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Volumn 1763, Issue 7, 2006, Pages 646-651

Iron-dependent metabolic remodeling in S. cerevisiae

Author keywords

Heme; Iron; Metabolism; Oxygen; Sterol; Yeast

Indexed keywords

BIOTIN; GLUTAMATE SYNTHASE; GLUTAMINE; HEME; IRON; MESSENGER RNA; OXYGEN; PROTOPORPHYRINOGEN OXIDASE; SIDEROPHORE; STEROL;

EID: 33746920351     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2006.03.008     Document Type: Review
Times cited : (98)

References (38)
  • 1
    • 0033964626 scopus 로고    scopus 로고
    • Limitation of bacterial growth by dissolved organic matter and iron in the Southern Ocean
    • Church M.J., Hutchins D.A., and Ducklow H.W. Limitation of bacterial growth by dissolved organic matter and iron in the Southern Ocean. Appl. Environ. Microbiol. 66 (2000) 455-466
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 455-466
    • Church, M.J.1    Hutchins, D.A.2    Ducklow, H.W.3
  • 4
    • 0032422847 scopus 로고    scopus 로고
    • Siderophore-mediated iron uptake in Saccharomyces cerevisiae: the Sit1 gene encodes a ferrioxamine B permease that belongs to the major facilitator superfamily
    • Lesuisse E., Simon-Casteras M., and Labbe P. Siderophore-mediated iron uptake in Saccharomyces cerevisiae: the Sit1 gene encodes a ferrioxamine B permease that belongs to the major facilitator superfamily. Microbiology 144 (1998) 3455-3462
    • (1998) Microbiology , vol.144 , pp. 3455-3462
    • Lesuisse, E.1    Simon-Casteras, M.2    Labbe, P.3
  • 5
    • 0034616016 scopus 로고    scopus 로고
    • Desferrioxamine-mediated iron uptake in Saccharomyces cerevisiae. evidence for two pathways of iron uptake [in Process Citation]
    • Yun C.W., Ferea T., Rashford J., Ardon O., Brown P.O., Botstein D., Kaplan J., and Philpott C.C. Desferrioxamine-mediated iron uptake in Saccharomyces cerevisiae. evidence for two pathways of iron uptake [in Process Citation]. J. Biol. Chem. 275 (2000) 10709-10715
    • (2000) J. Biol. Chem. , vol.275 , pp. 10709-10715
    • Yun, C.W.1    Ferea, T.2    Rashford, J.3    Ardon, O.4    Brown, P.O.5    Botstein, D.6    Kaplan, J.7    Philpott, C.C.8
  • 6
    • 0025354925 scopus 로고
    • Genetic evidence that ferric reductase is required for iron uptake in Saccharomyces cerevisiae
    • Dancis A., Klausner R.D., Hinnebusch A.G., and Barriocanal J.G. Genetic evidence that ferric reductase is required for iron uptake in Saccharomyces cerevisiae. Mol. Cell. Biol. 10 (1990) 2294-2301
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2294-2301
    • Dancis, A.1    Klausner, R.D.2    Hinnebusch, A.G.3    Barriocanal, J.G.4
  • 7
    • 0028205244 scopus 로고
    • Two distinctly regulated genes are required for ferric reduction, the first step of iron uptake in Saccharomyces cerevisiae
    • Georgatsou E., and Alexandraki D. Two distinctly regulated genes are required for ferric reduction, the first step of iron uptake in Saccharomyces cerevisiae. Mol. Cell. Biol. 14 (1994) 3065-3073
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3065-3073
    • Georgatsou, E.1    Alexandraki, D.2
  • 8
    • 0028058038 scopus 로고
    • The Fet3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake
    • Askwith C., Eide D., Van Ho A., Bernard P.S., Li L., Davis-Kaplan S., Sipe D.M., and Kaplan J. The Fet3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell 76 (1994) 403-410
    • (1994) Cell , vol.76 , pp. 403-410
    • Askwith, C.1    Eide, D.2    Van Ho, A.3    Bernard, P.S.4    Li, L.5    Davis-Kaplan, S.6    Sipe, D.M.7    Kaplan, J.8
  • 9
    • 0030820818 scopus 로고    scopus 로고
    • Restriction of copper export in Saccharomyces cerevisiae to a late Golgi or post-Golgi compartment in the secretory pathway
    • Yuan D.S., Dancis A., and Klausner R.D. Restriction of copper export in Saccharomyces cerevisiae to a late Golgi or post-Golgi compartment in the secretory pathway. J. Biol. Chem. 272 (1997) 25787-25793
    • (1997) J. Biol. Chem. , vol.272 , pp. 25787-25793
    • Yuan, D.S.1    Dancis, A.2    Klausner, R.D.3
