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Volumn 1833, Issue 12, 2013, Pages 3326-3337

Metabolic remodeling in frataxin-deficient yeast is mediated by Cth2 and Adr1

Author keywords

Friedreich ataxia; Iron; Oxidative stress; Yeast frataxin

Indexed keywords

ACONITATE HYDRATASE; ALCOHOL DEHYDROGENASE; CTH2 PROTEIN; FRATAXIN; HYDROGEN PEROXIDE; IRON REGULATORY PROTEIN 1; MESSENGER RNA; RNA BINDING PROTEIN; SUCCINATE DEHYDROGENASE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ADR1; UNCLASSIFIED DRUG; YEAST FRATAXIN HOMOLOGUE PROTEIN;

EID: 84886406190     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.09.019     Document Type: Article
Times cited : (18)

References (45)
  • 1
    • 62549117369 scopus 로고    scopus 로고
    • Friedreich ataxia: the clinical picture
    • Pandolfo M. Friedreich ataxia: the clinical picture. J. Neurol. 2009, 256(Suppl. 1):3-8.
    • (2009) J. Neurol. , vol.256 , Issue.SUPPL. 1 , pp. 3-8
    • Pandolfo, M.1
  • 3
    • 79551514731 scopus 로고    scopus 로고
    • Mammalian frataxin: an essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex
    • Schmucker S., Martelli A., Colin F., Page A., Wattenhofer-Donze M., Reutenauer L., Puccio H. Mammalian frataxin: an essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex. PLoS One 2011, 6:e16199.
    • (2011) PLoS One , vol.6
    • Schmucker, S.1    Martelli, A.2    Colin, F.3    Page, A.4    Wattenhofer-Donze, M.5    Reutenauer, L.6    Puccio, H.7
  • 4
    • 38649103446 scopus 로고    scopus 로고
    • Hydrogen peroxide scavenging rescues frataxin deficiency in a Drosophila model of Friedreich's ataxia
    • Anderson P.R., Kirby K., Orr W.C., Hilliker A.J., Phillips J.P. Hydrogen peroxide scavenging rescues frataxin deficiency in a Drosophila model of Friedreich's ataxia. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:611-616.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 611-616
    • Anderson, P.R.1    Kirby, K.2    Orr, W.C.3    Hilliker, A.J.4    Phillips, J.P.5
  • 5
    • 78650671292 scopus 로고    scopus 로고
    • Frataxin depletion in yeast triggers up-regulation of iron transport systems before affecting iron-sulfur enzyme activities
    • Moreno-Cermeno A., Obis E., Belli G., Cabiscol E., Ros J., Tamarit J. Frataxin depletion in yeast triggers up-regulation of iron transport systems before affecting iron-sulfur enzyme activities. J. Biol. Chem. 2010, 285:41653-41664.
    • (2010) J. Biol. Chem. , vol.285 , pp. 41653-41664
    • Moreno-Cermeno, A.1    Obis, E.2    Belli, G.3    Cabiscol, E.4    Ros, J.5    Tamarit, J.6
  • 7
    • 84859178535 scopus 로고    scopus 로고
    • Effector role reversal during evolution: the case of frataxin in Fe-S cluster biosynthesis
    • Bridwell-Rabb J., Iannuzzi C., Pastore A., Barondeau D.P. Effector role reversal during evolution: the case of frataxin in Fe-S cluster biosynthesis. Biochemistry 2012, 51:92506-92514.
    • (2012) Biochemistry , vol.51 , pp. 92506-92514
    • Bridwell-Rabb, J.1    Iannuzzi, C.2    Pastore, A.3    Barondeau, D.P.4
  • 8
    • 42449093713 scopus 로고    scopus 로고
    • Structural basis of the iron storage function of frataxin from single-particle reconstruction of the iron-loaded oligomer
    • Schagerlof U., Elmlund H., Gakh O., Nordlund G., Hebert H., Lindahl M., Isaya G., Al-Karadaghi S. Structural basis of the iron storage function of frataxin from single-particle reconstruction of the iron-loaded oligomer. Biochemistry 2008, 47:4948-4954.
    • (2008) Biochemistry , vol.47 , pp. 4948-4954
    • Schagerlof, U.1    Elmlund, H.2    Gakh, O.3    Nordlund, G.4    Hebert, H.5    Lindahl, M.6    Isaya, G.7    Al-Karadaghi, S.8
  • 10
    • 77952480112 scopus 로고    scopus 로고
    • Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin
    • Condo I., Malisan F., Guccini I., Serio D., Rufini A., Testi R. Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin. Hum. Mol. Genet. 2010, 19:1221-1229.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 1221-1229
