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Volumn 330, Issue 2, 2005, Pages 604-610

Localization and function of three monothiol glutaredoxins in Schizosaccharomyces pombe

Author keywords

Grx3 4 5; Mitochondria; Monothiol glutaredoxin; Nucleus; Oxidative stress; Sub cellular localization

Indexed keywords

DIAMIDE; GLUTAREDOXIN; HYDROGEN PEROXIDE; OXIDIZING AGENT; PARAQUAT;

EID: 15744374257     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.02.183     Document Type: Article
Times cited : (36)

References (33)
  • 1
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • A. Holmgren Thioredoxin and glutaredoxin systems J. Biol. Chem. 264 1989 13963 13966
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 2
    • 0033767925 scopus 로고    scopus 로고
    • Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress
    • O. Carmel-Harel, and G. Storz Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress Annu. Rev. Microbiol. 54 2000 439 461
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 439-461
    • Carmel-Harel, O.1    Storz, G.2
  • 3
    • 0035131144 scopus 로고    scopus 로고
    • Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions
    • C.M. Grant Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions Mol. Microbiol. 39 2001 533 541
    • (2001) Mol. Microbiol. , vol.39 , pp. 533-541
    • Grant, C.M.1
  • 5
    • 0036359544 scopus 로고    scopus 로고
    • Glutaredoxins and oxidative stress defense in yeast
    • E. Herrero, and J. Ros Glutaredoxins and oxidative stress defense in yeast Methods Enzymol. 348 2002 136 146
    • (2002) Methods Enzymol. , vol.348 , pp. 136-146
    • Herrero, E.1    Ros, J.2
  • 6
    • 0025993780 scopus 로고
    • A putative glutathione-binding site in T4 glutaredoxin investigated by site-directed mutagenesis
    • M. Nikkola, F.K. Gleason, M. Saarinen, T. Joelson, O. Bjornberg, and H. Eklund A putative glutathione-binding site in T4 glutaredoxin investigated by site-directed mutagenesis J. Biol. Chem. 266 1991 16105 16112
    • (1991) J. Biol. Chem. , vol.266 , pp. 16105-16112
    • Nikkola, M.1    Gleason, F.K.2    Saarinen, M.3    Joelson, T.4    Bjornberg, O.5    Eklund, H.6
  • 7
    • 0025788552 scopus 로고
    • Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis
    • Y. Yang, and W.W. Wells Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis J. Biol. Chem. 266 1991 12759 12765
    • (1991) J. Biol. Chem. , vol.266 , pp. 12759-12765
    • Yang, Y.1    Wells, W.W.2
  • 8
    • 0026799490 scopus 로고
    • Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14-S) and its mixed disulfide with glutathione
    • J.H. Bushweller, F. Aslund, K. Wuthrich, and A. Holmgren Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14-S) and its mixed disulfide with glutathione Biochemistry 31 1992 9288 9293
    • (1992) Biochemistry , vol.31 , pp. 9288-9293
    • Bushweller, J.H.1    Aslund, F.2    Wuthrich, K.3    Holmgren, A.4
  • 9
    • 0040932016 scopus 로고    scopus 로고
    • Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae
    • M.T. Rodriguez-Manzaneque, J. Ros, E. Cabiscol, A. Sorribas, and E. Herrero Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae Mol. Cell. Biol. 19 1999 8180 8190
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8180-8190
    • Rodriguez-Manzaneque, M.T.1    Ros, J.2    Cabiscol, E.3    Sorribas, A.4    Herrero, E.5
  • 10
    • 0028804668 scopus 로고
    • Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin
    • C.A. Padilla, E. Martinez-Galisteo, J.A. Barcena, G. Spyrou, and A. Holmgren Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin Eur. J. Biochem. 227 1995 27 34
    • (1995) Eur. J. Biochem. , vol.227 , pp. 27-34
    • Padilla, C.A.1    Martinez-Galisteo, E.2    Barcena, J.A.3    Spyrou, G.4    Holmgren, A.5
  • 13
    • 0037096975 scopus 로고    scopus 로고