  • 10
    • 0242664909 scopus 로고    scopus 로고
    • The Snf1 protein kinase controls the induction of genes of the iron uptake pathway at the diauxic shift in Saccharomyces cerevisiae
    • Haurie V., Boucherie H., and Sagliocco F. The Snf1 protein kinase controls the induction of genes of the iron uptake pathway at the diauxic shift in Saccharomyces cerevisiae. J. Biol. Chem. 278 (2003) 45391-45396
    • (2003) J. Biol. Chem. , vol.278 , pp. 45391-45396
    • Haurie, V.1    Boucherie, H.2    Sagliocco, F.3
  • 11
    • 0026559542 scopus 로고
    • Regulation of gene expression by oxygen in Saccharomyces cerevisiae
    • Zitomer R.S., and Lowry C.V. Regulation of gene expression by oxygen in Saccharomyces cerevisiae. Microbiol. Rev. 56 (1992) 1-11
    • (1992) Microbiol. Rev. , vol.56 , pp. 1-11
    • Zitomer, R.S.1    Lowry, C.V.2
  • 12
    • 0242413149 scopus 로고    scopus 로고
    • Inhibition of heme biosynthesis prevents transcription of iron uptake genes in yeast
    • Crisp R.J., Pollington A., Galea C., Jaron S., Yamaguchi-Iwai Y., and Kaplan J. Inhibition of heme biosynthesis prevents transcription of iron uptake genes in yeast. J. Biol. Chem. 278 (2003) 45499-45506
    • (2003) J. Biol. Chem. , vol.278 , pp. 45499-45506
    • Crisp, R.J.1    Pollington, A.2    Galea, C.3    Jaron, S.4    Yamaguchi-Iwai, Y.5    Kaplan, J.6
  • 13
    • 0032483421 scopus 로고    scopus 로고
    • Spectral and kinetic properties of the Fet3 protein from Saccharomyces cerevisiae, a multinuclear copper ferroxidase enzyme
    • Hassett R.F., Yuan D.S., and Kosman D.J. Spectral and kinetic properties of the Fet3 protein from Saccharomyces cerevisiae, a multinuclear copper ferroxidase enzyme. J. Biol. Chem. 273 (1998) 23274-23282
    • (1998) J. Biol. Chem. , vol.273 , pp. 23274-23282
    • Hassett, R.F.1    Yuan, D.S.2    Kosman, D.J.3
  • 14
    • 0142248154 scopus 로고    scopus 로고
    • Role of the non-respiratory pathways in the utilization of molecular oxygen by Saccharomyces cerevisiae
    • Rosenfeld E., and Beauvoit B. Role of the non-respiratory pathways in the utilization of molecular oxygen by Saccharomyces cerevisiae. Yeast 20 (2003) 1115-1144
    • (2003) Yeast , vol.20 , pp. 1115-1144
    • Rosenfeld, E.1    Beauvoit, B.2
  • 15
    • 32544446330 scopus 로고    scopus 로고
    • Recruitment of Tup1p and Cti6p Regulates Heme Deficient Expression of Aft1p Target Genes
    • Crisp R.C., Adkins E.M., Kimmel E., and Kaplan J. Recruitment of Tup1p and Cti6p Regulates Heme Deficient Expression of Aft1p Target Genes. EMBO J. 25 (2006) 512-521
    • (2006) EMBO J. , vol.25 , pp. 512-521
    • Crisp, R.C.1    Adkins, E.M.2    Kimmel, E.3    Kaplan, J.4
  • 16
    • 0035800856 scopus 로고    scopus 로고
    • Ccc1 is a transporter that mediates vacuolar iron storage in yeast
    • Li L., Chen O.S., McVey Ward D., and Kaplan J. Ccc1 is a transporter that mediates vacuolar iron storage in yeast. J. Biol. Chem. 276 (2001) 29515-29519
    • (2001) J. Biol. Chem. , vol.276 , pp. 29515-29519
    • Li, L.1    Chen, O.S.2    McVey Ward, D.3    Kaplan, J.4
  • 17
    • 0033621395 scopus 로고    scopus 로고
    • The iron transporter Fth1p forms a complex with the Fet5 iron oxidase and resides on the vacuolar membrane
    • Urbanowski J.L., and Piper R.C. The iron transporter Fth1p forms a complex with the Fet5 iron oxidase and resides on the vacuolar membrane. J. Biol. Chem. 274 (1999) 38061-38070
    • (1999) J. Biol. Chem. , vol.274 , pp. 38061-38070
    • Urbanowski, J.L.1    Piper, R.C.2
  • 18
    • 0033773040 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae expresses three functionally distinct homologues of the Nramp family of metal transporters
    • Portnoy M.E., Liu X.F., and Culotta V.C. Saccharomyces cerevisiae expresses three functionally distinct homologues of the Nramp family of metal transporters. Mol. Cell. Biol. 20 (2000) 7893-7902
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7893-7902
    • Portnoy, M.E.1    Liu, X.F.2    Culotta, V.C.3
  • 19
    • 0028961739 scopus 로고
