메뉴 건너뛰기




Volumn 6, Issue 5, 2007, Pages 764-775

Crm1-mediated nuclear export of the Schizosaccharomyces pombe transcription factor Cuf1 during a shift from low to high copper concentrations

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CELL RECEPTOR; COPPER; CUF1 PROTEIN, S POMBE; EXPORTIN 1 PROTEIN; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; KARYOPHERIN; LEPTOMYCIN B; SCHIZOSACCHAROMYCES POMBE PROTEIN; SILVER; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; UNSATURATED FATTY ACID;

EID: 34249746266     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00002-07     Document Type: Article
Times cited : (16)

References (55)
  • 3
    • 33746889803 scopus 로고    scopus 로고
    • Copper homeostasis in eukaryotes: Teetering on a tightrope
    • Balamurugan, K., and W. Schaffner. 2006. Copper homeostasis in eukaryotes: teetering on a tightrope. Biochim. Biophys. Acta 1763:737-746.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 737-746
    • Balamurugan, K.1    Schaffner, W.2
  • 4
    • 0035805543 scopus 로고    scopus 로고
    • The fission yeast copper-sensing transcription factor Cuf1 regulates the copper transporter gene expression through an Ace1/Amt1-like recognition sequence
    • Beaudoin, J., and S. Labbé. 2001. The fission yeast copper-sensing transcription factor Cuf1 regulates the copper transporter gene expression through an Ace1/Amt1-like recognition sequence. J. Biol. Chem. 276:15472-15480.
    • (2001) J. Biol. Chem , vol.276 , pp. 15472-15480
    • Beaudoin, J.1    Labbé, S.2
  • 5
    • 32944469753 scopus 로고    scopus 로고
    • Copper induces cytoplasmic retention of fission yeast transcription factor Cuf1
    • Beaudoin, J., and S. Labbé. 2006. Copper induces cytoplasmic retention of fission yeast transcription factor Cuf1. Eukaryot. Cell 5:277-292.
    • (2006) Eukaryot. Cell , vol.5 , pp. 277-292
    • Beaudoin, J.1    Labbé, S.2
  • 6
    • 30744431881 scopus 로고    scopus 로고
    • Functional dissection of Ctr4 and Ctr5 amino-terminal regions reveals motifs with redundant roles in copper transport
    • Beaudoin, J., J. Laliberté, and S. Labbé. 2006. Functional dissection of Ctr4 and Ctr5 amino-terminal regions reveals motifs with redundant roles in copper transport. Microbiology 152:209-222.
    • (2006) Microbiology , vol.152 , pp. 209-222
    • Beaudoin, J.1    Laliberté, J.2    Labbé, S.3
  • 7
    • 0038529682 scopus 로고    scopus 로고
    • The Schizosaccharomyces pombe Cuf1 is composed of functional modules from two distinct classes of copper metalloregulatory transcription factors
    • Beaudoin, J., A. Mercier, R. Langlois, and S. Labbé. 2003. The Schizosaccharomyces pombe Cuf1 is composed of functional modules from two distinct classes of copper metalloregulatory transcription factors. J. Biol. Chem. 278:14565-14577.
    • (2003) J. Biol. Chem , vol.278 , pp. 14565-14577
    • Beaudoin, J.1    Mercier, A.2    Langlois, R.3    Labbé, S.4
  • 9
    • 0030693969 scopus 로고    scopus 로고
    • Identification of a second myosin-II in Schizosaccharomyces pombe: Myp2p is conditionally required for cytokinesis
    • Bezanilla, M., S. L. Forsburg, and T. D. Pollard. 1997. Identification of a second myosin-II in Schizosaccharomyces pombe: Myp2p is conditionally required for cytokinesis. Mol. Biol. Cell 8:2693-2705.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2693-2705
    • Bezanilla, M.1    Forsburg, S.L.2    Pollard, T.D.3
  • 10
    • 0142135189 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe cells lacking the Ran-binding protein Hba1 show a multidrug resistance phenotype due to constitutive nuclear accumulation of Pap1
    • Castillo, E. A., A. P. Vivancos, N. Jones, J. Ayte, and E. Hidalgo. 2003. Schizosaccharomyces pombe cells lacking the Ran-binding protein Hba1 show a multidrug resistance phenotype due to constitutive nuclear accumulation of Pap1. J. Biol. Chem. 278:40565- 40572.