    • Two isoforms of Saccharomyces cerevisiae glutaredoxin 2 are expressed in vivo and localize to different subcellular compartments
    • J.R. Pedrajas, P. Porras, E. Martinez-Galisteo, C.A. Padilla, A. Miranda-Vizuete, and J.A. Barcena Two isoforms of Saccharomyces cerevisiae glutaredoxin 2 are expressed in vivo and localize to different subcellular compartments Biochem. J. 364 2002 617 623
    • (2002) Biochem. J. , vol.364 , pp. 617-623
    • Pedrajas, J.R.1    Porras, P.2    Martinez-Galisteo, E.3    Padilla, C.A.4    Miranda-Vizuete, A.5    Barcena, J.A.6
  • 14
    • 10644242480 scopus 로고    scopus 로고
    • Nuclear monothiol glutaredoxins of Saccharomyces cerevisiae can function as mitochondrial glutaredoxins
    • M.M. Molina, G. Belli, M.A. de la Torre, M.T. Rodriguez-Manzaneque, and E. Herrero Nuclear monothiol glutaredoxins of Saccharomyces cerevisiae can function as mitochondrial glutaredoxins J. Biol. Chem. 279 2004 51923 51930
    • (2004) J. Biol. Chem. , vol.279 , pp. 51923-51930
    • Molina, M.M.1    Belli, G.2    De La Torre, M.A.3    Rodriguez-Manzaneque, M.T.4    Herrero, E.5
  • 15
    • 0942268722 scopus 로고    scopus 로고
    • Analysis of the interaction between piD261/Bud32, an evolutionarily conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin
    • R. Lopreiato, S. Facchin, G. Sartori, G. Arrigoni, S. Casonato, M. Ruzzene, L.A. Pinna, and G. Carignani Analysis of the interaction between piD261/Bud32, an evolutionarily conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin Biochem. J. 377 2004 395 405
    • (2004) Biochem. J. , vol.377 , pp. 395-405
    • Lopreiato, R.1    Facchin, S.2    Sartori, G.3    Arrigoni, G.4    Casonato, S.5    Ruzzene, M.6    Pinna, L.A.7    Carignani, G.8
  • 16
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • M.T. Rodriguez-Manzaneque, J. Tamarit, G. Belli, J. Ros, and E. Herrero Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes Mol. Biol. Cell 13 2002 1109 1121
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1109-1121
    • Rodriguez-Manzaneque, M.T.1    Tamarit, J.2    Belli, G.3    Ros, J.4    Herrero, E.5
  • 17
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • U. Muhlenhoff, J. Gerber, N. Richhardt, and R. Lill Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p EMBO J. 22 2003 4815 4825
    • (2003) EMBO J. , vol.22 , pp. 4815-4825
    • Muhlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 18
    • 3843120910 scopus 로고    scopus 로고
    • Differential expression and role of two dithiol glutaredoxins Grx1 and Grx2 in Schizosaccharomyces pombe
    • W.H. Chung, K.D. Kim, Y.J. Cho, and J.H. Roe Differential expression and role of two dithiol glutaredoxins Grx1 and Grx2 in Schizosaccharomyces pombe Biochem. Biophys. Res. Commun. 321 2004 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
  • 19
    • 0037148758 scopus 로고    scopus 로고
    • The genome sequence of Schizosaccharomyces pombe
    • V. Wood The genome sequence of Schizosaccharomyces pombe Nature 415 2002 871 880
    • (2002) Nature , vol.415 , pp. 871-880
    • Wood, V.1
  • 20
    • 0026025891 scopus 로고
    • Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
    • S. Moreno, A. Klar, and P. Nurse Molecular genetic analysis of fission yeast Schizosaccharomyces pombe Methods Enzymol. 194 1991 795 823
    • (1991) Methods Enzymol. , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 22
    • 0024215989 scopus 로고
    • Genetic engineering of Schizosaccharomyces pombe: A system for gene disruption and replacement using the ura4 gene as a selectable marker
    • C. Grimm, J. Kohli, J. Murray, and K. Maundrell Genetic engineering of Schizosaccharomyces pombe: a system for gene disruption and replacement using the ura4 gene as a selectable marker Mol. Gen. Genet. 215 1988 81 86
    • (1988) Mol. Gen. Genet. , vol.215 , pp. 81-86
    • Grimm, C.1    Kohli, J.2    Murray, J.3    Maundrell, K.4
  • 23
