메뉴 건너뛰기




Volumn 234, Issue 2, 2004, Pages 379-385

Stress-dependent regulation of the gene encoding thioredoxin reductase from the fission yeast

Author keywords

Fission yeast; Genomic DNA; Oxidative stress; Pap1; Regulation; Schizosaccharomyces pombe; Thioredoxin reductase

Indexed keywords

ALUMINUM CHLORIDE; BETA GALACTOSIDASE; FUNGAL DNA; FUNGAL ENZYME; HYDROGEN PEROXIDE; MENADIONE; MERCURIC CHLORIDE; MESSENGER RNA; SODIUM SELENITE; THIOREDOXIN REDUCTASE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR PAP1; UNCLASSIFIED DRUG;

EID: 2342651894     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsle.2004.04.007     Document Type: Article
Times cited : (12)

References (27)
  • 3
    • 0029187491 scopus 로고
    • Thioredoxin and thioredoxin reductase
    • Holmgren A., Bjornstedt M. Thioredoxin and thioredoxin reductase. Methods Enzymol. 2528:1995;199-208
    • (1995) Methods Enzymol. , vol.2528 , pp. 199-208
    • Holmgren, A.1    Bjornstedt, M.2
  • 4
    • 0030570764 scopus 로고    scopus 로고
    • Efficient reduction of lipoamide and lipoic acid by mammalian thioredoxin reductase
    • Arnér E.S., Nordberg J.J., Holmgren A. Efficient reduction of lipoamide and lipoic acid by mammalian thioredoxin reductase. Biochem. Biophys. Res. Commun. 225:1996;268-274
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 268-274
    • Arnér, E.S.1    Nordberg, J.J.2    Holmgren, A.3
  • 5
    • 0033775650 scopus 로고    scopus 로고
    • Thioredoxin reductase as a pathophysiological factor and drug target
    • Becker K.S., Gromer S., Schirmer R.H., Müller S. Thioredoxin reductase as a pathophysiological factor and drug target. Eur. J. Biochem. 267:2000;6118-6125
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6118-6125
    • Becker, K.S.1    Gromer, S.2    Schirmer, R.H.3    Müller, S.4
  • 6
    • 0028037601 scopus 로고
    • Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidative damaged proteins
    • Yoshitake S., Nanri H., Fernando M.R., Minakami S. Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidative damaged proteins. Biochem. J. 116:1994;42-46
    • (1994) Biochem. J. , vol.116 , pp. 42-46
    • Yoshitake, S.1    Nanri, H.2    Fernando, M.R.3    Minakami, S.4
  • 7
    • 0030610239 scopus 로고    scopus 로고
    • Heparin-binding properties of selenium-containing thioredoxin reductase from HeLa cells and human lung adenocarcinoma cells
    • Liu S.Y., Stadtman T.C. Heparin-binding properties of selenium-containing thioredoxin reductase from HeLa cells and human lung adenocarcinoma cells. Proc. Natl. Acad. Sci. USA. 94:1997;6138-6141
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6138-6141
    • Liu, S.Y.1    Stadtman, T.C.2
  • 9
    • 0032908575 scopus 로고    scopus 로고
    • Localization of thioredoxin reductase and thioredoxin in normal human placenta and their protective effect against oxidative stress
    • Ejima K., Nanri H., Toki N., Kashimura M., Ikeda M. Localization of thioredoxin reductase and thioredoxin in normal human placenta and their protective effect against oxidative stress. Placenta. 20:1999;95-101
    • (1999) Placenta , vol.20 , pp. 95-101
    • Ejima, K.1    Nanri, H.2    Toki, N.3    Kashimura, M.4    Ikeda, M.5
  • 12
    • 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
  • 13
    • 0034036431 scopus 로고    scopus 로고
    • Multistep phosphorelay proteins transmit oxidative stress signals to the fission yeast stress-activated protein kinase
    • Nguyen A.N., Lee A., Place W., Shiozaki K. Multistep phosphorelay proteins transmit oxidative stress signals to the fission yeast stress-activated protein kinase. Mol. Biol. Cell. 11:2000;1169-1181
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1169-1181
    • Nguyen, A.N.1    Lee, A.2    Place, W.3    Shiozaki, K.4
  • 14
    • 0032523783 scopus 로고    scopus 로고
    • Regulation of the fission yeast transcription factor Pap1 by oxidative stress: Requirement for the nuclear export factor Crm1 (exportin) and the stress-activated MAP kinase Sty1/Spc1
    • Toone W.M., Kuge S., Samuels M., Morgan B.A., Toda T., Jones N. Regulation of the fission yeast transcription factor Pap1 by oxidative stress: requirement for the nuclear export factor Crm1 (exportin) and the stress-activated MAP kinase Sty1/Spc1. Genes Dev. 12:1998;23042-23049
    • (1998) Genes Dev. , vol.12 , pp. 23042-23049
    • Toone, W.M.1    Kuge, S.2    Samuels, M.3    Morgan, B.A.4    Toda, T.5    Jones, N.6
  • 15
    • 0033785699 scopus 로고    scopus 로고
