메뉴 건너뛰기




Volumn 62, Issue 12, 2011, Pages 4281-4294

Plants contain two SCO proteins that are differentially involved in cytochrome c oxidase function and copper and redox homeostasis

Author keywords

Arabidopsis thaliana, copper homeostasis; cytochrome c oxidase; SCO protein

Indexed keywords

ARABIDOPSIS PROTEIN; CATION TRANSPORT PROTEIN; COPPER; CYTOCHROME C OXIDASE; HCC1 PROTEIN, ARABIDOPSIS; HCC2 PROTEIN, ARABIDOPSIS; ISOENZYME; MITOCHONDRIAL PROTEIN; SUPEROXIDE DISMUTASE;

EID: 80051762466     PISSN: 00220957     EISSN: 14602431     Source Type: Journal    
DOI: 10.1093/jxb/err138     Document Type: Article
Times cited : (45)

References (60)
  • 3
    • 14844336406 scopus 로고    scopus 로고
    • Ortholog search of proteins involved in copper delivery to cytochrome c oxidase and functional analysis of paralogs and gene neighbors by genomic context
    • DOI 10.1021/pr049862f
    • Arnesano F, Banci L, Bertini I, Martinelli M. 2005. Ortholog search of proteins involved in copper delivery to cytochrome c oxidase and functional analysis of paralogs and gene neighbors by genomic context. Journal of Proteome Research 4, 63-70. (Pubitemid 40344457)
    • (2005) Journal of Proteome Research , vol.4 , Issue.1 , pp. 63-70
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Martinelli, M.4
  • 4
    • 33845636142 scopus 로고    scopus 로고
    • The promoters of Arabidopsis thaliana genes AtCOX17-1 and -2, encoding a copper chaperone involved in cytochrome c oxidase biogenesis, are preferentially active in roots and anthers and induced by biotic and abiotic stress
    • DOI 10.1111/j.1399-3054.2006.00776.x
    • Attallah CV, Welchen E, Gonzalez DH. 2007a. The promoters of Arabidopsis thaliana genes AtCOX17-1 and-2, encoding a copper chaperone involved in cytochrome c oxidase biogenesis, are preferentially active in roots and anthers and induced by biotic and abiotic stress. Physiologia Plantarum 1290, 123-134. (Pubitemid 44953380)
    • (2007) Physiologia Plantarum , vol.129 , Issue.1 , pp. 123-134
    • Attallah, C.V.1    Welchen, E.2    Gonzalez, D.H.3
  • 5
    • 34548680499 scopus 로고    scopus 로고
    • Characterization of Arabidopsis thaliana genes encoding functional homologues of the yeast metal chaperone Cox19p, involved in cytochrome c oxidase biogenesis
    • DOI 10.1007/s11103-007-9224-1
    • Attallah CV, Welchen E, Pujol C, Bonnard G, Gonzalez DH. 2007b. Characterization of Arabidopsis thaliana genes encoding functional homologues of the yeast metal chaperone Cox19p, involved in cytochrome c oxidase biogenesis. Plant Molecular Biology 65, 343-355. (Pubitemid 47414564)
    • (2007) Plant Molecular Biology , vol.65 , Issue.3 , pp. 343-355
    • Attallah, C.V.1    Welchen, E.2    Pujol, C.3    Bonnard, G.4    Gonzalez, D.H.5
  • 6
    • 0037008216 scopus 로고    scopus 로고
    • AtCOX17, an Arabidopsis homolog of the yeast copper chaperone COX17
    • DOI 10.1104/pp.010963
    • Balandin T, Castresana C. 2002. AtCOX17, an Arabidopsis homolog of the yeast copper chaperone COX17. Plant Physiology 129, 1852-1857. (Pubitemid 34923249)
    • (2002) Plant Physiology , vol.129 , Issue.4 , pp. 1852-1857
    • Balandin, T.1    Castresana, C.2
  • 7
    • 0242541974 scopus 로고    scopus 로고
    • Solution structure of Sco1: A thioredoxin-like protein involved in cytochrome c oxidase assembly
    • DOI 10.1016/j.str.2003.10.004
