메뉴 건너뛰기




Volumn 23, Issue 18, 2012, Pages 3582-3590

The essential iron-sulfur protein Rli1 is an important target accounting for inhibition of cell growth by reactive oxygen species

Author keywords

[No Author keywords available]

Indexed keywords

IRON SULFUR PROTEIN; PROTEIN RLI1P; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 84866371799     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E12-05-0413     Document Type: Article
Times cited : (64)

References (55)
  • 2
    • 0034748413 scopus 로고    scopus 로고
    • Metal toxicity in yeasts and the role of oxidative stress
    • Avery SV (2001). Metal toxicity in yeasts and the role of oxidative stress. Adv Appl Microbiol 49, 111-142.
    • (2001) Adv Appl Microbiol , vol.49 , pp. 111-142
    • Avery, S.V.1
  • 3
    • 79951518607 scopus 로고    scopus 로고
    • Molecular targets of oxidative stress
    • Avery SV (2011). Molecular targets of oxidative stress. Biochem J 434, 201-210.
    • (2011) Biochem J , vol.434 , pp. 201-210
    • Avery, S.V.1
  • 4
    • 0029848731 scopus 로고    scopus 로고
    • Copper toxicity towards Saccharomyces cerevisiae: Dependence on plasma membrane fatty acid composition
    • Avery SV, Howlett NG, Radice S (1996). Copper toxicity towards Saccharomyces cerevisiae: dependence on plasma membrane fatty acid composition. Appl Environ Microbiol 62, 3960-3966. (Pubitemid 26371490)
    • (1996) Applied and Environmental Microbiology , vol.62 , Issue.11 , pp. 3960-3966
    • Avery, S.V.1    Howlett, N.G.2    Radice, S.3
  • 5
    • 2942565619 scopus 로고    scopus 로고
    • The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins
    • DOI 10.1038/sj.emboj.7600216
    • Balk J, Pierik AJ, Netz DJA, Muhlenhoff U, Lill R (2004). The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins. EMBO J 23, 2105-2115. (Pubitemid 38737737)
    • (2004) EMBO Journal , vol.23 , Issue.10 , pp. 2105-2115
    • Balk, J.1    Pierik, A.J.2    Aguilar, N.D.J.3    Muhlenhoff, U.4    Lill, R.5
  • 6
    • 79952750280 scopus 로고    scopus 로고
    • Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1
    • Barthelme D, Dinkelaker S, Albers SV, Londei P, Ermler U, Tampe R (2011). Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1. Proc Natl Acad Sci USA 108, 3228-3233.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 3228-3233
    • Barthelme, D.1    Dinkelaker, S.2    Albers, S.V.3    Londei, P.4    Ermler, U.5    Tampe, R.6
  • 8
    • 84857396073 scopus 로고    scopus 로고
    • Structural basis of highly conserved ribosome recycling in eukaryotes and archaea
    • Becker T et al. (2012). Structural basis of highly conserved ribosome recycling in eukaryotes and archaea. Nature 482, 501-508.
    • (2012) Nature , vol.482 , pp. 501-508
    • Becker, T.1
  • 10
    • 21244466032 scopus 로고    scopus 로고
    • A chaperone pathway in protein disaggregation: HSP26 alteks the nature of protein aggregates to facilitate reactivation by HSP104
    • DOI 10.1074/jbc.M502854200
    • Cashikar AG, Duennwald M, Lindquist SL (2005). A chaperone pathway in protein disaggregation - Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J Biol Chem 280, 23869-23875. (Pubitemid 40884874)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 23869-23875
    • Cashikar, A.G.1    Duennwald, M.2    Lindquist, S.L.3
  • 11
  • 12
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems, and apoptosis
    • Circu ML, Aw TY (2010). Reactive oxygen species, cellular redox systems, and apoptosis. Free Rad Biol Med 48, 749-762.
    • (2010) Free Rad Biol Med , vol.48 , pp. 749-762
    • Circu, M.L.1    Aw, T.Y.2
  • 13
    • 84855352363 scopus 로고    scopus 로고
    • Death by protein damage in irradiated cells
    • Daly MJ (2012). Death by protein damage in irradiated cells. DNA Repair 11, 12-21.
    • (2012) DNA Repair , vol.11 , pp. 12-21
    • Daly, M.J.1
  • 14
    • 4744350877 scopus 로고    scopus 로고
    • The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly
    • DOI 10.1074/jbc.M404502200