    • Condo, I.1    Malisan, F.2    Guccini, I.3    Serio, D.4    Rufini, A.5    Testi, R.6
  • 11
    • 0006339631 scopus 로고
    • Growth and assimilation in cultures of Saccharomyces cerevisiae
    • Swanson W.H., Clifton C.E. Growth and assimilation in cultures of Saccharomyces cerevisiae. J. Bacteriol. 1948, 56:115-124.
    • (1948) J. Bacteriol. , vol.56 , pp. 115-124
    • Swanson, W.H.1    Clifton, C.E.2
  • 12
    • 55249118618 scopus 로고    scopus 로고
    • Mitochondrial oxidative phosphorylation is regulated by fructose 1,6-bisphosphate. A possible role in Crabtree effect induction?
    • Diaz-Ruiz R., Averet N., Araiza D., Pinson B., Uribe-Carvajal S., Devin A., Rigoulet M. Mitochondrial oxidative phosphorylation is regulated by fructose 1,6-bisphosphate. A possible role in Crabtree effect induction?. J. Biol. Chem. 2008, 283:26948-26955.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26948-26955
    • Diaz-Ruiz, R.1    Averet, N.2    Araiza, D.3    Pinson, B.4    Uribe-Carvajal, S.5    Devin, A.6    Rigoulet, M.7
  • 16
    • 44349183685 scopus 로고    scopus 로고
    • Cooperation of two mRNA-binding proteins drives metabolic adaptation to iron deficiency
    • Puig S., Vergara S.V., Thiele D.J. Cooperation of two mRNA-binding proteins drives metabolic adaptation to iron deficiency. Cell Metab. 2008, 7:555-564.
    • (2008) Cell Metab. , vol.7 , pp. 555-564
    • Puig, S.1    Vergara, S.V.2    Thiele, D.J.3
  • 18
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • Rodríguez-Manzaneque M.T., Tamarit J., Bellí G., Ros J., Herrero E. Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol. Biol. Cell 2002, 13:1109-1121.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1109-1121
    • Rodríguez-Manzaneque, M.T.1    Tamarit, J.2    Bellí, G.3    Ros, J.4    Herrero, E.5
  • 19
    • 6344278689 scopus 로고    scopus 로고
    • Characterization of the calcium-mediated response to alkaline stress in Saccharomyces cerevisiae
    • Viladevall L., Serrano R., Ruiz A., Domenech G., Giraldo J., Barcelo A., Arino J. Characterization of the calcium-mediated response to alkaline stress in Saccharomyces cerevisiae. J. Biol. Chem. 2004, 279:43614-43624.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43614-43624
    • Viladevall, L.1    Serrano, R.2    Ruiz, A.3    Domenech, G.4    Giraldo, J.5    Barcelo, A.6    Arino, J.7
  • 20
    • 85077257460 scopus 로고    scopus 로고
    • Relative quantification
    • Taylor and Francis Group, New York, T. Dorak (Ed.)
    • Pfaffl M.W. Relative quantification. Real-time PCR 2006, 63-82. Taylor and Francis Group, New York. T. Dorak (Ed.).
    • (2006) Real-time PCR , pp. 63-82
    • Pfaffl, M.W.1
  • 23
    • 0027324683 scopus 로고
    • Detection of c-type cytochromes using enhanced chemiluminescence
    • Vargas C., McEwan A.G., Downie J.A. Detection of c-type cytochromes using enhanced chemiluminescence. Anal. Biochem. 1993, 209:323-326.
    • (1993) Anal. Biochem. , vol.209 , pp. 323-326
    • Vargas, C.1    McEwan, A.G.2    Downie, J.A.3
  • 24
    • 0033613163 scopus 로고    scopus 로고
    • Friedreich's ataxia is a mitochondrial disorder
    • Kaplan J. Friedreich's ataxia is a mitochondrial disorder. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:10948-10949.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10948-10949
    • Kaplan, J.1
  • 25
    • 54049146291 scopus 로고    scopus 로고
    • The alcohol dehydrogenases of Saccharomyces cerevisiae: a comprehensive review
    • de Smidt O., du Preez J.C., Albertyn J. The alcohol dehydrogenases of Saccharomyces cerevisiae: a comprehensive review. FEMS Yeast Res. 2008, 8:967-978.
    • (2008) FEMS Yeast Res. , vol.8 , pp. 967-978
    • De Smidt, O.1    Du Preez, J.C.2    Albertyn, J.3
  • 26
    • 36448968951 scopus 로고    scopus 로고