    • (2003) J. Biol. Chem , vol.278 , pp. 40565-40572
    • Castillo, E.A.1    Vivancos, A.P.2    Jones, N.3    Ayte, J.4    Hidalgo, E.5
  • 11
    • 5044235320 scopus 로고    scopus 로고
    • Supraphysiological nuclear export signals bind CRM1 independently of RanGTP and arrest at Nup358
    • Engelsma, D., R. Bernad, J. Calafat, and M. Fornerod. 2004. Supraphysiological nuclear export signals bind CRM1 independently of RanGTP and arrest at Nup358. EMBO J. 23:3643-3652.
    • (2004) EMBO J , vol.23 , pp. 3643-3652
    • Engelsma, D.1    Bernad, R.2    Calafat, J.3    Fornerod, M.4
  • 12
    • 0034760338 scopus 로고    scopus 로고
    • RanBP3 influences interactions between CRM1 and its nuclear protein export substrates
    • Englmeier, L., M. Fornerod, F. R. Bischoff, C. Petosa, I. W. Mattaj, and U. Kutay. 2001. RanBP3 influences interactions between CRM1 and its nuclear protein export substrates. EMBO Rep. 2:926-932.
    • (2001) EMBO Rep , vol.2 , pp. 926-932
    • Englmeier, L.1    Fornerod, M.2    Bischoff, F.R.3    Petosa, C.4    Mattaj, I.W.5    Kutay, U.6
  • 13
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod, M., M. Ohno, M. Yoshida, and I. W. Mattaj. 1997. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90:1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 14
    • 0027185274 scopus 로고
    • Comparison of Schizosaccharomyces pombe expression systems
    • Forsburg, S. L. 1993. Comparison of Schizosaccharomyces pombe expression systems. Nucleic Acids Res. 21:2955-2956.
    • (1993) Nucleic Acids Res , vol.21 , pp. 2955-2956
    • Forsburg, S.L.1
  • 15
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda, M., S. Asano, T. Nakamura, M. Adachi, M. Yoshida, M. Yanagida, and E. Nishida. 1997. CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature 390:308-311.
    • (1997) Nature , vol.390 , pp. 308-311
    • Fukuda, M.1    Asano, S.2    Nakamura, T.3    Adachi, M.4    Yoshida, M.5    Yanagida, M.6    Nishida, E.7
  • 16
    • 0032524018 scopus 로고    scopus 로고
    • Phosphorylation and association with the transcription factor Atf1 regulate localization of Spc1/ Sty1 stress-activated kinase in fission yeast
    • Gaits, F., G. Degols, K. Shiozaki, and P. Russell. 1998. Phosphorylation and association with the transcription factor Atf1 regulate localization of Spc1/ Sty1 stress-activated kinase in fission yeast. Genes Dev. 12:1464-1473.
    • (1998) Genes Dev , vol.12 , pp. 1464-1473
    • Gaits, F.1    Degols, G.2    Shiozaki, K.3    Russell, P.4
  • 17
    • 0026740508 scopus 로고
    • Biologically relevant metal ion-dependent hydroxyl radical generation
    • Halliwell, B., and J. M. Gutteridge. 1992. Biologically relevant metal ion-dependent hydroxyl radical generation. FEBS Lett. 307:108-112.
