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Volumn 8, Issue 2, 2013, Pages

Chaperonin 20 might be an iron chaperone for superoxide dismutase in activating iron superoxide dismutase (FeSOD)

Author keywords

Arabidopsis; Chaperonin 20; FeSOD; Iron chaperone; Iron homeostasis; SOD activation

Indexed keywords

ARABIDOPSIS;

EID: 84873546706     PISSN: 15592316     EISSN: 15592324     Source Type: Journal    
DOI: 10.4161/psb.23074     Document Type: Article
Times cited : (13)

References (23)
  • 3
    • 33644798462 scopus 로고    scopus 로고
    • A copper chaperone for superoxide dismutase that confers three types of copper/zinc superoxide dismutase activity in Arabidopsis
    • PMID:16126858
    • Chu CC, Lee WC, Guo WY, Pan SM, Chen LJ, Li HM, et al. A copper chaperone for superoxide dismutase that confers three types of copper/zinc superoxide dismutase activity in Arabidopsis. Plant Physiol 2005; 139:425-436; PMID:16126858; http://dx.doi.org/10.1104/pp.105.065284.
    • (2005) Plant Physiol , vol.139 , pp. 425-436
    • Chu, C.C.1    Lee, W.C.2    Guo, W.Y.3    Pan, S.M.4    Chen, L.J.5    Li, H.M.6
  • 4
    • 17644422168 scopus 로고    scopus 로고
    • AtCCS is a functional homolog of the yeast copper chaperone Ccs1/Lys7
    • PMID:15848163
    • Abdel-Ghany SE, Burkhead JL, Gogolin KA, Andrés-Colás N, Bodecker JR, Puig S, et al. AtCCS is a functional homolog of the yeast copper chaperone Ccs1/Lys7. FEBS Lett 2005; 579:2307-2312; PMID:15848163; http://dx.doi.org/10.1016/j.febslet.2005.03.025.
    • (2005) FEBS Lett , vol.579 , pp. 2307-2312
    • Abdel-Ghany, S.E.1    Burkhead, J.L.2    Gogolin, K.A.3    Andrés-Colás, N.4    Bodecker, J.R.5    Puig, S.6
  • 5
    • 84863082820 scopus 로고    scopus 로고
    • Copper chaperone-dependent and-independent activation of three copper-zinc superoxide dismutase homologs localized in different cellular compartments in Arabidopsis
    • PMID:22186608
    • Huang CH, Kuo WY, Weiss C, Jinn TL. Copper chaperone-dependent and-independent activation of three copper-zinc superoxide dismutase homologs localized in different cellular compartments in Arabidopsis. Plant Physiol 2012; 158:737-746; PMID:22186608; http://dx.doi.org/10.1104/pp.111.190223.
    • (2012) Plant Physiol , vol.158 , pp. 737-746
    • Huang, C.H.1    Kuo, W.Y.2    Weiss, C.3    Jinn, T.L.4
  • 6
    • 85045352144 scopus 로고    scopus 로고
    • Models for the mechanism for activating copper-zinc superoxide dismutase in the absence of the CCS Cu chaperone in Arabidopsis
    • PMID:22476460
    • Huang CH, Kuo WY, Jinn TL. Models for the mechanism for activating copper-zinc superoxide dismutase in the absence of the CCS Cu chaperone in Arabidopsis. Plant Signal Behav 2012; 7:428-430; PMID:22476460; http://dx.doi.org/10.4161/psb.19192.
    • (2012) Plant Signal Behav , vol.7 , pp. 428-430
    • Huang, C.H.1    Kuo, W.Y.2    Jinn, T.L.3
  • 7
    • 0036001083 scopus 로고    scopus 로고
    • Role of superoxide dismutases (SODs) in controlling oxidative stress in plants
    • PMID:11997379
    • Alscher RG, Erturk N, Heath LS. Role of superoxide dismutases (SODs) in controlling oxidative stress in plants. J Exp Bot 2002; 53:1331-141; PMID:11997379; http://dx.doi.org/10.1093/jexbot/53.372.1331.
    • (2002) J Exp Bot , vol.53 , pp. 1331-1411
    • Alscher, R.G.1    Erturk, N.2    Heath, L.S.3
  • 8
    • 0036509440 scopus 로고    scopus 로고
    • Molecular evolution and structure--function relationships of the superoxide dismutase gene families in angiosperms and their relationship to other eukaryotic and prokaryotic superoxide dismutases
    • PMID:11883900
    • Fink RC, Scandalios JG. Molecular evolution and structure--function relationships of the superoxide dismutase gene families in angiosperms and their relationship to other eukaryotic and prokaryotic superoxide dismutases. Arch Biochem Biophys 2002; 399:19-36; PMID:11883900; http://dx.doi.org/10.1006/abbi.2001.2739.
