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Volumn 24, Issue 6, 2007, Pages 481-490

The txl1+ gene from Schizosaccharomyces pombe encodes a new thioredoxin-like I protein that participates in the antioxidant defence against tert-butyl hydroperoxide

Author keywords

Antioxidant; Schizosaccharomyces pombe; Tert butyl hydroperoxide; Thioredoxin like

Indexed keywords

GLUCOSE; HYDROGEN PEROXIDE; MESSENGER RNA; SCHIZOSACCHAROMYCES POMBE PROTEIN; TERT BUTYL HYDROPEROXIDE; THIOREDOXIN LIKE 1 PROTEIN; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

EID: 34347385044     PISSN: 0749503X     EISSN: 10970061     Source Type: Journal    
DOI: 10.1002/yea.1483     Document Type: Article
Times cited : (13)

References (40)
  • 1
    • 0031818471 scopus 로고    scopus 로고
    • Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe
    • Bahler J, Wu JQ, Longtine MS, et al. 1998. Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe. Yeast 14: 943-951.
    • (1998) Yeast , vol.14 , pp. 943-951
    • Bahler, J.1    Wu, J.Q.2    Longtine, M.S.3
  • 3
    • 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, 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
  • 4
    • 12244267727 scopus 로고    scopus 로고
    • Global transcriptional responses of fission yeast to environmental stress
    • Chen D, Toone WM, Mata J, et al. 2003. Global transcriptional responses of fission yeast to environmental stress. Mol Biol Cell 14: 214-229.
    • (2003) Mol Biol Cell , vol.14 , pp. 214-229
    • Chen, D.1    Toone, W.M.2    Mata, J.3
  • 5
    • 0035911713 scopus 로고    scopus 로고
    • Characterization and regulation of Schizosaccharomyces pombe gene encoding thioredoxin
    • Cho Y, Shin YH, Kim Y, et al. 2001. Characterization and regulation of Schizosaccharomyces pombe gene encoding thioredoxin. Biochim Biophys Acta 1518: 194-199.
    • (2001) Biochim Biophys Acta , vol.1518 , pp. 194-199
    • Cho, Y.1    Shin, Y.H.2    Kim, Y.3
  • 6
    • 3843120910 scopus 로고    scopus 로고
    • Differential expression and role of two dithiol glutaredoxins Grx1 and Grx2 in Schizosaccharomyces pombe
    • Chung WH, Kim KD, Cho YJ, Roe JH. 2004. Differential expression and role of two dithiol glutaredoxins Grx1 and Grx2 in Schizosaccharomyces pombe. Biochem Biophys Res Commun 321: 922-929.
    • (2004) Biochem Biophys Res Commun , vol.321 , pp. 922-929
    • Chung, W.H.1    Kim, K.D.2    Cho, Y.J.3    Roe, J.H.4
  • 7
    • 0037428470 scopus 로고    scopus 로고
    • ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress
    • Cunnea PM, Miranda-Vizuete A, Bertoli G, et al. 2003. ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress. J Biol Chem 278: 1059-1066.
    • (2003) J Biol Chem , vol.278 , pp. 1059-1066
    • Cunnea, P.M.1    Miranda-Vizuete, A.2    Bertoli, G.3
  • 8
    • 0026020092 scopus 로고
    • Yeast thioredoxin genes
    • Gan ZR. 1991. Yeast thioredoxin genes. J Biol Chem 266: 1692-1696.
    • (1991) J Biol Chem , vol.266 , pp. 1692-1696
    • Gan, Z.R.1
  • 9
    • 33750915613 scopus 로고    scopus 로고
    • Thioredoxin-1 and posttranslational modifications
    • Haendeler J. 2006. Thioredoxin-1 and posttranslational modifications. Antioxid Redox Signal 8: 1723-1728.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1723-1728
    • Haendeler, J.1
  • 10
    • 15544389841 scopus 로고    scopus 로고
    • Rapid subfunctionalization accompanied by prolonged and substantial neofunctionalization in duplicate gene evolution
    • He X, Zhang J. 2005. Rapid subfunctionalization accompanied by prolonged and substantial neofunctionalization in duplicate gene evolution. Genetics 169: 1157-1164.
    • (2005) Genetics , vol.169 , pp. 1157-1164