    • (1992) FEBS Lett , vol.307 , pp. 108-112
    • Halliwell, B.1    Gutteridge, J.M.2
  • 18
    • 0028358324 scopus 로고
    • The transcription factor MTF-1 is essential for basal and heavy metal-induced melallothionein gene expression
    • Heuchel, R., F. Radtke, O. Georgiev, G. Stark, M. Aguet, and W. Schaffner. 1994. The transcription factor MTF-1 is essential for basal and heavy metal-induced melallothionein gene expression. EMBO J. 13:2870-2875.
    • (1994) EMBO J , vol.13 , pp. 2870-2875
    • Heuchel, R.1    Radtke, F.2    Georgiev, O.3    Stark, G.4    Aguet, M.5    Schaffner, W.6
  • 19
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 20
    • 0026087180 scopus 로고
    • Preparation of high molecular weight RNA
    • Kohrer, K., and H. Domdey. 1991. Preparation of high molecular weight RNA. Methods Enzymol. 194:398-405.
    • (1991) Methods Enzymol , vol.194 , pp. 398-405
    • Kohrer, K.1    Domdey, H.2
  • 22
    • 0033591412 scopus 로고    scopus 로고
    • A novel nuclear export signal sensitive to oxidative stress in the fission yeast transcription factor Pap1
    • Kudo, N., H. Taoka, T. Toda, M. Yoshida, and S. Horinouchi. 1999. A novel nuclear export signal sensitive to oxidative stress in the fission yeast transcription factor Pap1. J. Biol. Chem. 274:15151-15158.
    • (1999) J. Biol. Chem , vol.274 , pp. 15151-15158
    • Kudo, N.1    Taoka, H.2    Toda, T.3    Yoshida, M.4    Horinouchi, S.5
  • 23
    • 14744301997 scopus 로고    scopus 로고
    • Leucine-rich nuclear-export signals: Born to be weak
    • Kutay, U., and S. Guttinger. 2005. Leucine-rich nuclear-export signals: born to be weak. Trends Cell Biol. 15:121-124.
    • (2005) Trends Cell Biol , vol.15 , pp. 121-124
    • Kutay, U.1    Guttinger, S.2
  • 25
    • 0040437349 scopus 로고    scopus 로고
    • A copper-sensing transcription factor regulates iron uptake genes in Schizosaccharomyces pombe
    • Labbé, S., M. M. O. Peña, A. R. Fernandes, and D. J. Thiele. 1999. A copper-sensing transcription factor regulates iron uptake genes in Schizosaccharomyces pombe. J. Biol. Chem. 274:36252- 36260.
    • (1999) J. Biol. Chem , vol.274 , pp. 36252-36260
    • Labbé, S.1    Peña, M.M.O.2    Fernandes, A.R.3    Thiele, D.J.4
  • 26
    • 0033388950 scopus 로고    scopus 로고
    • Pipes and wiring: The regulation of copper uptake and distribution in yeast
    • Labbé S., and D. J. Thiele. 1999. Pipes and wiring: the regulation of copper uptake and distribution in yeast. Trends Microbiol. 7:500-505.
    • (1999) Trends Microbiol , vol.7 , pp. 500-505
    • Labbé, S.1    Thiele, D.J.2
  • 28
    • 34247135913 scopus 로고    scopus 로고
    • Classical nuclear localization signals: Definition, function, and interaction with importin alpha
    • Lange, A., R. E. Mills, C. J. Lange, M. Stewart, S. E. Devine, and A. H. Corbett. 2007. Classical nuclear localization signals: definition, function, and interaction with importin alpha. J. Biol. Chem 282:5101-5105.
    • (2007) J. Biol. Chem , vol.282 , pp. 5101-5105
    • Lange, A.1    Mills, R.E.2    Lange, C.J.3    Stewart, M.4    Devine, S.E.5    Corbett, A.H.6
  • 29
    • 0035954439 scopus 로고    scopus 로고
    • Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export
    • Lindsay, M. E., J. M. Holaska, K. Welch, B. M. Paschal, and I. G. Macara. 2001. Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export. J. Cell Biol. 153:1391-1402.