    • (2002) Arch Biochem Biophys , vol.399 , pp. 19-36
    • Fink, R.C.1    Scandalios, J.G.2
  • 9
    • 58549118439 scopus 로고    scopus 로고
    • A heterocomplex of iron superoxide dismutases defends chloroplast nucleoids against oxidative stress and is essential for chloroplast development in Arabidopsis
    • PMID:18996978
    • Myouga F, Hosoda C, Umezawa T, Iizumi H, Kuromori T, Motohashi R, et al. A heterocomplex of iron superoxide dismutases defends chloroplast nucleoids against oxidative stress and is essential for chloroplast development in Arabidopsis. Plant Cell 2008; 20:3148-3162; PMID:18996978; http://dx.doi.org/10.1105/tpc.108.061341.
    • (2008) Plant Cell , vol.20 , pp. 3148-3162
    • Myouga, F.1    Hosoda, C.2    Umezawa, T.3    Iizumi, H.4    Kuromori, T.5    Motohashi, R.6
  • 10
    • 84870249599 scopus 로고    scopus 로고
    • CHAPERONIN 20 mediates iron superoxide dismutase (FeSOD) activity independent of its co-chaperonin role in Arabidopsis chloroplasts
    • In press, PMID:23057508
    • Kuo WY, Huang CH, Liu AC, Cheng CP, Li SH, Chang WC, et al. CHAPERONIN 20 mediates iron superoxide dismutase (FeSOD) activity independent of its co-chaperonin role in Arabidopsis chloroplasts. New Phytol 2012, In press; PMID:23057508; http://dx.doi.org/10.1111/j.1469-8137.2012.04369.x.
    • (2012) New Phytol
    • Kuo, W.Y.1    Huang, C.H.2    Liu, A.C.3    Cheng, C.P.4    Li, S.H.5    Chang, W.C.6
  • 11
    • 0026744722 scopus 로고
    • Identification, characterization, and DNA sequence of a functional "double" groES-like chaperonin from chloroplasts of higher plants
    • PMID:1356267
    • Bertsch U, Soll J, Seetharam R, Viitanen PV. Identification, characterization, and DNA sequence of a functional "double" groES-like chaperonin from chloroplasts of higher plants. Proc Natl Acad Sci U S A 1992; 89:8696-700; PMID:1356267; http://dx.doi.org/10.1073/pnas.89.18.8696.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 8696-8700
    • Bertsch, U.1    Soll, J.2    Seetharam, R.3    Viitanen, P.V.4
  • 12
    • 0028921271 scopus 로고
    • Spinach chloroplast cpn21 cochaperonin possesses two functional domains fused together in a toroidal structure and exhibits nucleotidedependent binding to plastid chaperonin 60
    • PMID:7738007
    • Baneyx F, Bertsch U, Kalbach CE, van der Vies SM, Soll J, Gatenby AA. Spinach chloroplast cpn21 cochaperonin possesses two functional domains fused together in a toroidal structure and exhibits nucleotidedependent binding to plastid chaperonin 60. J Biol Chem 1995; 270:10695-10702; PMID:7738007; http://dx.doi.org/10.1074/jbc.270.18.10695.
    • (1995) J Biol Chem , vol.270 , pp. 10695-10702
    • Baneyx, F.1    Bertsch, U.2    Kalbach, C.E.3    van der Vies, S.M.4    Soll, J.5    Gatenby, A.A.6
  • 13
    • 0032898910 scopus 로고    scopus 로고
    • CDNA sequence and overexpression of chloroplast chaperonin 21 from Arabidopsis thaliana
    • PMID:9989238
    • Hirohashi T, Nishio K, Nakai M. cDNA sequence and overexpression of chloroplast chaperonin 21 from Arabidopsis thaliana. Biochim Biophys Acta 1999; 1429:512-515; PMID:9989238; http://dx.doi.org/10.1016/S0167-4838(98)00268-4.
    • (1999) Biochim Biophys Acta , vol.1429 , pp. 512-515
    • Hirohashi, T.1    Nishio, K.2    Nakai, M.3
  • 14
    • 0033103962 scopus 로고    scopus 로고
    • Chloroplast Cpn20 forms a tetrameric structure in Arabidopsis thaliana
    • PMID:10205903
    • Koumoto Y, Shimada T, Kondo M, Takao T, Shimonishi Y, Hara-Nishimura I, et al. Chloroplast Cpn20 forms a tetrameric structure in Arabidopsis thaliana. Plant J 1999; 17:467-477; PMID:10205903; http://dx.doi.org/10.1046/j.1365-313X.1999.00388.x.
    • (1999) Plant J , vol.17 , pp. 467-477
    • Koumoto, Y.1    Shimada, T.2    Kondo, M.3    Takao, T.4    Shimonishi, Y.5    Hara-Nishimura, I.6
  • 15
    • 58549113565 scopus 로고    scopus 로고
    • Cpn20: Siamese twins of the chaperonin world
    • PMID:19031045