    • Dong JS, Lai R, Nielsen K, Fekete CA, Qiu HF, Hinnebusch AG (2004). The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly. J Biol Chem 279, 42157-42168. (Pubitemid 39313665)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.40 , pp. 42157-42168
    • Dong, J.1    Lai, R.2    Nielsen, K.3    Fekete, C.A.4    Qiu, H.5    Hinnebusch, A.G.6
  • 15
    • 79957992260 scopus 로고    scopus 로고
    • Peroxide stress elicits adaptive changes in bacterial metal ion homeostasis
    • Faulkner MJ, Helmann JD (2011). Peroxide stress elicits adaptive changes in bacterial metal ion homeostasis. Antiox Redox Signal 15, 175-189.
    • (2011) Antiox Redox Signal , vol.15 , pp. 175-189
    • Faulkner, M.J.1    Helmann, J.D.2
  • 16
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • Flint DH, Tuminello JF, Emptage MH (1993). The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J Biol Chem 268, 22369-22376. (Pubitemid 23318282)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.30 , pp. 22369-22376
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.H.3
  • 17
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • DOI 10.1016/S0076-6879(02)50957-5
    • Gietz RD, Woods RA (2002). Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method. Methods Enzymol 350, 87-96. (Pubitemid 34619485)
    • (2002) Methods in Enzymology , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 18
    • 84863027436 scopus 로고    scopus 로고
    • Heterogeneous expression of the virulence-related adhesin Epa1 between individual cells and strains of the pathogen Candida glabrata
    • Halliwell SC, Smith MCA, Muston P, Holland SL, Avery SV (2012). Heterogeneous expression of the virulence-related adhesin Epa1 between individual cells and strains of the pathogen Candida glabrata. Eukaryot Cell 11, 141-150.
    • (2012) Eukaryot Cell , vol.11 , pp. 141-150
    • Halliwell, S.C.1    Smith, M.C.A.2    Muston, P.3    Holland, S.L.4    Avery, S.V.5
  • 19
    • 84856812987 scopus 로고    scopus 로고
    • The role of ABC transporters in progression and clinical outcome of colorectal cancer
    • Hlavata I et al. (2012). The role of ABC transporters in progression and clinical outcome of colorectal cancer. Mutagenesis 27, 187-196.
    • (2012) Mutagenesis , vol.27 , pp. 187-196
    • Hlavata, I.1
  • 21
    • 33645065589 scopus 로고    scopus 로고
    • Iron-sulphur clusters and the problem with oxygen
    • Imlay JA (2006). Iron-sulphur clusters and the problem with oxygen. Mol Microbiol 59, 1073-1082.
    • (2006) Mol Microbiol , vol.59 , pp. 1073-1082
    • Imlay, J.A.1
  • 22
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay JA (2008). Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem 77, 755-776.
    • (2008) Annu Rev Biochem , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 23
    • 33744960105 scopus 로고    scopus 로고
    • Manganese is the link between frataxin and iron-sulfur deficiency in the yeast model of Friedreich ataxia
    • DOI 10.1074/jbc.M511649200
    • Irazusta V, Cabiscol E, Reverter-Branchat G, Ros J, Tamarit J (2006). Manganese is the link between frataxin and iron-sulfur deficiency in the yeast model of Friedreich ataxia. J Biol Chem 281, 12227-12232. (Pubitemid 43855305)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , pp. 12227-12232
    • Irazusta, V.1    Cabiscol, E.2    Reverter-Branchat, G.3    Ros, J.4    Tamarit, J.5
  • 24
    • 78649983777 scopus 로고    scopus 로고
    • Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate
    • Jang SJ, Imlay JA (2010). Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate. Mol Microbiol 78, 1448-1467.
    • (2010) Mol Microbiol , vol.78 , pp. 1448-1467
    • Jang, S.J.1    Imlay, J.A.2
  • 25
    • 43149119755 scopus 로고    scopus 로고
    • X-ray structure of the complete ABC enzyme ABCE1 from Pyrococcus abyssi
    • Karcher A, Schele A, Hopfner KP (2008). X-ray structure of the complete ABC enzyme ABCE1 from Pyrococcus abyssi. J Biol Chem 283, 7962-7971.
    • (2008) J Biol Chem , vol.283 , pp. 7962-7971
    • Karcher, A.1    Schele, A.2    Hopfner, K.P.3
  • 27
    • 77649240878 scopus 로고    scopus 로고
    • The iron-sulphur protein RNase L inhibitor functions in translation termination