    • Balatri E, Banci L, Bertini I, Cantini F, Ciofi-Baffoni S. 2003. Solution structure of Sco1: a thioredoxin-like protein involved in cytochrome c oxidase assembly. Structure 11, 1431-1443. (Pubitemid 37412425)
    • (2003) Structure , vol.11 , Issue.11 , pp. 1431-1443
    • Balatri, E.1    Banci, L.2    Bertini, I.3    Cantini, F.4    Ciofi-Baffoni, S.5
  • 8
    • 34248223700 scopus 로고    scopus 로고
    • The functions of Sco proteins from genome-based analysis
    • DOI 10.1021/pr060538p
    • Banci L, Bertini I, Cavallaro G, Rosato A. 2007. The functions of Sco proteins from genome-based analysis. Journal of Proteome Research 6, 1568-1579. (Pubitemid 46724054)
    • (2007) Journal of Proteome Research , vol.6 , Issue.4 , pp. 1568-1579
    • Banci, L.1    Bertini, I.2    Cavallaro, G.3    Rosato, A.4
  • 9
    • 0037029074 scopus 로고    scopus 로고
    • Cytochrome oxidase in health and disease
    • DOI 10.1016/S0378-1119(01)00803-4, PII S0378111901008034
    • Barrientos A, Barrios MH, Valnot I, Rö tig A, Rustin P, Tzagoloff A. 2002. Cytochrome oxidase in health and disease. Gene 286, 53-63. (Pubitemid 34273861)
    • (2002) Gene , vol.286 , Issue.1 , pp. 53-63
    • Barrientos, A.1    Barros, M.H.2    Valnot, I.3    Rotig, A.4    Rustin, P.5    Tzagoloff, A.6
  • 10
    • 33646825207 scopus 로고    scopus 로고
    • A spatiotemporal analysis of enzymatic activities associated with carbon metabolism in wild-type and mutant embryos of Arabidopsis using in situ histochemistry
    • DOI 10.1111/j.1365-313X.2006.02682.x
    • Baud S, Graham IA. 2006. A spatiotemporal analysis of enzymatic activities associated with carbon metabolism in wild-type and mutant embryos of Arabidopsis using in situ histochemistry. The Plant Journal 46, 155-169. (Pubitemid 43773586)
    • (2006) Plant Journal , vol.46 , Issue.1 , pp. 155-169
    • Baud, S.1    Graham, I.A.2
  • 11
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp C, Fridovich I. 1971. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Analytical Biochemistry 44, 276-287.
    • (1971) Analytical Biochemistry , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 12
    • 0031626987 scopus 로고    scopus 로고
    • Preparation of RNA
    • Martinez-Zapater J, Salinas J, eds. Arabidopsis protocols. Totowa, NJ: Humana Press Inc
    • Carpenter CD, Simon AE. 1998. Preparation of RNA. In: Martinez-Zapater J, Salinas J, eds. Methods in molecular biology, Vol. 82. Arabidopsis protocols. Totowa, NJ: Humana Press Inc, 85-89.
    • (1998) Methods in Molecular Biology , vol.82 , pp. 85-89
    • Carpenter, C.D.1    Simon, A.E.2
  • 13
    • 0036772151 scopus 로고    scopus 로고
    • Expression profiling of the whole Arabidopsis Shaggy-like kinase multigene family by real-time reverse transcriptase-polymerase chain reaction
    • DOI 10.1104/pp.009175
    • Charrier B, Champion A, Henry Y, Kreis M. 2002. Expression profiling of the whole Arabidopsis shaggy-like kinase multigene family by real-time reverse transcriptase-polymerase chain reaction. Plant Physiology 130, 577-590. (Pubitemid 35235282)
    • (2002) Plant Physiology , vol.130 , Issue.2 , pp. 577-590
    • Charrier, B.1    Champion, A.2    Henry, Y.3    Kreis, M.4
  • 14
    • 29144470346 scopus 로고    scopus 로고
    • Real-time quantification of microRNAs by stem-loop RT-PCR
    • Chen C, Ridzon DA, Broomer AJ, et al. 2005. Real-time quantification of microRNAs by stem-loop RT-PCR. Nucleic Acids Research 33, e179.