    • Weiss C, Bonshtien A, Farchi-Pisanty O, Vitlin A, Azem A. Cpn20: siamese twins of the chaperonin world. Plant Mol Biol 2009; 69:227-238; PMID:19031045; http://dx.doi.org/10.1007/s11103-008-9432-3.
    • (2009) Plant Mol Biol , vol.69 , pp. 227-238
    • Weiss, C.1    Bonshtien, A.2    Farchi-Pisanty, O.3    Vitlin, A.4    Azem, A.5
  • 16
    • 0017853485 scopus 로고
    • A study on the reconstitution of ironsuperoxide dismutase from Pseudomonas ovalis
    • PMID:25273
    • Yamakura F. A study on the reconstitution of ironsuperoxide dismutase from Pseudomonas ovalis. J Biochem 1978; 83:849-857; PMID:25273.
    • (1978) J Biochem , vol.83 , pp. 849-857
    • Yamakura, F.1
  • 17
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase
    • PMID:10221913
    • Rae TD, Schmidt PJ, Pufahl RA, Culotta VC, O'Halloran TV. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 1999; 284:805-808; PMID:10221913; http://dx.doi.org/10.1126/science.284.5415.805.
    • (1999) Science , vol.284 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 18
    • 33746932518 scopus 로고    scopus 로고
    • Activation of superoxide dismutases: Putting the metal to the pedal
    • Culotta VC, Yang M, O'Halloran TV. Activation of superoxide dismutases: putting the metal to the pedal. Biochim Biophys Acta 2006; 1763:747-758.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 747-758
    • Culotta, V.C.1    Yang, M.2    O'Halloran, T.V.3
  • 19
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • PMID:15247478
    • Bulteau AL, O'Neill HA, Kennedy MC, Ikeda-Saito M, Isaya G, Szweda LI. Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 2004; 305:242-245; PMID:15247478; http://dx.doi.org/10.1126/science.1098991.
    • (2004) Science , vol.305 , pp. 242-245
    • Bulteau, A.L.1    O'Neill, H.A.2    Kennedy, M.C.3    Ikeda-Saito, M.4    Isaya, G.5    Szweda, L.I.6
  • 20
    • 45849123222 scopus 로고    scopus 로고
    • A cytosolic iron chaperone that delivers iron to ferritin
    • PMID:18511687
    • Shi H, Bencze KZ, Stemmler TL, Philpott CC. A cytosolic iron chaperone that delivers iron to ferritin. Science 2008; 320:1207-1210; PMID:18511687; http://dx.doi.org/10.1126/science.1157643.
    • (2008) Science , vol.320 , pp. 1207-1210
    • Shi, H.1    Bencze, K.Z.2    Stemmler, T.L.3    Philpott, C.C.4
  • 21
    • 0035914375 scopus 로고    scopus 로고
    • Copper stabilizes a heterodimer of the yCCS metallochaperone and its target superoxide dismutase
    • PMID:11473116
    • Torres AS, Petri V, Rae TD, O'Halloran TV. Copper stabilizes a heterodimer of the yCCS metallochaperone and its target superoxide dismutase. J Biol Chem 2001; 276:38410-38416; PMID:11473116; http://dx.doi.org/10.1074/jbc.M104790200.
    • (2001) J Biol Chem , vol.276 , pp. 38410-38416
    • Torres, A.S.1    Petri, V.2    Rae, T.D.3    O'Halloran, T.V.4
  • 22
    • 0034721928 scopus 로고    scopus 로고
    • Copper activation of superoxide dismutase 1 (SOD1) in vivo. Role for protein-protein interactions with the copper chaperone for SOD1
    • PMID:10944535
    • Schmidt PJ, Kunst C, Culotta VC. Copper activation of superoxide dismutase 1 (SOD1) in vivo. Role for protein-protein interactions with the copper chaperone for SOD1. J Biol Chem 2000; 275:33771-33776; PMID:10944535; http://dx.doi.org/10.1074/jbc.M006254200.
    • (2000) J Biol Chem , vol.275 , pp. 33771-33776
    • Schmidt, P.J.1    Kunst, C.2    Culotta, V.C.3
  • 23
    • 3543029884 scopus 로고    scopus 로고
    • Oxygeninduced maturation of SOD1: A key role for disulfide formation by the copper chaperone CCS
    • PMID:15215895
    • Furukawa Y, Torres AS, O'Halloran TV. Oxygeninduced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS. EMBO J 2004; 23:2872-2881; PMID:15215895; http://dx.doi.org/10.1038/sj.emboj.7600276.
    • (2004) EMBO J , vol.23 , pp. 2872-2881
    • Furukawa, Y.1    Torres, A.S.2    O'Halloran, T.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.