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Volumn 111, Issue 4, 2002, Pages 471-481

A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; RECEPTOR; THIOL DERIVATIVE; THIOREDOXIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR YAP1; UNCLASSIFIED DRUG; CYSTEINE; DISULFIDE; DNA BINDING PROTEIN; FUNGAL DNA; FUNGAL PROTEIN; GLUTATHIONE; HYBRID PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; YAP1 PROTEIN, S CEREVISIAE;

EID: 0037110454     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(02)01048-6     Document Type: Article
Times cited : (758)

References (32)
  • 1
    • 0035823498 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases
    • Avery A.M., Avery S.V. Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases. J. Biol. Chem. 276:2001;33730-33735.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33730-33735
    • Avery, A.M.1    Avery, S.V.2
  • 2
    • 0028139014 scopus 로고
    • The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase
    • Bjornstedt M., Xue J., Huang W., Akesson B., Holmgren A. The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase. J. Biol. Chem. 269:1994;29382-29384.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29382-29384
    • Bjornstedt, M.1    Xue, J.2    Huang, W.3    Akesson, B.4    Holmgren, A.5
  • 3
    • 0033230807 scopus 로고    scopus 로고
    • Tissue-specific functions of individual glutathione peroxidases
    • Brigelius-Flohe R. Tissue-specific functions of individual glutathione peroxidases. Free Radic. Biol. Med. 27:1999;951-965.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 951-965
    • Brigelius-Flohe, R.1
  • 4
    • 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., Storz G. Role of thioredoxin reductase in the Yap1p-dependent response to oxidative stress in Saccharomyces cerevisiae. Mol. Microbiol. 39:2001;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
  • 5
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae H.Z., Chung S.J., Rhee S.G. Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269:1994;27670-27678.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 6
    • 0033598677 scopus 로고    scopus 로고
    • Protein-sulfenic acids: Diverse roles for an unlikely player in enzyme catalysis and redox regulation
    • Claiborne A., Yeh J.I., Mallett T.C., Luba J., Crane E.J., Charrier V., Parsonage D. Protein-sulfenic acids. diverse roles for an unlikely player in enzyme catalysis and redox regulation Biochemistry. 38:1999;15407-15416.
    • (1999) Biochemistry , vol.38 , pp. 15407-15416
    • Claiborne, A.1    Yeh, J.I.2    Mallett, T.C.3    Luba, J.4    Crane, E.J.5    Charrier, V.6    Parsonage, D.7
  • 8
    • 0034597012 scopus 로고    scopus 로고
    • 2 sensing through oxidation of the Yap1 transcription factor
    • 2 sensing through oxidation of the Yap1 transcription factor. EMBO J. 19:2000;5157-5166.
    • (2000) EMBO J. , vol.19 , pp. 5157-5166
    • Delaunay, A.1    Isnard, A.D.2    Toledano, M.B.3
  • 9
    • 0030822346 scopus 로고    scopus 로고
    • Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium
    • Ellis H.R., Poole L.B. Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium. Biochemistry. 36:1997;13349-13356.
    • (1997) Biochemistry , vol.36 , pp. 13349-13356
    • Ellis, H.R.1    Poole, L.B.2
  • 11
    • 0030667302 scopus 로고    scopus 로고
    • Distribution and possible novel role of phospholipid hydroperoxide glutathione peroxidase in rat epididymal spermatozoa
    • Godeas C., Tramer F., Micali F., Soranzo M., Sandri G., Panfili E. Distribution and possible novel role of phospholipid hydroperoxide glutathione peroxidase in rat epididymal spermatozoa. Biol. Reprod. 57:1997;1502-1508.
    • (1997) Biol. Reprod. , vol.57 , pp. 1502-1508
    • Godeas, C.1    Tramer, F.2    Micali, F.3    Soranzo, M.4    Sandri, G.5    Panfili, E.6
  • 12
    • 0034082979 scopus 로고    scopus 로고
    • Genetic responses to free radicals. Homeostasis and gene control
    • Gonzalez-Flecha B., Demple B. Genetic responses to free radicals. Homeostasis and gene control. Ann. N Y Acad. Sci. 899:2000;69-87.
    • (2000) Ann. N Y Acad. Sci. , vol.899 , pp. 69-87
    • Gonzalez-Flecha, B.1    Demple, B.2
  • 13
    • 0033578750 scopus 로고    scopus 로고
    • Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae
    • Inoue Y., Matsuda T., Sugiyama S., Izawa S., Kimura A. Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae. J. Biol. Chem. 274:1999;27002-27009.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27002-27009