    • He, X.1    Zhang, J.2
  • 11
    • 0033600744 scopus 로고    scopus 로고
    • Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-κB
    • Hirota K, Murata M, Sachi Y, et al. 1999. Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-κB. J Biol Chem 274: 27891-27897.
    • (1999) J Biol Chem , vol.274 , pp. 27891-27897
    • Hirota, K.1    Murata, M.2    Sachi, Y.3
  • 12
    • 0036290861 scopus 로고    scopus 로고
    • Thioredoxin superfamily and thioredoxin-inducing agents
    • Hirota K, Nakamura H, Masutani H, Yodoi J. 2002. Thioredoxin superfamily and thioredoxin-inducing agents. Ann N Y Acad Sci 957: 189-199.
    • (2002) Ann N Y Acad Sci , vol.957 , pp. 189-199
    • Hirota, K.1    Nakamura, H.2    Masutani, H.3    Yodoi, J.4
  • 13
    • 0034534165 scopus 로고    scopus 로고
    • Antioxidant function of thioredoxin and glutaredoxin systems
    • Holmgren A. 2000. Antioxidant function of thioredoxin and glutaredoxin systems. Antioxid Redox Signal 2: 811-820.
    • (2000) Antioxid Redox Signal , vol.2 , pp. 811-820
    • Holmgren, A.1
  • 14
    • 0029187491 scopus 로고
    • Thioredoxin and thioredoxin reductase
    • Holmgren A, Björnstedt M 1995. Thioredoxin and thioredoxin reductase. Methods Enzymol 252: 199-208.
    • (1995) Methods Enzymol , vol.252 , pp. 199-208
    • Holmgren, A.1    Björnstedt, M.2
  • 15
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito H, Fukuda Y, Murata K, Kimura A. 1983. Transformation of intact yeast cells treated with alkali cations. J Bacteriol 153: 163-168.
    • (1983) J Bacteriol , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 16
    • 0028774178 scopus 로고
    • High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin
    • Jeng MF, Campbell AP, Begley T, et al. 1994. High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin. Structure 2: 853-868.
    • (1994) Structure , vol.2 , pp. 853-868
    • Jeng, M.F.1    Campbell, A.P.2    Begley, T.3
  • 17
    • 31544452809 scopus 로고    scopus 로고
    • Characterization of human thioredoxin-like-1: Potential involvement in the cellular response against glucose deprivation
    • Jiménez A, Pelto-Huikko M, Gustafsson J-Å, Miranda-Vizuete A. 2006. Characterization of human thioredoxin-like-1: potential involvement in the cellular response against glucose deprivation. FEBS Lett 580: 960-967.
    • (2006) FEBS Lett , vol.580 , pp. 960-967
    • Jiménez, A.1    Pelto-Huikko, M.2    Gustafsson, J.-Å.3    Miranda-Vizuete, A.4
  • 18
    • 18344386776 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of a human thioredoxin-like protein
    • Jin J, Chen X, Zhou Y, et al. 2002. Crystal structure of the catalytic domain of a human thioredoxin-like protein. Eur J Biochem 269: 2060-2068.
    • (2002) Eur J Biochem , vol.269 , pp. 2060-2068
    • Jin, J.1    Chen, X.2    Zhou, Y.3
  • 19
    • 33744962865 scopus 로고    scopus 로고
    • Redefining oxidative stress
    • Jones DP. 2006. Redefining oxidative stress. Antioxid Redox Signal 8: 1865-1879.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1865-1879
    • Jones, D.P.1
  • 21
    • 0025865875 scopus 로고
    • Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis
    • Krause G, Holmgren A. 1991. Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis. J Biol Chem 266: 4056-4066.
    • (1991) J Biol Chem , vol.266 , pp. 4056-4066
    • Krause, G.1    Holmgren, A.2
  • 22
    • 0033582416 scopus 로고    scopus 로고
    • A new antioxidant with alkyl hydroperoxide defence properties in yeast
    • Lee J, Spector D, Godon C, Labarre J, Toledano MB. 1999. A new antioxidant with alkyl hydroperoxide defence properties in yeast. J Biol Chem 274: 4537-4544.
    • (1999) J Biol Chem , vol.274 , pp. 4537-4544