    • Aft1: a mediator of iron regulated transcriptional control in Saccharomyces cerevisiae
    • Yamaguchi-Iwai Y., Dancis A., and Klausner R.D. Aft1: a mediator of iron regulated transcriptional control in Saccharomyces cerevisiae. EMBO J. 14 (1995) 1231-1239
    • (1995) EMBO J. , vol.14 , pp. 1231-1239
    • Yamaguchi-Iwai, Y.1    Dancis, A.2    Klausner, R.D.3
  • 20
    • 0042847393 scopus 로고    scopus 로고
    • Aft1p and Aft2p mediate iron-responsive gene expression in yeast through related promoter elements
    • Rutherford J.C., Jaron S., and Winge D.R. Aft1p and Aft2p mediate iron-responsive gene expression in yeast through related promoter elements. J. Biol. Chem. 278 (2003) 27636-27643
    • (2003) J. Biol. Chem. , vol.278 , pp. 27636-27643
    • Rutherford, J.C.1    Jaron, S.2    Winge, D.R.3
  • 21
    • 22544475881 scopus 로고    scopus 로고
    • Direct activation of genes involved in intracellular iron use by the yeast iron-responsive transcription factor Aft2 without its paralog Aft1
    • Courel M., Lallet S., Camadro J.M., and Blaiseau P.L. Direct activation of genes involved in intracellular iron use by the yeast iron-responsive transcription factor Aft2 without its paralog Aft1. Mol. Cell. Biol. 25 (2005) 6760-6771
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6760-6771
    • Courel, M.1    Lallet, S.2    Camadro, J.M.3    Blaiseau, P.L.4
  • 22
    • 0037166279 scopus 로고    scopus 로고
    • Subcellular localization of Aft1 transcription factor responds to iron status in Saccharomyces cerevisiae
    • Yamaguchi-Iwai Y., Ueta R., Fukunaka A., and Sasaki R. Subcellular localization of Aft1 transcription factor responds to iron status in Saccharomyces cerevisiae. J. Biol. Chem. 277 (2002) 18914-18919
    • (2002) J. Biol. Chem. , vol.277 , pp. 18914-18919
    • Yamaguchi-Iwai, Y.1    Ueta, R.2    Fukunaka, A.3    Sasaki, R.4
  • 23
    • 3142667831 scopus 로고    scopus 로고
    • Transcription of the yeast iron regulon responds not directly to iron but rather to iron-sulfur cluster biosynthesis
    • Chen O.S., Crisp R.J., Valachovic M., Bard M., Winge D.R., and Kaplan J. Transcription of the yeast iron regulon responds not directly to iron but rather to iron-sulfur cluster biosynthesis. J. Biol. Chem. 280 (2004) 29513-29518
    • (2004) J. Biol. Chem. , vol.280 , pp. 29513-29518
    • Chen, O.S.1    Crisp, R.J.2    Valachovic, M.3    Bard, M.4    Winge, D.R.5    Kaplan, J.6
  • 24
    • 0034717027 scopus 로고    scopus 로고
    • The aconitase function of iron regulatory protein 1. Genetic studies in yeast implicate its role in iron-mediated redox regulation
    • Narahari J., Ma R., Wang M., and Walden W.E. The aconitase function of iron regulatory protein 1. Genetic studies in yeast implicate its role in iron-mediated redox regulation. J. Biol. Chem. 275 (2000) 16227-16234
    • (2000) J. Biol. Chem. , vol.275 , pp. 16227-16234
    • Narahari, J.1    Ma, R.2    Wang, M.3    Walden, W.E.4
  • 25
    • 0032746009 scopus 로고    scopus 로고
    • The essential role of mitochondria in the biogenesis of cellular iron-sulfur proteins
    • Lill R., Diekert K., Kaut A., Lange H., Pelzer W., Prohl C., and Kispal G. The essential role of mitochondria in the biogenesis of cellular iron-sulfur proteins. Biol. Chem. 380 (1999) 1157-1166
    • (1999) Biol. Chem. , vol.380 , pp. 1157-1166
    • Lill, R.1    Diekert, K.2    Kaut, A.3    Lange, H.4    Pelzer, W.5    Prohl, C.6    Kispal, G.7
  • 26
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • Kispal G., Csere P., Prohl C., and Lill R. The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 18 (1999) 3981-3989
    • (1999) EMBO J. , vol.18 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 27
    • 2942565619 scopus 로고    scopus 로고
    • The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins
    • Balk J., Pierik A.J., Netz D.J., Muhlenhoff U., and Lill R. The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins. EMBO J. 23 (2004) 2105-2115
    • (2004) EMBO J. , vol.23 , pp. 2105-2115