    • Khoshnevis S, Gross T, Rotte C, Baierlein C, Ficner R, Krebber H (2010). The iron-sulphur protein RNase L inhibitor functions in translation termination. EMBO Rep 11, 214-219.
    • (2010) EMBO Rep , vol.11 , pp. 214-219
    • Khoshnevis, S.1    Gross, T.2    Rotte, C.3    Baierlein, C.4    Ficner, R.5    Krebber, H.6
  • 28
    • 67650547020 scopus 로고    scopus 로고
    • The antimalarial drug quinine disrupts Tat2p-mediated tryptophan transport and causes tryptophan starvation
    • Khozoie C, Pleass RJ, Avery SV (2009). The antimalarial drug quinine disrupts Tat2p-mediated tryptophan transport and causes tryptophan starvation. J Biol Chem 284, 17968-17974.
    • (2009) J Biol Chem , vol.284 , pp. 17968-17974
    • Khozoie, C.1    Pleass, R.J.2    Avery, S.V.3
  • 29
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • DOI 10.1093/emboj/18.14.3981
    • Kispal G, Csere P, Prohl C, Lill R (1999). The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J 18, 3981-3989. (Pubitemid 29335851)
    • (1999) EMBO Journal , vol.18 , Issue.14 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 31
    • 34548492954 scopus 로고    scopus 로고
    • An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis
    • DOI 10.1038/nsmb1288, PII NSMB1288
    • Klinge S, Hirst J, Maman JD, Krude T, Pellegrini L (2007). An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis. Nat Struct Mol Biol 14, 875-877. (Pubitemid 47373835)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.9 , pp. 875-877
    • Klinge, S.1    Hirst, J.2    Maman, J.D.3    Krude, T.4    Pellegrini, L.5
  • 32
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill R (2009). Function and biogenesis of iron-sulphur proteins. Nature 460, 831-838.
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 33
    • 61649088812 scopus 로고    scopus 로고
    • The role of antioxidants and antioxidant-related enzymes in protective responses to environmentally induced oxidative stress
    • Limon-Pacheco J, Gonsebatt ME (2009). The role of antioxidants and antioxidant-related enzymes in protective responses to environmentally induced oxidative stress. Mutat Res 674, 137-147.
    • (2009) Mutat Res , vol.674 , pp. 137-147
    • Limon-Pacheco, J.1    Gonsebatt, M.E.2
  • 34
    • 77749239882 scopus 로고    scopus 로고
    • Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site
    • Ling J, Soll D (2010). Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site. Proc Natl Acad Sci USA 107, 4028-4033.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4028-4033
    • Ling, J.1    Soll, D.2
  • 35
    • 0032732998 scopus 로고    scopus 로고
    • Superoxide and iron: Partners in crime
    • DOI 10.1080/152165499307161
    • Liochev SI, Fridovich I (1999). Superoxide and iron: partners in crime. IUBMB Life 48, 157-161. (Pubitemid 29518805)
    • (1999) IUBMB Life , vol.48 , Issue.2 , pp. 157-161
    • Liochev, S.I.1    Fridovich, I.2
  • 36
    • 66249112833 scopus 로고    scopus 로고
    • The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
    • Macomber L, Imlay JA (2009). The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity. Proc Natl Acad Sci USA 106, 8344-8349.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 8344-8349
    • Macomber, L.1    Imlay, J.A.2
  • 38
    • 80053041158 scopus 로고    scopus 로고
    • Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective
    • Moller IM, Rogowska-Wrzesinska A, Rao RSP (2011). Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective. J Proteom 74, 2228-2242.
    • (2011) J Proteom , vol.74 , pp. 2228-2242
    • Moller, I.M.1    Rogowska-Wrzesinska, A.2    Rao, R.S.P.3
  • 40
    • 79955626576 scopus 로고    scopus 로고
    • Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes
    • Pisareva VP, Skabkin MA, Hellen CUT, Pestova TV, Pisarev AV (2011). Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes. EMBO J 30, 1804-1817.
    • (2011) EMBO J , vol.30 , pp. 1804-1817
    • Pisareva, V.P.1    Skabkin, M.A.2    Hellen, C.U.T.3    Pestova, T.V.4    Pisarev, A.V.5
  • 42
    • 79954617423 scopus 로고    scopus 로고
