 scopus 로고    scopus 로고
    • The human p53 negative regulatory domain mediates inhibition of reporter gene transactivation in yeast lacking thioredoxin reductase
    • Merrill, G.M., Dowell, P. and Pearson, G.D. (1999) The human p53 negative regulatory domain mediates inhibition of reporter gene transactivation in yeast lacking thioredoxin reductase. Cancer Res., 59, 3175-3179.
    • (1999) Cancer Res , vol.59 , pp. 3175-3179
    • Merrill, G.M.1    Dowell, P.2    Pearson, G.D.3
  • 30
    • 0029948308 scopus 로고    scopus 로고
    • A glutathione reductase mutant of yeast accumulates high levels of oxidized glutathione and requires thioredoxin for growth
    • Muller, E.G.D. (1996) A glutathione reductase mutant of yeast accumulates high levels of oxidized glutathione and requires thioredoxin for growth. Mol. Biol. Cell, 7, 1805-1813.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1805-1813
    • Muller, E.G.D.1
  • 31
    • 0028987974 scopus 로고
    • A redox-dependent function of thioredoxin is necessary to sustain a rapid rate of DNA synthesis in yeast
    • Muller, E.G.D. (1994) A redox-dependent function of thioredoxin is necessary to sustain a rapid rate of DNA synthesis in yeast. Arch. Biochem. Biophys., 318, 356-361.
    • (1994) Arch. Biochem. Biophys , vol.318 , pp. 356-361
    • Muller, E.G.D.1
  • 32
    • 0028953840 scopus 로고
    • Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
    • Mumberg, D., Muller, R. and Funk, M. (1995) Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene, 156, 119-122.
    • (1995) Gene , vol.156 , pp. 119-122
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 33
    • 0034652113 scopus 로고    scopus 로고
    • Thioredoxin reductase
    • Mustacich, D. and Powis, G. (2000) Thioredoxin reductase. Biochem. J., 346, 1-8.
    • (2000) Biochem. J , vol.346 , pp. 1-8
    • Mustacich, D.1    Powis, G.2
  • 34
    • 0032489461 scopus 로고    scopus 로고
    • Deletion of the Saccharomyces cerevisiae TRR1 gene encoding thioredoxin reductase inhibits p53-dependent reporter gene expression
    • Pearson, G.D. and Merrill, G.F. (1998) Deletion of the Saccharomyces cerevisiae TRR1 gene encoding thioredoxin reductase inhibits p53-dependent reporter gene expression. J. Biol. Chem., 273, 5431-5434.
    • (1998) J. Biol. Chem , vol.273 , pp. 5431-5434
    • Pearson, G.D.1    Merrill, G.F.2
  • 35
    • 0035029131 scopus 로고    scopus 로고
    • Properties and biological activities of thioredoxins
    • Powis, G. and Montfort, W.R. (2001) Properties and biological activities of thioredoxins. Ann. Rev Pharmacol Toxicol., 41, 261-295.
    • (2001) Ann. Rev Pharmacol Toxicol , vol.41 , pp. 261-295
    • Powis, G.1    Montfort, W.R.2
  • 36
    • 0029644240 scopus 로고
    • Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B
    • Qin, J., Clore, G.M., Kennedy, W.M., Huth, J.R. and Gronenborn, A.M. (1995) Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B. Structure, 3, 289-297.
    • (1995) Structure , vol.3 , pp. 289-297
    • Qin, J.1    Clore, G.M.2    Kennedy, W.M.3    Huth, J.R.4    Gronenborn, A.M.5
  • 39
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.1    Hieter, P.2
  • 40
    • 0025122797 scopus 로고
    • Determination of sulfhydryl groups and disulfide bonds in a protein by polyacrylamide gel electrophoresis
    • Takahashi, N. and Hirose, M. (1990) Determination of sulfhydryl groups and disulfide bonds in a protein by polyacrylamide gel electrophoresis. Anal. Biochem., 188, 359-365.
    • (1990) Anal. Biochem , vol.188 , pp. 359-365
    • Takahashi, N.1    Hirose, M.2
  • 42
    • 0033544915 scopus 로고    scopus 로고
    • Thioredoxin-dependent redox regulation of p53-mediated p21 activation
    • Ueno, M., Masutani, R.J., Arai, A., et al. (1999) Thioredoxin-dependent redox regulation of p53-mediated p21 activation. J. Biol. Chem., 274, 35809-35815.
    • (1999) J. Biol. Chem , vol.274 , pp. 35809-35815
    • Ueno, M.1    Masutani, R.J.2    Arai, A.3
  • 43
    • 0030764172 scopus 로고    scopus 로고
    • Regulation of p53 by metal ions and by antioxidants: Dithiocarbamate down-regulates p53 DNA-binding activity by increasing the intracellular level of copper
    • Verhaegh, G.W., Richard, M.J. and Hainaut, P. (1997) Regulation of p53 by metal ions and by antioxidants: dithiocarbamate down-regulates p53 DNA-binding activity by increasing the intracellular level of copper. Mol. Cell. Biol., 17, 5699-706.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 5699-5706
    • Verhaegh, G.W.1    Richard, M.J.2    Hainaut, P.3
  • 44
    • 0024324482 scopus 로고
    • A hyper-recombination mutation in S. cerevisiae identifies a novel eucaryotic topoisomerase
    • Wallis, J.W., Chrebet, G., Brodsky, G., Rolfe, M. and Rothstein, R. (1989) A hyper-recombination mutation in S. cerevisiae identifies a novel eucaryotic topoisomerase. Cell, 58, 409-419.
    • (1989) Cell , vol.58 , pp. 409-419
    • Wallis, J.W.1    Chrebet, G.2    Brodsky, G.3    Rolfe, M.4    Rothstein, R.5
  • 45
    • 0032563191 scopus 로고    scopus 로고
    • Pyrrolidine dithiocarbamate prevents p53 activation and promotes p53 cysteine residue oxidation
    • Wu, H.H. and Momand, J. (1998) Pyrrolidine dithiocarbamate prevents p53 activation and promotes p53 cysteine residue oxidation. J. Biol. Chem., 273, 18898-18905.
    • (1998) J. Biol. Chem , vol.273 , pp. 18898-18905
    • Wu, H.H.1    Momand, J.2
  • 46
    • 0028212746 scopus 로고
    • Isolation and characterization of sulfite mutants of Saccharomyces cerevisiae
    • Xu, X., Wightman, J.D., Geller, B.L., Avram, D. and Bakalinsky, A.T. (1994) Isolation and characterization of sulfite mutants of Saccharomyces cerevisiae. Curr. Genet., 25, 488-496.
    • (1994) Curr. Genet , vol.25 , pp. 488-496
    • Xu, X.1    Wightman, J.D.2    Geller, B.L.3    Avram, D.4    Bakalinsky, A.T.5


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