    • Structural basis for the diversity of DNA recognition by bZIP transcription factors
    • Fujii Y., Shimizu T., Toda T., Yanagida M., Hakoshima T. Structural basis for the diversity of DNA recognition by bZIP transcription factors. Nat. Struct. Biol. 7:2000;889-893
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 889-893
    • Fujii, Y.1    Shimizu, T.2    Toda, T.3    Yanagida, M.4    Hakoshima, T.5
  • 16
    • 0033591412 scopus 로고    scopus 로고
    • A novel nuclear export signal sensitive to oxidative stress in the fission yeast transcription factor Pap1
    • Kudo N., Taoka H., Toda T., Yoshida M., Horinouchi S. A novel nuclear export signal sensitive to oxidative stress in the fission yeast transcription factor Pap1. J. Biol. Chem. 274:1999;15151-15158
    • (1999) J. Biol. Chem. , vol.274 , pp. 15151-15158
    • Kudo, N.1    Taoka, H.2    Toda, T.3    Yoshida, M.4    Horinouchi, S.5
  • 17
    • 0030946973 scopus 로고    scopus 로고
    • Discrete roles of the Spc1 kinase and the Atf1 transcription factor in the UV response of Schizosaccharomyces pombe
    • Degols G., Russell P. Discrete roles of the Spc1 kinase and the Atf1 transcription factor in the UV response of Schizosaccharomyces pombe. Mol. Cell. Biol. 17:1997;3356-3363
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3356-3363
    • Degols, G.1    Russell, P.2
  • 18
    • 0034097579 scopus 로고    scopus 로고
    • Role of Atf1 and Pap1 in the induction of the catalase gene of fission yeast Schizosaccharomyces pombe
    • Nakagawa C.W, Yamada K., Mutoh N. Role of Atf1 and Pap1 in the induction of the catalase gene of fission yeast Schizosaccharomyces pombe. J. Biochem. 127:2000;233-238
    • (2000) J. Biochem. , vol.127 , pp. 233-238
    • Nakagawa, C.W.1    Yamada, K.2    Mutoh, N.3
  • 19
    • 0023481280 scopus 로고
    • A simple and efficient liposome method for transfection of DNA into mammalian cells grown in suspension
    • Hoffman C.S., Winston F. A simple and efficient liposome method for transfection of DNA into mammalian cells grown in suspension. Gene. 57:1987;267-272
    • (1987) Gene , vol.57 , pp. 267-272
    • Hoffman, C.S.1    Winston, F.2
  • 20
    • 0345462030 scopus 로고
    • Molecular Cloning: A Laboratory Manual
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: A Laboratory Manual. second ed. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1989) Second Ed.
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 21
    • 0023034916 scopus 로고
    • Yeast shuttle and integrative vectors with multiple cloning sites suitable for construction of lacZ fusions
    • Myers A.M., Tzagoloff A., Kinney D.M., Lusty C.J. Yeast shuttle and integrative vectors with multiple cloning sites suitable for construction of lacZ fusions. Gene. 45:1986;299-310
    • (1986) Gene , vol.45 , pp. 299-310
    • Myers, A.M.1    Tzagoloff, A.2    Kinney, D.M.3    Lusty, C.J.4
  • 22
    • 0020645052 scopus 로고
    • Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast
    • Guarante L. Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast. Methods Enzymol. 101:1983;181-191
    • (1983) Methods Enzymol. , vol.101 , pp. 181-191
    • Guarante, L.1
  • 23
    • 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.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0033525509 scopus 로고    scopus 로고
    • Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae
    • Pedrajas J.R., Kosmidou E., Miranda-Vizuete A., Gustafsson J., Wright A.P.H., Spyrou G. Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae. J. Biol. Chem. 274:1999;6366-6373
    • (1999) J. Biol. Chem. , vol.274 , pp. 6366-6373
    • Pedrajas, J.R.1    Kosmidou, E.2    Miranda-Vizuete, A.3    Gustafsson, J.4    Wright, A.P.H.5    Spyrou, G.6
  • 25
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arnér E.S.T., Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267:2000;6102-6109
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6102-6109
    • Arnér, E.S.T.1    Holmgren, A.2
  • 26
    • 0034674566 scopus 로고    scopus 로고
    • Essential role of selenium in the catalytic activities of mammalin thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteins mutations
    • Zhong L., Holmgren A. Essential role of selenium in the catalytic activities of mammalin thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteins mutations. J. Biol. Chem. 276:2000;18121-18128
    • (2000) J. Biol. Chem. , vol.276 , pp. 18121-18128
    • Zhong, L.1    Holmgren, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.