    • Fe-S clusters, fragile sentinels of the cell
    • Py B, Moreau PL, Barras F (2011). Fe-S clusters, fragile sentinels of the cell. Curr Opin Microbiol 14, 218-223.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 218-223
    • Py, B.1    Moreau, P.L.2    Barras, F.3
  • 43
    • 84863061003 scopus 로고    scopus 로고
    • Role of the ABCE1 gene in human lung adenocarcinoma
    • Ren Y, Li Y, Tian D (2012). Role of the ABCE1 gene in human lung adenocarcinoma. Oncol Rep 27, 965-970.
    • (2012) Oncol Rep , vol.27 , pp. 965-970
    • Ren, Y.1    Li, Y.2    Tian, D.3
  • 45
    • 33748428875 scopus 로고    scopus 로고
    • The DNA Repair Helicases XPD and FancJ Have Essential Iron-Sulfur Domains
    • DOI 10.1016/j.molcel.2006.07.019, PII S1097276506005168
    • Rudolf J, Makrantoni V, Ingledew WJ, Stark MJR, White MF (2006). The DNA repair helicases XPD and FancJ have essential iron-sulfur domains. Mol Cell 23, 801-808. (Pubitemid 44344515)
    • (2006) Molecular Cell , vol.23 , Issue.6 , pp. 801-808
    • Rudolf, J.1    Makrantoni, V.2    Ingledew, W.J.3    Stark, M.J.R.4    White, M.F.5
  • 47
    • 84855501083 scopus 로고    scopus 로고
    • Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast
    • Shoemaker CJ, Green R (2011). Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast. Proc Natl Acad Sci USA 108, E1392-E1398.
    • (2011) Proc Natl Acad Sci USA , vol.108
    • Shoemaker, C.J.1    Green, R.2
  • 48
    • 62249136392 scopus 로고    scopus 로고
    • Methionine sulphoxide reductases protect iron-sulphur clusters from oxidative inactivation in yeast
    • Sideri TC, Willetts SA, Avery SV (2009). Methionine sulphoxide reductases protect iron-sulphur clusters from oxidative inactivation in yeast. Microbiol 155, 612-623.
    • (2009) Microbiol , vol.155 , pp. 612-623
    • Sideri, T.C.1    Willetts, S.A.2    Avery, S.V.3
  • 49
    • 0242437869 scopus 로고    scopus 로고
    • Cell cycle- and age-dependent activation of Sod1p drives the formation of stress resistant cell subpopulations within clonal yeast cultures
    • DOI 10.1046/j.1365-2958.2003.03715.x
    • Sumner ER, Avery AM, Houghton JE, Robins RA, Avery SV (2003). Cell cycle- and age-dependent activation of Sod1p drives the formation of stress resistant cell subpopulations within clonal yeast cultures. Mol Microbiol 50, 857-870. (Pubitemid 37372249)
    • (2003) Molecular Microbiology , vol.50 , Issue.3 , pp. 857-870
    • Sumner, E.R.1    Avery, A.M.2    Houghton, J.E.3    Robins, R.A.4    Avery, S.V.5
  • 52
    • 0037214441 scopus 로고    scopus 로고
    • Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion
    • DOI 10.1128/JB.185.1.221-230.2003
    • Varghese S, Tang Y, Imlay JA (2003). Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion. J Bacteriol 185, 221-230. (Pubitemid 36008840)
    • (2003) Journal of Bacteriology , vol.185 , Issue.1 , pp. 221-230
    • Varghese, S.1    Tang, Y.2    Imlay, J.A.3
  • 53
    • 0030840519 scopus 로고    scopus 로고
    • Heterologous HIS3 marker and GFP reporter modules for PCR-targeting in Saccharomyces cerevisiae
    • DOI 10.1002/(SICI)1097-0061(19970915)13:11<1065::AID-YEA159>3.0. CO;2-K
    • Wach A, Brachat A, AlbertiSegui C, Rebischung C, Philippsen P (1997). Heterologous HIS3 marker and GFP reporter modules for PCR-targeting in Saccharomyces cerevisiae. Yeast 13, 1065-1075. (Pubitemid 27368517)
    • (1997) Yeast , vol.13 , Issue.11 , pp. 1065-1075
    • Wach, A.1    Brachat, A.2    Alberti-Segui, C.3    Rebischung, C.4    Philippsen, P.5
  • 54
    • 14744301484 scopus 로고    scopus 로고
    • Functional link between ribosome formation and biogenesis of iron-sulfur proteins
    • DOI 10.1038/sj.emboj.7600540
    • Yarunin A, Panse VG, Petfalski E, Dez C, Tollervey D, Hurt EC (2005). Functional link between ribosome formation and biogenesis of iron-sulfur proteins. EMBO J 24, 580-588. (Pubitemid 40343259)
    • (2005) EMBO Journal , vol.24 , Issue.3 , pp. 580-588
    • Yarunin, A.1    Panse, V.G.2    Petfalski, E.3    Dez, C.4    Tollervey, D.5    Hurt, E.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.