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Volumn 18, Issue 8, 2008, Pages 1368-1376

Proteomic analysis of recombinant Saccharomyces cerevisiae upon iron deficiency induced via human H-ferritin production

Author keywords

H ferritin; Iron deficiency; Saccharomyces cerevisiae; Two dimensional gel electrophoresis (2 DE)

Indexed keywords

FERRITIN; FOLIC ACID; HEAT SHOCK PROTEIN; IRON; METHIONINE; PURINE;

EID: 56749106857     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (10)

References (29)
  • 2
    • 0027943262 scopus 로고
    • Ferric iron reduction and iron uptake in eukaryotes: Studies with the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe
    • C. Hershko, A. M. Konijn, and P. Aisen eds, Plenum Press, New York
    • Anderson, G. A., A. Dancis, D. G. Roman, and R. D. Klausner. 1994. Ferric iron reduction and iron uptake in eukaryotes: Studies with the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, pp. 81-89. In C. Hershko, A. M. Konijn, and P. Aisen (eds.), Progress in Iron Research. Plenum Press, New York.
    • (1994) Progress in Iron Research , pp. 81-89
    • Anderson, G.A.1    Dancis, A.2    Roman, D.G.3    Klausner, R.D.4
  • 4
    • 0028067470 scopus 로고
    • Iron incorporation into ferritins: Evidence for the transfer of monomeric Fe (III) between ferritin molecules and for the formation of an unusual mineral in the ferritin of Escherichia coli
    • Bauminger, E. R., A. Treffry, A. J. Hudson, D. Hechel, N. W. Hodson, S. C. Andrews, et al. 1994. Iron incorporation into ferritins: Evidence for the transfer of monomeric Fe (III) between ferritin molecules and for the formation of an unusual mineral in the ferritin of Escherichia coli. Biochem. J. 302: 813-820.
    • (1994) Biochem. J , vol.302 , pp. 813-820
    • Bauminger, E.R.1    Treffry, A.2    Hudson, A.J.3    Hechel, D.4    Hodson, N.W.5    Andrews, S.C.6
  • 5
    • 0034669350 scopus 로고    scopus 로고
    • Conformational changes induced in the Saccharomyces cerevisiae GTPase-associated rRNA by ribosomal stalk components and a translocation inhibitor
    • Briones, C. and J. P. Ballesta. 2000. Conformational changes induced in the Saccharomyces cerevisiae GTPase-associated rRNA by ribosomal stalk components and a translocation inhibitor. Nucleic Acids Res. 28: 4497-4505.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4497-4505
    • Briones, C.1    Ballesta, J.P.2
  • 6
    • 0025086816 scopus 로고
    • SSB1 of the yeast Sacchromyces cerevisiae is a nuclear-specific, silver binding protein that is associated with the snR10 and snR11 small nuclear RNA
    • Clark, M. W., M. L. R. Yip, J. Compbell, and J. Abelson. 1990. SSB1 of the yeast Sacchromyces cerevisiae is a nuclear-specific, silver binding protein that is associated with the snR10 and snR11 small nuclear RNA. J. Cell Biol. 111: 1741-1751.
    • (1990) J. Cell Biol , vol.111 , pp. 1741-1751
    • Clark, M.W.1    Yip, M.L.R.2    Compbell, J.3    Abelson, J.4
  • 7
    • 0036629250 scopus 로고    scopus 로고
    • rRNA modifications and ribosome function
    • Decatur, W. A. and M. J. Fournier. 2002. rRNA modifications and ribosome function. Trends Biochem. Sci. 27: 344-351.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 344-351
    • Decatur, W.A.1    Fournier, M.J.2
  • 8
    • 0031688260 scopus 로고    scopus 로고
    • Synthesis of glutamine, glycine and 10-formyl tetrahydrofolate is coregulated with purine biosynthesis in Saccharomyces cerevisiae
    • Denis, V. and B. Dignan-Fornier. 1998. Synthesis of glutamine, glycine and 10-formyl tetrahydrofolate is coregulated with purine biosynthesis in Saccharomyces cerevisiae. Mol. Gen. Genet. 259: 246-255.
    • (1998) Mol. Gen. Genet , vol.259 , pp. 246-255
    • Denis, V.1    Dignan-Fornier, B.2
  • 9
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L. and A. Helenius. 2003. Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell. Biol. 4: 181-191.
    • (2003) Nat. Rev. Mol. Cell. Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 10
    • 0037353864 scopus 로고    scopus 로고
    • Yeast, a model organism for iron and copper metabolism studies
    • Freitas, J. D., H. Wintz, J. H. Kim, H. Poynton, T. Fox, and C. Vulpe. 2003. Yeast, a model organism for iron and copper metabolism studies. Biometals 16: 185-197.
    • (2003) Biometals , vol.16 , pp. 185-197
    • Freitas, J.D.1    Wintz, H.2    Kim, J.H.3    Poynton, H.4    Fox, T.5    Vulpe, C.6
  • 12
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins; molecular properties, iron storage function and cellular regulation
    • Harrison, P. M. and P. Arosio. 1996. The ferritins; molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1275: 161-203.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 13
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 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
  • 14
    • 33846586051 scopus 로고    scopus 로고