    • (2001) J. Cell Biol , vol.153 , pp. 1391-1402
    • Lindsay, M.E.1    Holaska, J.M.2    Welch, K.3    Paschal, B.M.4    Macara, I.G.5
  • 30
    • 4644278442 scopus 로고    scopus 로고
    • Karyopherins: From nuclear-transport mediators to nuclear-function regulators
    • Mosammaparast, N., and L. F. Pemberton. 2004. Karyopherins: from nuclear-transport mediators to nuclear-function regulators. Trends Cell Biol. 14:547-556.
    • (2004) Trends Cell Biol , vol.14 , pp. 547-556
    • Mosammaparast, N.1    Pemberton, L.F.2
  • 31
    • 0028318159 scopus 로고
    • Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression
    • Nishi, K., M. Yoshida, D. Fujiwara, M. Nishikawa, S. Horinouchi, and T. Beppu. 1994. Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression. J. Biol. Chem. 269:6320-6324.
    • (1994) J. Biol. Chem , vol.269 , pp. 6320-6324
    • Nishi, K.1    Yoshida, M.2    Fujiwara, D.3    Nishikawa, M.4    Horinouchi, S.5    Beppu, T.6
  • 32
    • 0032941773 scopus 로고    scopus 로고
    • Disruption of the YRB2 gene retards nuclear protein export, causing a profound mitotic delay, and can be rescued by overexpression of XPO1/CRM1
    • Noguchi, E., Y. Saitoh, S. Sazer, and T. Nishimoto. 1999. Disruption of the YRB2 gene retards nuclear protein export, causing a profound mitotic delay, and can be rescued by overexpression of XPO1/CRM1. J. Biochem. (Tokyo) 125:574-585.
    • (1999) J. Biochem. (Tokyo) , vol.125 , pp. 574-585
    • Noguchi, E.1    Saitoh, Y.2    Sazer, S.3    Nishimoto, T.4
  • 33
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari, B., F. Bachelerie, and C. Dargemont. 1997. Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science 278:141-144.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 34
    • 14544299215 scopus 로고    scopus 로고
    • Mechanisms of receptor-mediated nuclear import and nuclear export
    • Pemberton, L. F., and B. M. Paschal. 2005. Mechanisms of receptor-mediated nuclear import and nuclear export. Traffic 6:187-198.
    • (2005) Traffic , vol.6 , pp. 187-198
    • Pemberton, L.F.1    Paschal, B.M.2
  • 35
    • 0036525717 scopus 로고    scopus 로고
    • Molecular mechanisms of copper uptake and distribution
    • Puig, S., and D. J. Thiele. 2002. Molecular mechanisms of copper uptake and distribution. Curr. Opin. Chem. Biol. 6:171-180.
    • (2002) Curr. Opin. Chem. Biol , vol.6 , pp. 171-180
    • Puig, S.1    Thiele, D.J.2
  • 37
    • 1842453678 scopus 로고    scopus 로고
    • From aging to virulence: Forging connections through the study of copper homeostasis in eukaryotic microorganisms
    • Rees, E. M., and D. J. Thiele. 2004. From aging to virulence: forging connections through the study of copper homeostasis in eukaryotic microorganisms. Curr. Opin. Microbiol. 7:175-184.
    • (2004) Curr. Opin. Microbiol , vol.7 , pp. 175-184
    • Rees, E.M.1    Thiele, D.J.2
  • 38
    • 1242277806 scopus 로고    scopus 로고
    • Metal-responsive transcription factors that regulate iron, zinc, and copper homeostasis in eukaryotic cells
    • Rutherford, J. C., and A. J. Bird. 2004. Metal-responsive transcription factors that regulate iron, zinc, and copper homeostasis in eukaryotic cells. Eukaryot. Cell 3:1-13.
