메뉴 건너뛰기




Volumn 9, Issue 2, 2010, Pages 730-736

Oxidative stress studies in yeast with a frataxin mutant: A proteomics perspective

Author keywords

Cell viability; Frataxin; Friedreich ataxia; Oxidative stress; Protein damage

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; ALCOHOL DEHYDROGENASE; CARBONYL DERIVATIVE; CCHI PROTEIN; CFD1 PROTEIN; DNA TOPOISOMERASE (ATP HYDROLYSING); ELONGATION FACTOR 1ALPHA; ENOLASE; ENOLASE II PROTEIN; FRATAXIN; FRUCTOSE BISPHOSPHATE ALDOLASE; GLUTAMATE DEHYDROGENASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GUANOSINE DIPHOSPHATE MANNOSE; HEAT SHOCK PROTEIN 26; HYDROGEN PEROXIDE; IRON; KHELLIN; MINICHROMOSOME MAINTENANCE PROTEIN 2; PDCI PROTEIN; PEPTIDE FRAGMENT; PSAI PROTEIN; REACTIVE OXYGEN METABOLITE; RPLI4A PROTEIN; SPERMIDINE SYNTHASE; TRANSLATIONAL ELONGATION FACTOR 2 PROTEIN; TRX2 PROTEIN; TRYPSIN; UNCLASSIFIED DRUG; VPS13 PROTEIN;

EID: 76149118103     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr900538e     Document Type: Article
Times cited : (21)