    • Chronological and replicative life-span extension in Saccharomyces cerevisiae by increased dosage of alcohol dehydrogenase 1
    • Reverter-Branchat G., Cabiscol E., Tamarit J., Sorolla M.A., Angeles de la Torre M., Ros J. Chronological and replicative life-span extension in Saccharomyces cerevisiae by increased dosage of alcohol dehydrogenase 1. Microbiology 2007, 153:3667-3676.
    • (2007) Microbiology , vol.153 , pp. 3667-3676
    • Reverter-Branchat, G.1    Cabiscol, E.2    Tamarit, J.3    Sorolla, M.A.4    Angeles de la Torre, M.5    Ros, J.6
  • 27
    • 33744960105 scopus 로고    scopus 로고
    • Manganese is the link between frataxin and iron-sulfur deficiency in the yeast model of Friedreich ataxia
    • Irazusta V., Cabiscol E., Reverter-Branchat G., Ros J., Tamarit J. Manganese is the link between frataxin and iron-sulfur deficiency in the yeast model of Friedreich ataxia. J. Biol. Chem. 2006, 281:12227-12232.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12227-12232
    • Irazusta, V.1    Cabiscol, E.2    Reverter-Branchat, G.3    Ros, J.4    Tamarit, J.5
  • 28
    • 73449091792 scopus 로고    scopus 로고
    • Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage
    • Irazusta V., Obis E., Moreno-Cermeno A., Cabiscol E., Ros J., Tamarit J. Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage. Free Radic. Biol. Med. 2010, 48:411-420.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 411-420
    • Irazusta, V.1    Obis, E.2    Moreno-Cermeno, A.3    Cabiscol, E.4    Ros, J.5    Tamarit, J.6
  • 29
    • 0038506725 scopus 로고    scopus 로고
    • Multiple pathways are co-regulated by the protein kinase Snf1 and the transcription factors Adr1 and Cat8
    • Young E.T., Dombek K.M., Tachibana C., Ideker T. Multiple pathways are co-regulated by the protein kinase Snf1 and the transcription factors Adr1 and Cat8. J. Biol. Chem. 2003, 278:26146-26158.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26146-26158
    • Young, E.T.1    Dombek, K.M.2    Tachibana, C.3    Ideker, T.4
  • 30
    • 74549132460 scopus 로고    scopus 로고
    • Transcriptional regulation of nonfermentable carbon utilization in budding yeast
    • Turcotte B., Liang X.B., Robert F., Soontorngun N. Transcriptional regulation of nonfermentable carbon utilization in budding yeast. FEMS Yeast Res. 2010, 10:2-13.
    • (2010) FEMS Yeast Res. , vol.10 , pp. 2-13
    • Turcotte, B.1    Liang, X.B.2    Robert, F.3    Soontorngun, N.4
  • 31
    • 70349310032 scopus 로고    scopus 로고
    • Snf1 controls the activity of adr1 through dephosphorylation of Ser230
    • Ratnakumar S., Kacherovsky N., Arms E., Young E.T. Snf1 controls the activity of adr1 through dephosphorylation of Ser230. Genetics 2009, 182:735-745.
    • (2009) Genetics , vol.182 , pp. 735-745
    • Ratnakumar, S.1    Kacherovsky, N.2    Arms, E.3    Young, E.T.4
  • 32
    • 78649598716 scopus 로고    scopus 로고
    • 14-3-3 (Bmh) proteins inhibit transcription activation by Adr1 through direct binding to its regulatory domain
    • Parua P.K., Ratnakumar S., Braun K.A., Dombek K.M., Arms E., Ryan P.M., Young E.T. 14-3-3 (Bmh) proteins inhibit transcription activation by Adr1 through direct binding to its regulatory domain. Mol. Cell. Biol. 2010, 30:5273-5283.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 5273-5283
    • Parua, P.K.1    Ratnakumar, S.2    Braun, K.A.3    Dombek, K.M.4    Arms, E.5    Ryan, P.M.6    Young, E.T.7
  • 36
    • 16844368767 scopus 로고    scopus 로고
    • Pkc1 and the upstream elements of the cell integrity pathway in Saccharomyces
    • Vilella F., Herrero E., Torres J., de la Torre-Ruiz M.A. Pkc1 and the upstream elements of the cell integrity pathway in Saccharomyces. J. Biol. Chem. 2005, 280:9149-9159.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9149-9159
    • Vilella, F.1    Herrero, E.2    Torres, J.3    de la Torre-Ruiz, M.A.4
  • 38