    • Lee, J.1    Spector, D.2    Godon, C.3    Labarre, J.4    Toledano, M.B.5
  • 23
    • 0032563204 scopus 로고    scopus 로고
    • Purification, molecular cloning and characterization of TRP32, a novel thioredoxin-related mammalian protein of 32 kDa
    • Lee K-K, Murakawa M, Takahashi S, et al. 1998. Purification, molecular cloning and characterization of TRP32, a novel thioredoxin-related mammalian protein of 32 kDa. J Biol Chem 273: 19160-19166.
    • (1998) J Biol Chem , vol.273 , pp. 19160-19166
    • Lee, K.-K.1    Murakawa, M.2    Takahashi, S.3
  • 24
    • 0037012671 scopus 로고    scopus 로고
    • Characterization and regulation of a second gene encoding thioredoxin from the fission yeast
    • Lee YJ, Cho YW, Kim D, et al. 2002. Characterization and regulation of a second gene encoding thioredoxin from the fission yeast. Biochim Biophys Acta 1575: 143-147.
    • (2002) Biochim Biophys Acta , vol.1575 , pp. 143-147
    • Lee, Y.J.1    Cho, Y.W.2    Kim, D.3
  • 25
    • 33746112995 scopus 로고    scopus 로고
    • ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe
    • Matsuyama A, Arai R, Yashiroda Y, et al. 2006. ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe. Nat Biotechnol 24: 841-847.
    • (2006) Nat Biotechnol , vol.24 , pp. 841-847
    • Matsuyama, A.1    Arai, R.2    Yashiroda, Y.3
  • 26
    • 0032481292 scopus 로고    scopus 로고
    • Molecular cloning and expression of a cDNA encoding a human thioredoxin-like protein
    • Miranda-Vizuete A, Gustafsson J-Å, Spyrou G. 1998. Molecular cloning and expression of a cDNA encoding a human thioredoxin-like protein. Biochem Biophys Res Commun 243: 284-288.
    • (1998) Biochem Biophys Res Commun , vol.243 , pp. 284-288
    • Miranda-Vizuete, A.1    Gustafsson, J.-Å.2    Spyrou, G.3
  • 27
    • 0035943725 scopus 로고    scopus 로고
    • Characterization of Sptrx, a novel member of the thioredoxin family specifically expressed in human spermatozoa
    • Miranda-Vizuete A, Ljung J, Damdimopoulos AE, et al. 2001. Characterization of Sptrx, a novel member of the thioredoxin family specifically expressed in human spermatozoa. J Biol Chem 276: 31567-31574.
    • (2001) J Biol Chem , vol.276 , pp. 31567-31574
    • Miranda-Vizuete, A.1    Ljung, J.2    Damdimopoulos, A.E.3
  • 28
    • 0026025891 scopus 로고
    • Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
    • Moreno S, Klar A, Nurse P. 1991. Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Methods Enzymol 194: 795-823.
    • (1991) Methods Enzymol , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 29
    • 17644395645 scopus 로고    scopus 로고
    • Thioredoxin and its related molecules: Update 2005
    • Nakamura H. 2005. Thioredoxin and its related molecules: update 2005. Antioxid Redox Signal 7: 823-828.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 823-828
    • Nakamura, H.1
  • 30
    • 0029953712 scopus 로고    scopus 로고
    • Green fluorescent protein as a marker for gene expression and subcellular localization in budding yeast
    • Niedenthal RK, Riles L, Johnston M, Hegemann JH. 1996. Green fluorescent protein as a marker for gene expression and subcellular localization in budding yeast. Yeast 12: 773-786.
    • (1996) Yeast , vol.12 , pp. 773-786
    • Niedenthal, R.K.1    Riles, L.2    Johnston, M.3    Hegemann, J.H.4
  • 31
    • 0033525509 scopus 로고    scopus 로고
    • Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae
    • Pedrajas JR, Kosmidou E, Miranda-Vizuete A, et al. 1999. Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae. J Biol Chem 274: 6366-6373.
    • (1999) J Biol Chem , vol.274 , pp. 6366-6373
    • Pedrajas, J.R.1    Kosmidou, E.2    Miranda-Vizuete, A.3
  • 32
    • 0021306414 scopus 로고