References (31)
  • 6
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman, E. R.; Berlett, B. S. Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol. 1997, 10 (5), 485-494.
    • (1997) Chem. Res. Toxicol , vol.10 , Issue.5 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 7
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich, I. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 1995, 64, 97-112.
    • (1995) Annu. Rev. Biochem , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 9
    • 18544384019 scopus 로고
    • Oxidation of tartaric acid in presence of iron
    • Fenton, H. J. H. Oxidation of tartaric acid in presence of iron. J. Chem. Soc., Trans. 1894, 65, 899-910.
    • (1894) J. Chem. Soc., Trans , vol.65 , pp. 899-910
    • Fenton, H.J.H.1
  • 10
    • 0000162325 scopus 로고
    • The catalytic decomposition of hydrogen peroxide by iron salts
    • Haber, F.; Weiss, J. The catalytic decomposition of hydrogen peroxide by iron salts. Proc. R. Soc. London, Ser. A 1934, 147, 332-351.
    • (1934) Proc. R. Soc. London, Ser. A , vol.147 , pp. 332-351
    • Haber, F.1    Weiss, J.2
  • 12
    • 0037447390 scopus 로고    scopus 로고
    • Iron use for haeme synthesis is under control of the yeast frataxin homologue (Yfh1)
    • Lesuisse, E.; Santos, R.; Matzanke, B. F.; Knight, S. A.; Camadro, J. M.; Dancis, A. Iron use for haeme synthesis is under control of the yeast frataxin homologue (Yfh1). Hum. Mol. Genet. 2003, 12 (8), 879-889.
    • (2003) Hum. Mol. Genet , vol.12 , Issue.8 , pp. 879-889
    • Lesuisse, E.1    Santos, R.2    Matzanke, B.F.3    Knight, S.A.4    Camadro, J.M.5    Dancis, A.6
  • 13
    • 0037101845 scopus 로고    scopus 로고
    • The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins
    • Mühlenhoff, U.; Richhardt, N.; Ristow, M.; Kispal, G.; Lill, R. The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins. Hum. Mol. Genet. 2002, 11 (17), 2025-2036.
    • (2002) Hum. Mol. Genet , vol.11 , Issue.17 , pp. 2025-2036
    • Mühlenhoff, U.1    Richhardt, N.2    Ristow, M.3    Kispal, G.4    Lill, R.5
  • 14
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
    • 9
    • Gerber, J.; Mühlenhoff, U.; Lill, R. An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1. EMBO Rep. 2003, 4 (9), 906-911.
    • (2003) EMBO Rep , vol.4 , pp. 906-911
    • Gerber, J.1    Mühlenhoff, U.2    Lill, R.3
  • 15
    • 0036799372 scopus 로고    scopus 로고
    • A nonessential function for yeast frataxin in iron-sulfur cluster assembly
    • Duby, G.; Foury, F.; Ramazzotti, A.; Herrmann, J.; Lutz, T. A nonessential function for yeast frataxin in iron-sulfur cluster assembly. Hum. Mol. Genet. 2002, 11 (21), 2635-2643.
    • (2002) Hum. Mol. Genet , vol.11 , Issue.21 , pp. 2635-2643
    • Duby, G.1    Foury, F.2    Ramazzotti, A.3    Herrmann, J.4    Lutz, T.5
  • 16
    • 0033838364 scopus 로고    scopus 로고
    • Iron-Dependent self-assembly of recombinant yeast frataxin: Implications for Friedreich Ataxia
    • Adamec, J.; Rusnak, F.; Owen, W. G.; Naylor, S.; Benson, L. M.; Gacy, A. M.; Isaya, G. Iron-Dependent self-assembly of recombinant yeast frataxin: Implications for Friedreich Ataxia. Am. J. Hum. Genet. 2000, 67 (3), 549-562.
    • (2000) Am. J. Hum. Genet , vol.67 , Issue.3 , pp. 549-562
    • Adamec, J.1    Rusnak, F.2    Owen, W.G.3    Naylor, S.4    Benson, L.M.5    Gacy, A.M.6    Isaya, G.7
  • 17
    • 0031567601 scopus 로고    scopus 로고
    • Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria
    • Foury, F.; Cazzalini, O. Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria. FEBS Lett. 1997, 411 (2-3), 373-377.
    • (1997) FEBS Lett , vol.411 , Issue.2-3 , pp. 373-377
    • Foury, F.1    Cazzalini, O.2
  • 19
    • 0037341611 scopus 로고    scopus 로고
    • Short telomeres induce a DNA damage response in Saccharomyces cerevisiae
    • IJpma, A. S.; Greider, C. W. Short telomeres induce a DNA damage response in Saccharomyces cerevisiae. Mol. Biol. Cell 2003, 14 (3), 987-1001.
    • (2003) Mol. Biol. Cell , vol.14 , Issue.3 , pp. 987-1001
    • IJpma, A.S.1    Greider, C.W.2
  • 21
    • 23044512070 scopus 로고    scopus 로고
    • Moulder, R.; Filén, J. J.; Salmi, J.; Katajamaa, M.; Nevalainen, O. S.; Oresic, M.; Aittokallio, T.; Lahesmaa, R.; Nyman, T. A. A comparative evaluation of software for the analysis of liquid chromatography-tandem mass spectrometry data from isotope coded affinity tag experiments. Proteomics 2005, 5 (11), 2748-2760.
    • Moulder, R.; Filén, J. J.; Salmi, J.; Katajamaa, M.; Nevalainen, O. S.; Oresic, M.; Aittokallio, T.; Lahesmaa, R.; Nyman, T. A. A comparative evaluation of software for the analysis of liquid chromatography-tandem mass spectrometry data from isotope coded affinity tag experiments. Proteomics 2005, 5 (11), 2748-2760.