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • A. Wach, A. Brachat, R. Pohlmann, and P. Philippsen New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae Yeast 10 1994 1793 1808
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsen, P.4
  • 25
    • 0035029131 scopus 로고    scopus 로고
    • Properties and biological activities of thioredoxins
    • G. Powis, and W.R. Montfort Properties and biological activities of thioredoxins Annu. Rev. Pharmacol. Toxicol. 41 2001 261 295
    • (2001) Annu. Rev. Pharmacol. Toxicol. , vol.41 , pp. 261-295
    • Powis, G.1    Montfort, W.R.2
  • 26
    • 0034089165 scopus 로고    scopus 로고
    • Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library
    • D.Q. Ding, Y. Tomita, A. Yamamoto, Y. Chikashige, T. Haraguchi, and Y. Hiraoka Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library Genes Cells 5 2000 169 190
    • (2000) Genes Cells , vol.5 , pp. 169-190
    • Ding, D.Q.1    Tomita, Y.2    Yamamoto, A.3    Chikashige, Y.4    Haraguchi, T.5    Hiraoka, Y.6
  • 27
    • 0031719952 scopus 로고    scopus 로고
    • The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species
    • S. Luikenhuis, G. Perrone, I.W. Dawes, and C.M. Grant The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species Mol. Biol. Cell 9 1998 1081 1091
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1081-1091
    • Luikenhuis, S.1    Perrone, G.2    Dawes, I.W.3    Grant, C.M.4
  • 28
    • 0034326925 scopus 로고    scopus 로고
    • PICOT-HD: A highly conserved protein domain that is often associated with thioredoxin and glutaredoxin modules
    • N. Isakov, S. Witte, and A. Altman PICOT-HD: a highly conserved protein domain that is often associated with thioredoxin and glutaredoxin modules Trends Biochem. Sci. 25 2000 537 539
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 537-539
    • Isakov, N.1    Witte, S.2    Altman, A.3
  • 29
    • 0035813229 scopus 로고    scopus 로고
    • Plasmodium falciparum possesses a classical glutaredoxin and a second, glutaredoxin-like protein with a PICOT homology domain
    • S. Rahlfs, M. Fischer, and K. Becker Plasmodium falciparum possesses a classical glutaredoxin and a second, glutaredoxin-like protein with a PICOT homology domain J. Biol. Chem. 276 2001 37133 37140
    • (2001) J. Biol. Chem. , vol.276 , pp. 37133-37140
    • Rahlfs, S.1    Fischer, M.2    Becker, K.3
  • 30
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • J.C. Bardwell, K. McGovern, and J. Beckwith Identification of a protein required for disulfide bond formation in vivo Cell 67 1991 581 589
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 31
    • 2542475140 scopus 로고    scopus 로고
    • Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
    • E. Gross, D.B. Kastner, C.A. Kaiser, and D. Fass Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell Cell 117 2004 601 610
    • (2004) Cell , vol.117 , pp. 601-610
    • Gross, E.1    Kastner, D.B.2    Kaiser, C.A.3    Fass, D.4
  • 32
    • 6344293985 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe ER oxidoreductin-like proteins SpEro1a p and SpEro1b p
    • K. Kettner, A. Blomberg, and G. Rodel Schizosaccharomyces pombe ER oxidoreductin-like proteins SpEro1a p and SpEro1b p Yeast 21 2004 1035 1044
    • (2004) Yeast , vol.21 , pp. 1035-1044
    • Kettner, K.1    Blomberg, A.2    Rodel, G.3
  • 33
    • 0036150323 scopus 로고    scopus 로고
    • Sulphur amino acid synthesis in Schizosaccharomyces pombe represents a specific variant of sulphur metabolism in fungi
    • J. Brzywczy, M. Sienko, A. Kucharska, and A. Paszewski Sulphur amino acid synthesis in Schizosaccharomyces pombe represents a specific variant of sulphur metabolism in fungi Yeast 19 2002 29 35
    • (2002) Yeast , vol.19 , pp. 29-35
    • Brzywczy, J.1    Sienko, M.2    Kucharska, A.3    Paszewski, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.