    • 0034597012 scopus 로고    scopus 로고
    • 2 sensing through oxidation of the Yap1 transcription factor
    • 2 sensing through oxidation of the Yap1 transcription factor. EMBO J. 2000, 19:5157-5166.
    • (2000) EMBO J. , vol.19 , pp. 5157-5166
    • Delaunay, A.1    Isnard, A.D.2    Toledano, M.B.3
  • 39
    • 0034282468 scopus 로고    scopus 로고
    • Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae
    • Cabiscol E., Piulats E., Echave P., Herrero E., Ros J. Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. J. Biol. Chem. 2000, 275:27393-27398.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27393-27398
    • Cabiscol, E.1    Piulats, E.2    Echave, P.3    Herrero, E.4    Ros, J.5
  • 40
    • 84878981799 scopus 로고    scopus 로고
    • Negative feedback regulation of the yeast CTH1 and CTH2 mRNA binding proteins is required for adaptation to iron deficiency and iron supplementation
    • Martínez-Pastor M., Vergara S.V., Puig S., Thiele D.J. Negative feedback regulation of the yeast CTH1 and CTH2 mRNA binding proteins is required for adaptation to iron deficiency and iron supplementation. Mol. Cell. Biol. 2013, 33:2178-2187.
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 2178-2187
    • Martínez-Pastor, M.1    Vergara, S.V.2    Puig, S.3    Thiele, D.J.4
  • 41
    • 84871168299 scopus 로고    scopus 로고
    • Cells Lacking Pfh1, a fission yeast homolog of mammalian frataxin, display constitutive activation of the iron starvation response
    • Gabrielli N., Ayte J., Hidalgo E. Cells Lacking Pfh1, a fission yeast homolog of mammalian frataxin, display constitutive activation of the iron starvation response. J. Biol. Chem. 2012, 287:43042-43051.
    • (2012) J. Biol. Chem. , vol.287 , pp. 43042-43051
    • Gabrielli, N.1    Ayte, J.2    Hidalgo, E.3
  • 42
    • 82155178623 scopus 로고    scopus 로고
    • Iron regulatory protein-1 and -2: transcriptome-wide definition of binding mRNAs and shaping of the cellular proteome by iron regulatory proteins
    • Sanchez M., Galy B., Schwanhaeusser B., Blake J., Bahr-Ivacevic T., Benes V., Selbach M., Muckenthaler M.U., Hentze M.W. Iron regulatory protein-1 and -2: transcriptome-wide definition of binding mRNAs and shaping of the cellular proteome by iron regulatory proteins. Blood 2011, 118:168-179.
    • (2011) Blood , vol.118 , pp. 168-179
    • Sanchez, M.1    Galy, B.2    Schwanhaeusser, B.3    Blake, J.4    Bahr-Ivacevic, T.5    Benes, V.6    Selbach, M.7    Muckenthaler, M.U.8    Hentze, M.W.9
  • 44
    • 14844316642 scopus 로고    scopus 로고
    • Yeast flavohemoglobin, a nitric oxide oxidoreductase, is located in both the cytosol and the mitochondrial matrix: effects of respiration, anoxia, and the mitochondrial genome on its intracellular level and distribution
    • Cassanova N., O'Brien K.M., Stahl B.T., McClure T., Poyton R.O. Yeast flavohemoglobin, a nitric oxide oxidoreductase, is located in both the cytosol and the mitochondrial matrix: effects of respiration, anoxia, and the mitochondrial genome on its intracellular level and distribution. J. Biol. Chem. 2005, 280:7645-7653.
    • (2005) J. Biol. Chem. , vol.280 , pp. 7645-7653
    • Cassanova, N.1    O'Brien, K.M.2    Stahl, B.T.3    McClure, T.4    Poyton, R.O.5
  • 45
    • 25144499969 scopus 로고    scopus 로고
    • Gene expression profiling and phenotype analyses of S. cerevisiae in response to changing copper reveals six genes with new roles in copper and iron metabolism
    • van Bakel H., Strengman E., Wijmenga C., Holstege F.C. Gene expression profiling and phenotype analyses of S. cerevisiae in response to changing copper reveals six genes with new roles in copper and iron metabolism. Physiol. Genomics 2005, 22:356-367.
    • (2005) Physiol. Genomics , vol.22 , pp. 356-367
    • van Bakel, H.1    Strengman, E.2    Wijmenga, C.3    Holstege, F.C.4


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