    • (2004) Eukaryot. Cell , vol.3 , pp. 1-13
    • Rutherford, J.C.1    Bird, A.J.2
  • 39
    • 0042847393 scopus 로고    scopus 로고
    • Aft1p and Aft2p mediate iron-responsive gene expression in yeast through related promoter elements
    • Rutherford, J. C., S. Jaron, and D. R. Winge. 2003. Aft1p and Aft2p mediate iron-responsive gene expression in yeast through related promoter elements. J. Biol. Chem. 278:27636-27643.
    • (2003) J. Biol. Chem , vol.278 , pp. 27636-27643
    • Rutherford, J.C.1    Jaron, S.2    Winge, D.R.3
  • 40
    • 0035816670 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic trafficking of metal-regulatory transcription factor 1 is regulated by diverse stress signals
    • Saydam, N., O. Georgiev, M. Y. Nakano, U. F. Greber, and W. Schaffner. 2001. Nucleo-cytoplasmic trafficking of metal-regulatory transcription factor 1 is regulated by diverse stress signals. J. Biol. Chem. 276:25487-25495.
    • (2001) J. Biol. Chem , vol.276 , pp. 25487-25495
    • Saydam, N.1    Georgiev, O.2    Nakano, M.Y.3    Greber, U.F.4    Schaffner, W.5
  • 42
    • 0034737599 scopus 로고    scopus 로고
    • Zinc and cadmium can promote rapid nuclear translocation of metal response element-binding transcription factor-1
    • Smirnova, I. V., D. C. Bittel, R. Ravindra, H. Jiang, and G. K. Andrews. 2000. Zinc and cadmium can promote rapid nuclear translocation of metal response element-binding transcription factor-1. J. Biol. Chem. 275:9377-9384.
    • (2000) J. Biol. Chem , vol.275 , pp. 9377-9384
    • Smirnova, I.V.1    Bittel, D.C.2    Ravindra, R.3    Jiang, H.4    Andrews, G.K.5
  • 43
    • 0030985459 scopus 로고    scopus 로고
    • Exportin 1 (Crm1p) is an essential nuclear export factor
    • Stade, K., C. S. Ford, C. Guthrie, and K. Weis. 1997. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 90:1041-1050.
    • (1997) Cell , vol.90 , pp. 1041-1050
    • Stade, K.1    Ford, C.S.2    Guthrie, C.3    Weis, K.4
  • 44
    • 0032560478 scopus 로고    scopus 로고
    • A member of the Ran-binding protein family, Yrb2p, is involved in nuclear protein export
    • Taura, T., H. Krebber, and P. A. Silver. 1998. A member of the Ran-binding protein family, Yrb2p, is involved in nuclear protein export. Proc. Natl. Acad. Sci. USA 95:7427-7432.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7427-7432
    • Taura, T.1    Krebber, H.2    Silver, P.A.3
  • 45
    • 0031466904 scopus 로고    scopus 로고
    • Yrb2p is a nuclear protein that interacts with Prp20p, a yeast Rcc1 homologue
    • Taura, T., G. Schlenstedt, and P. A. Silver. 1997. Yrb2p is a nuclear protein that interacts with Prp20p, a yeast Rcc1 homologue. J. Biol. Chem. 272: 31877-31884.
    • (1997) J. Biol. Chem , vol.272 , pp. 31877-31884
    • Taura, T.1    Schlenstedt, G.2    Silver, P.A.3
  • 46
    • 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., S. Kuge, M. Samuels, B. A. Morgan, T. Toda, and N. Jones. 1998. 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. 12:1453-1463.
    • (1998) Genes Dev , vol.12 , pp. 1453-1463
    • Toone, W.M.1    Kuge, S.2    Samuels, M.3    Morgan, B.A.4    Toda, T.5    Jones, N.6
  • 47
    • 18544371009 scopus 로고    scopus 로고
    • Metals, toxicity and oxidative stress
    • Valko, M., H. Morris, and M. T. Cronin. 2005. Metals, toxicity and oxidative stress. Curr. Med. Chem. 12:1161-1208.