    • Enhanced expression of high-affinity iron transporters via H-ferritin production in yeast
    • Kim, K.-S., Y.-J. Chang, Y.-J. Chung, C.-U. Park, and H.-Y. Seo. 2007. Enhanced expression of high-affinity iron transporters via H-ferritin production in yeast. J. Biochem. Mol. Biol. 40: 82-87.
    • (2007) J. Biochem. Mol. Biol , vol.40 , pp. 82-87
    • Kim, K.-S.1    Chang, Y.-J.2    Chung, Y.-J.3    Park, C.-U.4    Seo, H.-Y.5
  • 16
    • 0022779096 scopus 로고
    • Negative regulatory gene for general control of amino acid biosynthesis in Saccharomyces cerevisiae
    • Myers, P. L., R. C. Skvirsky, M. L. Greenberg, and H. Greer. 1986. Negative regulatory gene for general control of amino acid biosynthesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 6: 3150-3155.
    • (1986) Mol. Cell. Biol , vol.6 , pp. 3150-3155
    • Myers, P.L.1    Skvirsky, R.C.2    Greenberg, M.L.3    Greer, H.4
  • 17
    • 0032705369 scopus 로고    scopus 로고
    • Iron-dependent changes in cellular energy metabolism: Influence on citric acid cycle and oxidative phosphorylation
    • Oexle, H., E. Gnaiger, and G. Weiss. 1999. Iron-dependent changes in cellular energy metabolism: Influence on citric acid cycle and oxidative phosphorylation. Biochim. Biophys. Acta 1413: 99-107.
    • (1999) Biochim. Biophys. Acta , vol.1413 , pp. 99-107
    • Oexle, H.1    Gnaiger, E.2    Weiss, G.3
  • 18
    • 0034694896 scopus 로고    scopus 로고
    • Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast
    • Okamura, K., Y. Kimata, H. Higashio, A. Tsuru, and K. Kohno. 2000. Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast. Biochem. Biophys. Res. Commun. 279: 445-450.
    • (2000) Biochem. Biophys. Res. Commun , vol.279 , pp. 445-450
    • Okamura, K.1    Kimata, Y.2    Higashio, H.3    Tsuru, A.4    Kohno, K.5
  • 19
    • 0034705423 scopus 로고    scopus 로고
    • Mimosine is a cell-specific antagonist of folate metabolism
    • Oppenheim, E. W., I. M. Nasrallh, M. G. Mastri, and P. J. Stover. 2000. Mimosine is a cell-specific antagonist of folate metabolism. J. Biol. Chem. 275: 19268-19274.
    • (2000) J. Biol. Chem , vol.275 , pp. 19268-19274
    • Oppenheim, E.W.1    Nasrallh, I.M.2    Mastri, M.G.3    Stover, P.J.4
  • 20
    • 0032579887 scopus 로고    scopus 로고
    • The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae
    • Planta, R. J. and W. H. Mager. 1998. The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae. Yeast 14: 471-477.
    • (1998) Yeast , vol.14 , pp. 471-477
    • Planta, R.J.1    Mager, W.H.2
  • 21
    • 0033773040 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae expresses three functionally distinct homologues of the Nramp family of metal transporters
    • Portnoy, M. E., X. F. Liu, and V. C. Culotta. 2000. Saccharomyces cerevisiae expresses three functionally distinct homologues of the Nramp family of metal transporters. Mol. Cell. Biol. 20: 7893-7902.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 7893-7902
    • Portnoy, M.E.1    Liu, X.F.2    Culotta, V.C.3
  • 22
    • 11844257593 scopus 로고    scopus 로고
    • Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation
    • Puig, S., E. Askeland, and D. J. Thiele. 2005. Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation. Cell 120: 99-110.
    • (2005) Cell , vol.120 , pp. 99-110
    • Puig, S.1    Askeland, E.2    Thiele, D.J.3
  • 23
    • 0033582433 scopus 로고    scopus 로고
    • Regulation of transition metal transport across the yeast plasma membrane
    • Radisky, D. C. and J. Kaplan. 1999. Regulation of transition metal transport across the yeast plasma membrane. J. Biol. Chem. 274: 4481-4484.
    • (1999) J. Biol. Chem , vol.274 , pp. 4481-4484
    • Radisky, D.C.1    Kaplan, J.2
  • 24
    • 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
  • 25
    • 1542344021 scopus 로고    scopus 로고
    • Endoplasmic reticulum quality control of unassembled iron transporter depends on Rer1p-mediated retrieval from the Golgi
    • Sato, M., K. Sato, and A. Nakano. 2004. Endoplasmic reticulum quality control of unassembled iron transporter depends on Rer1p-mediated retrieval from the Golgi. Mol. Biol. Cell 15: 1417-1424.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1417-1424
    • Sato, M.1    Sato, K.2    Nakano, A.3
  • 26
    • 1642440153 scopus 로고    scopus 로고
    • Enhanced expression and functional characterization of the human ferritin H- and L-chain genes in Saccharomyces cerevisiae
    • Seo, H.-Y., Y.-J. Chung, S.-J. Kim, C.-U. Park, and K.-S. Kim. 2003. Enhanced expression and functional characterization of the human ferritin H- and L-chain genes in Saccharomyces cerevisiae. Appl. Microbiol. Biotech. 63: 57-63.
    • (2003) Appl. Microbiol. Biotech , vol.63 , pp. 57-63
    • Seo, H.-Y.1    Chung, Y.-J.2    Kim, S.-J.3    Park, C.-U.4    Kim, K.-S.5
  • 29
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.