    • Inoue, Y.1    Matsuda, T.2    Sugiyama, S.3    Izawa, S.4    Kimura, A.5
  • 14
    • 0033214613 scopus 로고    scopus 로고
    • Thioredoxin deficiency causes the constitutive activation of Yap1, an AP-1-like transcription factor in Saccharomyces cerevisiae
    • Izawa S., Maeda K., Sugiyama K., Mano J., Inoue Y., Kimura A. Thioredoxin deficiency causes the constitutive activation of Yap1, an AP-1-like transcription factor in Saccharomyces cerevisiae. J. Biol. Chem. 274:1999;28459-28465.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28459-28465
    • Izawa, S.1    Maeda, K.2    Sugiyama, K.3    Mano, J.4    Inoue, Y.5    Kimura, A.6
  • 16
    • 0028057226 scopus 로고
    • YAP1 dependent activation fo TRX2 is essential for the response of Saccharomyces cerevisiae to oxidative stress by hydroperoxides
    • Kuge S., Jones N. YAP1 dependent activation fo TRX2 is essential for the response of Saccharomyces cerevisiae to oxidative stress by hydroperoxides. EMBO J. 13:1994;655-664.
    • (1994) EMBO J. , vol.13 , pp. 655-664
    • Kuge, S.1    Jones, N.2
  • 17
    • 0030942294 scopus 로고    scopus 로고
    • Regulation of yAP-1 nuclear localization in response to oxidative stress
    • Kuge S., Jones N., Nomoto A. Regulation of yAP-1 nuclear localization in response to oxidative stress. EMBO J. 16:1997;1710-1720.
    • (1997) EMBO J. , vol.16 , pp. 1710-1720
    • Kuge, S.1    Jones, N.2    Nomoto, A.3
  • 18
    • 0031595764 scopus 로고    scopus 로고
    • Crm1 (Xpo1) dependent nuclear export of the budding yeast transcription factor yAP-1 is sensitive to oxidative stress
    • Kuge S., Toda T., Lizuka N., Nomoto A. Crm1 (Xpo1) dependent nuclear export of the budding yeast transcription factor yAP-1 is sensitive to oxidative stress. Genes Cells. 3:1998;521-532.
    • (1998) Genes Cells , vol.3 , pp. 521-532
    • Kuge, S.1    Toda, T.2    Lizuka, N.3    Nomoto, A.4
  • 19
    • 0035726624 scopus 로고    scopus 로고
    • Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation
    • Kuge S., Arita M., Murayama A., Maeta K., Izawa S., Inoue Y., Nomoto A. Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation. Mol. Cell. Biol. 21:2001;6139-6150.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6139-6150
    • Kuge, S.1    Arita, M.2    Murayama, A.3    Maeta, K.4    Izawa, S.5    Inoue, Y.6    Nomoto, A.7
  • 22
    • 0035283587 scopus 로고    scopus 로고
    • Redox-operated genetic switches: The SoxR and OxyR transcription factors
    • Pomposiello P.J., Demple B. Redox-operated genetic switches. the SoxR and OxyR transcription factors Trends Biotechnol. 19:2001;109-114.
    • (2001) Trends Biotechnol. , vol.19 , pp. 109-114
    • Pomposiello, P.J.1    Demple, B.2
  • 23
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68:1996;850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 24
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski R.S., Hieter P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:1989;19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 25
    • 0035831449 scopus 로고    scopus 로고
    • A genetic investigation of the essential role of glutathione: Mutations in the proline biosynthesis pathway are the only suppressors of glutathione auxotrophy in yeast
    • Spector D., Labarre J., Toledano M.B. A genetic investigation of the essential role of glutathione. mutations in the proline biosynthesis pathway are the only suppressors of glutathione auxotrophy in yeast J. Biol. Chem. 276:2000;7011-7016.
    • (2000) J. Biol. Chem. , vol.276 , pp. 7011-7016
    • Spector, D.1    Labarre, J.2    Toledano, M.B.3
  • 28
    • 0031225515 scopus 로고    scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase (PHGPx): More than an antioxidant enzyme?
    • Ursini F., Maiorino M., Roveri A. Phospholipid hydroperoxide glutathione peroxidase (PHGPx). more than an antioxidant enzyme? Biomed. Environ. Sci. 10:1997;327-332.
    • (1997) Biomed. Environ. Sci. , vol.10 , pp. 327-332
    • Ursini, F.1    Maiorino, M.2    Roveri, A.3
  • 31
    • 0032535486 scopus 로고    scopus 로고
    • Crm1p mediates regulated nuclear export of a yeast AP-1-like transcription factor
    • Yan C., Lee L.H., Davis L.I. Crm1p mediates regulated nuclear export of a yeast AP-1-like transcription factor. EMBO J. 17:1998;7416-7429.
    • (1998) EMBO J. , vol.17 , pp. 7416-7429
    • Yan, C.1    Lee, L.H.2    Davis, L.I.3
  • 32
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng M., Aslund F., Storz G. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science. 279:1998;1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.