    • (2005) Nucleic Acids Research , vol.33
    • Chen, C.1    Ridzon, D.A.2    Broomer, A.J.3
  • 15
    • 0033930194 scopus 로고    scopus 로고
    • Cytochrome c oxidase assembly factors with a thioredoxin fold are conserved among prokaryotes and eukaryotes
    • Chinenov YV. 2000. Cytochrome c oxidase assembly factors with a thioredoxin fold are conserved among prokaryotes and eukaryotes. Journal of Molecular Medicine 78, 239-242. (Pubitemid 30489706)
    • (2000) Journal of Molecular Medicine , vol.78 , Issue.5 , pp. 239-242
    • Chinenov, Y.V.1
  • 16
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough SJ, Bent AF. 1998. Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. The Plant Journal 16, 735-743.
    • (1998) The Plant Journal , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 17
    • 33746929896 scopus 로고    scopus 로고
    • Copper trafficking to the mitochondrion and assembly of copper metalloenzymes
    • DOI 10.1016/j.bbamcr.2006.03.002, PII S016748890600053X
    • Cobine PA, Pierrel F, Winge DR. 2006. Copper trafficking to the mitochondrion and assembly of copper metalloenzymes. Biochimica et Biophysica Acta 1763, 759-772. (Pubitemid 44189537)
    • (2006) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1763 , Issue.7 , pp. 759-772
    • Cobine, P.A.1    Pierrel, F.2    Winge, D.R.3
  • 18
    • 70350045014 scopus 로고    scopus 로고
    • Identification of regulatory elements involved in expression and induction by sucrose and UV-B light of the Arabidopsis thaliana COX5b-2 gene, encoding an isoform of cytochrome c oxidase subunit 5b
    • Comelli RN, Gonzalez DH. 2009. Identification of regulatory elements involved in expression and induction by sucrose and UV-B light of the Arabidopsis thaliana COX5b-2 gene, encoding an isoform of cytochrome c oxidase subunit 5b. Physiologia Plantarum 137, 213-224.
    • (2009) Physiologia Plantarum , vol.137 , pp. 213-224
    • Comelli, R.N.1    Gonzalez, D.H.2
  • 20
    • 0025978277 scopus 로고
    • A simple and rapid method for the preparation of plant genomic DNA for PCR analysis
    • Edwards K, Johnstone C, Thompson C. 1991. A simple and rapid method for the preparation of plant genomic DNA for PCR analysis. Nucleic Acids Research 19, 1349.
    • (1991) Nucleic Acids Research , vol.19 , pp. 1349
    • Edwards, K.1    Johnstone, C.2    Thompson, C.3
  • 21
    • 0000122573 scopus 로고
    • PHYLIP: Phylogeny Inference Package (Version 3.2)
    • Felsenstein J. 1989. PHYLIP: Phylogeny Inference Package (Version 3.2). Cladistics 5, 164-166.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 22
    • 33845298268 scopus 로고    scopus 로고
    • Assembly of mitochondrial cytochrome c-oxidase, a complicated and highly regulated cellular process
    • DOI 10.1152/ajpcell.00233.2006
    • Fontanesi F, Soto IC, Horn D, Barrientos A. 2006. Assembly of mitochondrial cytochrome c-oxidase, a complicated and highly regulated cellular process. American Journal of Physiology Cell Physiology 291, C1129-C1147. (Pubitemid 44878584)
    • (2006) American Journal of Physiology - Cell Physiology , vol.291 , Issue.6
    • Fontanesi, F.1    Soto, I.C.2    Horn, D.3    Barrientos, A.4
  • 23
    • 9444296498 scopus 로고    scopus 로고
    • SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.271.34.20531