    • (2005) Curr. Med. Chem , vol.12 , pp. 1161-1208
    • Valko, M.1    Morris, H.2    Cronin, M.T.3
  • 48
    • 0002375072 scopus 로고    scopus 로고
    • Searching for interacting proteins with the two-hybrid system II
    • P. Bartel and S. Fields ed, Oxford University Press, New York. NY
    • Vojtek, A. B., J. A. Cooper, and S. M. Hollenberg. 1997. Searching for interacting proteins with the two-hybrid system II, p. 29-42. In P. Bartel and S. Fields (ed.), The yeast two-hybrid system: a practical approach. Oxford University Press, New York. NY.
    • (1997) The yeast two-hybrid system: A practical approach , pp. 29-42
    • Vojtek, A.B.1    Cooper, J.A.2    Hollenberg, S.M.3
  • 49
    • 0027250250 scopus 로고    scopus 로고
    • Vojtek, A. B., S. M. Hollenberg, and J. A. Cooper. 1993. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74:205-214.
    • Vojtek, A. B., S. M. Hollenberg, and J. A. Cooper. 1993. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74:205-214.
  • 50
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome: Nucleocytoplasmic transport throughout the cell cycle
    • Weis, K. 2003. Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle. Cell 112:441-451.
    • (2003) Cell , vol.112 , pp. 441-451
    • Weis, K.1
  • 51
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen, W., J. L. Meinkoth, R. Y. Tsien, and S. S. Taylor. 1995. Identification of a signal for rapid export of proteins from the nucleus. Cell 82:463-473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 52
    • 0028961739 scopus 로고
    • AFT1: A mediator of iron regulated transcriptional control in Saccharomyces cerevisiae
    • Yamaguchi-Iwai, Y., A. Dancis, and R. D. Klausner. 1995. AFT1: a mediator of iron regulated transcriptional control in Saccharomyces cerevisiae. EMBO J. 14:1231-1239.
    • (1995) EMBO J , vol.14 , pp. 1231-1239
    • Yamaguchi-Iwai, Y.1    Dancis, A.2    Klausner, R.D.3
  • 53
    • 0030054971 scopus 로고    scopus 로고
    • Iron-regulated DNA binding by the AFT1 protein controls the iron regulon in yeast
    • Yamaguchi-Iwai, Y., R. Stearman, A. Dancis, and R. D. Klausner. 1996. Iron-regulated DNA binding by the AFT1 protein controls the iron regulon in yeast. EMBO J. 15:3377-3384.
    • (1996) EMBO J , vol.15 , pp. 3377-3384
    • Yamaguchi-Iwai, Y.1    Stearman, R.2    Dancis, A.3    Klausner, R.D.4
  • 54
    • 0037166279 scopus 로고    scopus 로고
    • Subcellular localization of Aft1 transcription factor responds to iron status in Saccharomyces cerevisiae
    • Yamaguchi-Iwai, Y., R. Ueta, A. Fukunaka, and R. Sasaki. 2002. Subcellular localization of Aft1 transcription factor responds to iron status in Saccharomyces cerevisiae. J. Biol. Chem. 277:18914-18918.
    • (2002) J. Biol. Chem , vol.277 , pp. 18914-18918
    • Yamaguchi-Iwai, Y.1    Ueta, R.2    Fukunaka, A.3    Sasaki, R.4
  • 55
    • 0035827610 scopus 로고    scopus 로고
    • Identification of a novel high affinity copper transport complex in the fission yeast Schizosaccharomyces pombe
    • Zhou, H., and D. J. Thiele. 2001. Identification of a novel high affinity copper transport complex in the fission yeast Schizosaccharomyces pombe. J. Biol. Chem. 276:20529-20535.
    • (2001) J. Biol. Chem , vol.276 , pp. 20529-20535
    • Zhou, H.1    Thiele, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.