  • 22
    • 23944451618 scopus 로고    scopus 로고
    • An evaluation, comparison, and accurate benchmarking of several publicly available MS/MS search algorithms: Sensitivity and specificity analysis
    • Kapp, E. A.; Schutz, F.; Connolly, L. M.; Chakel, J. A.; Meza, J. E.; Miller, C. A.; Fenyo, D.; Eng, J. K.; Adkins, J. N.; Omenn, G. S. An evaluation, comparison, and accurate benchmarking of several publicly available MS/MS search algorithms: sensitivity and specificity analysis. Proteomics 2005, 5 (13), 3475-3490.
    • (2005) Proteomics , vol.5 , Issue.13 , pp. 3475-3490
    • Kapp, E.A.1    Schutz, F.2    Connolly, L.M.3    Chakel, J.A.4    Meza, J.E.5    Miller, C.A.6    Fenyo, D.7    Eng, J.K.8    Adkins, J.N.9    Omenn, G.S.10
  • 23
    • 3042523891 scopus 로고    scopus 로고
    • Proteomic analysis of carbonylated proteins in two-dimensional gel electrophoresis using avidin-fluorescein affinity staining
    • Yoo, B.-S.; Regnier, F. E. Proteomic analysis of carbonylated proteins in two-dimensional gel electrophoresis using avidin-fluorescein affinity staining. Electrophoresis 2004, 25 (9), 1334-1341.
    • (2004) Electrophoresis , vol.25 , Issue.9 , pp. 1334-1341
    • Yoo, B.-S.1    Regnier, F.E.2
  • 24
    • 33644932478 scopus 로고    scopus 로고
    • Yeast oxidative stress response: Influences of cytosolic thioredoxin peroxidase I and of the mitochondrial functional state
    • Demasi, A. P.; Pereira, G. A.; Netto, L. E. Yeast oxidative stress response: influences of cytosolic thioredoxin peroxidase I and of the mitochondrial functional state. FEBS J. 2006, 273 (4), 805-816.
    • (2006) FEBS J , vol.273 , Issue.4 , pp. 805-816
    • Demasi, A.P.1    Pereira, G.A.2    Netto, L.E.3
  • 25
    • 0032502723 scopus 로고    scopus 로고
    • Hydrogen peroxide causes RAD9-dependent cell cycle arrest in G2 in Saccharomyces cerevisiae whereas menadione causes G1 arrest independent of RAD9 function
    • Flattery-O'Brien, J. A.; Dawes, I. W. Hydrogen peroxide causes RAD9-dependent cell cycle arrest in G2 in Saccharomyces cerevisiae whereas menadione causes G1 arrest independent of RAD9 function. J. Biol. Chem. 1998, 273 (15), 8564-8571.
    • (1998) J. Biol. Chem , vol.273 , Issue.15 , pp. 8564-8571
    • Flattery-O'Brien, J.A.1    Dawes, I.W.2
  • 27
    • 41549083260 scopus 로고
    • Major targets of iron-induced protein oxidative damage in frataxin-deficient yeasts are magnesium-binding proteins
    • 2008
    • Irazusta, V.; Moreno-Cermeño, A.; Cabiscol, E.; Ros, J.; Tamarit, J. Major targets of iron-induced protein oxidative damage in frataxin-deficient yeasts are magnesium-binding proteins. Free Radical Biol. Med. 2008, 44 (9), 1712-1723.
    • (1712) Free Radical Biol. Med , vol.44 , Issue.9
    • Irazusta, V.1    Moreno-Cermeño, A.2    Cabiscol, E.3    Ros, J.4    Tamarit, J.5
  • 28
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota, D. A.; Davies, K. J. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat. Cell Biol. 2002, 4 (9), 674-680.
    • (2002) Nat. Cell Biol , vol.4 , Issue.9 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.2
  • 29
    • 4344677922 scopus 로고    scopus 로고
    • Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease
    • Grune, T.; Jung, T.; Merker, K.; Davies, K. J. Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int. J. Biochem. Cell Biol. 2004, 36 (12), 2519-2530.
    • (2004) Int. J. Biochem. Cell Biol , vol.36 , Issue.12 , pp. 2519-2530
    • Grune, T.1    Jung, T.2    Merker, K.3    Davies, K.J.4
  • 30
    • 0037021453 scopus 로고    scopus 로고
    • Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress
    • Bota, D. A.; Van Remmen, H.; Davies, K. J. Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress. FEBS Lett. 2002, 532 (1-2), 103-106.
    • (2002) FEBS Lett , vol.532 , Issue.1-2 , pp. 103-106
    • Bota, D.A.1    Van Remmen, H.2    Davies, K.J.3
  • 31
    • 33846025822 scopus 로고    scopus 로고
    • Identification of yeast oxidized proteins Chromatographic top-down approach for identification of carbonylated, fragmented and cross-linked proteins in yeast
    • Mirzaei, H.; Regnier, F. E. Identification of yeast oxidized proteins Chromatographic top-down approach for identification of carbonylated, fragmented and cross-linked proteins in yeast. J. Chromatogr., A 2007, 1141 (1), 22-31.
    • (2007) J. Chromatogr., A , vol.1141 , Issue.1 , pp. 22-31
    • Mirzaei, H.1    Regnier, F.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.