    • Isolation of DNA sequences preferentially expressed during sporulation in Saccharomyces cerevisiae
    • Percival-Smith A, Segall J. 1984. Isolation of DNA sequences preferentially expressed during sporulation in Saccharomyces cerevisiae. Mol Cell Biol 4: 142-150.
    • (1984) Mol Cell Biol , vol.4 , pp. 142-150
    • Percival-Smith, A.1    Segall, J.2
  • 33
    • 0035206849 scopus 로고    scopus 로고
    • Sptrx-2, a fusion protein composed of one thioredoxin and three tandemly repeated NDP-kinase domains, is expressed in human testis germ cells
    • Sadek CM, Damdimopoulos AE, Pelto-Huikko M, et al. 2001. Sptrx-2, a fusion protein composed of one thioredoxin and three tandemly repeated NDP-kinase domains, is expressed in human testis germ cells. Genes Cells 6: 1077-1090.
    • (2001) Genes Cells , vol.6 , pp. 1077-1090
    • Sadek, C.M.1    Damdimopoulos, A.E.2    Pelto-Huikko, M.3
  • 34
    • 0038644884 scopus 로고    scopus 로고
    • Characterization of human thioredoxin-like 2 (Txl-2): A novel microtubule-binding thioredoxin predominantly expressed in the cilia of lung airway epithelium and spermatid manchette and axoneme
    • Sadek CM, Jiménez A, Damdimopoulos AE, et al. 2003. Characterization of human thioredoxin-like 2 (Txl-2): a novel microtubule-binding thioredoxin predominantly expressed in the cilia of lung airway epithelium and spermatid manchette and axoneme. J Biol Chem 278: 13133-13142.
    • (2003) J Biol Chem , vol.278 , pp. 13133-13142
    • Sadek, C.M.1    Jiménez, A.2    Damdimopoulos, A.E.3
  • 35
    • 33750214650 scopus 로고    scopus 로고
    • Exportin-5 orthologues are functionally divergent among species
    • Shibata S, Sasaki M, Miki T, et al. 2006. Exportin-5 orthologues are functionally divergent among species. Nucleic Acids Res 34: 4711-4721.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4711-4721
    • Shibata, S.1    Sasaki, M.2    Miki, T.3
  • 37
    • 2342487990 scopus 로고    scopus 로고
    • Cells have distinct mechanisms to maintain protection against different reactive oxygen species: Oxidative-stress-response genes
    • Thorpe GW, Fong CS, Alic N, Higgins VJ, Dawes IW. 2004. Cells have distinct mechanisms to maintain protection against different reactive oxygen species: oxidative-stress-response genes. Proc Natl Acad Sci USA 101: 6564-6569.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6564-6569
    • Thorpe, G.W.1    Fong, C.S.2    Alic, N.3    Higgins, V.J.4    Dawes, I.W.5
  • 38
    • 33646743554 scopus 로고    scopus 로고
    • A parallel proteomic and metabolomic analysis of the hydrogen peroxide- and Sty1p-dependent stress response in Schizosaccharomyces pombe
    • Weeks ME, Sinclair J, Butt A, et al. 2006. A parallel proteomic and metabolomic analysis of the hydrogen peroxide- and Sty1p-dependent stress response in Schizosaccharomyces pombe. Proteomics 6: 2772-2796.
    • (2006) Proteomics , vol.6 , pp. 2772-2796
    • Weeks, M.E.1    Sinclair, J.2    Butt, A.3
  • 39
    • 0023685552 scopus 로고
    • Cloning and expression of a cDNA for human thioredoxin
    • Wollman E, d'Auriol L, Rimsky L, et al. 1988. Cloning and expression of a cDNA for human thioredoxin. J Biol Chem 263: 15506-15512.
    • (1988) J Biol Chem , vol.263 , pp. 15506-15512
    • Wollman, E.1    d'Auriol, L.2    Rimsky, L.3
  • 40
    • 0037148758 scopus 로고    scopus 로고
    • The genome sequence of Schizosaccharomyces pombe
    • Wood V, Gwilliam R, Rajandream MA, et al. 2002. The genome sequence of Schizosaccharomyces pombe. Nature 415: 871-880.
    • (2002) Nature , vol.415 , pp. 871-880
    • Wood, V.1    Gwilliam, R.2    Rajandream, M.A.3


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