    • Balk, J.1    Pierik, A.J.2    Netz, D.J.3    Muhlenhoff, U.4    Lill, R.5
  • 28
    • 28544450863 scopus 로고    scopus 로고
    • The essential Wd40 protein Cia1 is involved in a late step of cytosolic and nuclear iron-sulfur protein assembly
    • Balk J., Aguilar Netz D.J., Tepper K., Pierik A.J., and Lill R. The essential Wd40 protein Cia1 is involved in a late step of cytosolic and nuclear iron-sulfur protein assembly. Mol. Cell. Biol. 25 (2005) 10833-10841
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10833-10841
    • Balk, J.1    Aguilar Netz, D.J.2    Tepper, K.3    Pierik, A.J.4    Lill, R.5
  • 30
    • 15444371876 scopus 로고    scopus 로고
    • Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis
    • Rutherford J.C., Ojeda L., Balk J., Muhlenhoff U., Lill R., and Winge D.R. Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis. J. Biol. Chem. 280 (2005) 10135-10140
    • (2005) J. Biol. Chem. , vol.280 , pp. 10135-10140
    • Rutherford, J.C.1    Ojeda, L.2    Balk, J.3    Muhlenhoff, U.4    Lill, R.5    Winge, D.R.6
  • 33
    • 0141704206 scopus 로고    scopus 로고
    • Regulation of intracellular heme levels by Hmx1, a homologue of heme oxygenase, in Saccharomyces cerevisiae
    • Protchenko O., and Philpott C.C. Regulation of intracellular heme levels by Hmx1, a homologue of heme oxygenase, in Saccharomyces cerevisiae. J. Biol. Chem. 278 (2003) 36582-36587
    • (2003) J. Biol. Chem. , vol.278 , pp. 36582-36587
    • Protchenko, O.1    Philpott, C.C.2
  • 34
    • 1842478044 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae glutaredoxin 5-deficient cells subjected to continuous oxidizing conditions are affected in the expression of specific sets of genes
    • Belli G., Molina M.M., Garcia-Martinez J., Perez-Ortin J.E., and Herrero E. Saccharomyces cerevisiae glutaredoxin 5-deficient cells subjected to continuous oxidizing conditions are affected in the expression of specific sets of genes. J. Biol. Chem. 279 (2004) 12386-12395
    • (2004) J. Biol. Chem. , vol.279 , pp. 12386-12395
    • Belli, G.1    Molina, M.M.2    Garcia-Martinez, J.3    Perez-Ortin, J.E.4    Herrero, E.5
  • 35
    • 3142660192 scopus 로고    scopus 로고
    • Sut1-promoted sterol uptake involves the Abc transporter Aus1 and the mannoprotein Dan1 whose synergistic action is sufficient for this process
    • Alimardani P., Regnacq M., Moreau-Vauzelle C., Ferreira T., Rossignol T., Blondin B., and Berges T. Sut1-promoted sterol uptake involves the Abc transporter Aus1 and the mannoprotein Dan1 whose synergistic action is sufficient for this process. Biochem. J. 381 (2004) 195-202
    • (2004) Biochem. J. , vol.381 , pp. 195-202
    • Alimardani, P.1    Regnacq, M.2    Moreau-Vauzelle, C.3    Ferreira, T.4    Rossignol, T.5    Blondin, B.6    Berges, T.7
  • 36
    • 7244238074 scopus 로고    scopus 로고
    • Atp-Binding Cassette (Abc) transporters mediate nonvesicular, raft-modulated sterol movement from the plasma membrane to the endoplasmic reticulum
    • Li Y., and Prinz W.A. Atp-Binding Cassette (Abc) transporters mediate nonvesicular, raft-modulated sterol movement from the plasma membrane to the endoplasmic reticulum. J. Biol. Chem. 279 (2004) 45226-45234
    • (2004) J. Biol. Chem. , vol.279 , pp. 45226-45234
    • Li, Y.1    Prinz, W.A.2
  • 37
    • 11844257593 scopus 로고    scopus 로고
    • Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation
    • Puig S., Askel E., and Thiele D.J. Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation. Cell 120 (2005) 99-110
    • (2005) Cell , vol.120 , pp. 99-110
    • Puig, S.1    Askel, E.2    Thiele, D.J.3
  • 38
    • 0030014654 scopus 로고    scopus 로고
    • Characterization of yeast methyl sterol oxidase (Erg25) and identification of a human homologue
    • Li L., and Kaplan J. Characterization of yeast methyl sterol oxidase (Erg25) and identification of a human homologue. J. Biol. Chem. 271 (1996) 16927-16933
    • (1996) J. Biol. Chem. , vol.271 , pp. 16927-16933
    • Li, L.1    Kaplan, J.2


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