    • Glerum DM, Shtanko A, Tzagoloff A. 1996. SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. Journal of Biological Chemistry 271, 20531-20535. (Pubitemid 26281827)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.34 , pp. 20531-20535
    • Moira Glerum, D.1    Shtanko, A.2    Tzagoloff, A.3
  • 24
    • 0028674948 scopus 로고
    • Rescue of a maize mitochondrial cytochrome oxidase mutant by tissue culture
    • Gu J, Dempsey S, Newton KJ. 1994. Rescue of a maize mitochondrial cytochrome oxidase mutant by tissue culture. The Plant Journal 6, 787-794. (Pubitemid 124000305)
    • (1994) Plant Journal , vol.6 , Issue.6 , pp. 787-794
    • Gu, J.1    Dempsey, S.2    Newton, K.J.3
  • 25
    • 51449101034 scopus 로고    scopus 로고
    • Identification of regulatory pathways controlling gene expression of stress-responsive mitochondrial proteins in arabidopsis
    • DOI 10.1104/pp.108.121384
    • Ho LHM, Giraud E, Uggalla V, Lister R, Clifton R, Glen A, Thirkettle-Watts D, Van Aken O, Whelan J. 2008. Identification of regulatory pathways controlling gene expression of stress-responsive mitochondrial proteins in Arabidopsis. Plant Physiology 147, 1858-1873. (Pubitemid 352844228)
    • (2008) Plant Physiology , vol.147 , Issue.4 , pp. 1858-1873
    • Ho, L.H.M.1    Giraud, E.2    Uggalla, V.3    Lister, R.4    Clifton, R.5    Glen, A.6    Thirkettle-Watts, D.7    Van Aken, O.8    Whelan, J.9
  • 26
    • 4143074731 scopus 로고    scopus 로고
    • Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome c oxidase
    • DOI 10.1074/jbc.M404747200
    • Horng YC, Cobine PA, Maxfield AB, Carr HS, Winge DR. 2004. Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome c oxidase. Journal of Biological Chemistry 279, 35334-35340. (Pubitemid 39100532)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35334-35340
    • Horng, Y.-C.1    Cobine, P.A.2    Maxfield, A.B.3    Carr, H.S.4    Winge, D.R.5
  • 28
    • 0029438206 scopus 로고
    • The beta-glucuronidase (gus) reporter gene system. Gene fusions; Spectrophotometric, fluorometric, and histochemical detection
    • Jones H, ed Plant gene transfer and expression protocols. Totowa, NJ: Humana Press Inc
    • Hull GA, Devic M. 1995. The beta-glucuronidase (gus) reporter gene system. Gene fusions; spectrophotometric, fluorometric, and histochemical detection. In: Jones H, ed. Methods in plant molecular biology, Vol. 49. Plant gene transfer and expression protocols. Totowa, NJ: Humana Press Inc, 125-141.
    • (1995) Methods in Plant Molecular Biology , vol.49 , pp. 125-141
    • Hull, G.A.1    Devic, M.2
  • 29
    • 0342444416 scopus 로고
    • GUS fusions: B-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson RA, Kavanagh TA, Bevan MW. 1987. GUS fusions: b-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO Journal 20, 3901-3907.
    • (1987) EMBO Journal , vol.20 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 30
    • 34547113093 scopus 로고    scopus 로고
    • Evidence for a pro-oxidant intermediate in the assembly of cytochrome oxidase
    • DOI 10.1074/jbc.M702379200
    • Khalimonchuk O, Bird A, Winge DR. 2007. Evidence for a pro-oxidant intermediate in the assembly of cytochrome oxidase. Journal of Biological Chemistry 282, 17442-17449. (Pubitemid 47100294)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.24 , pp. 17442-17449
    • Khalimonchuk, O.1    Bird, A.2    Winge, D.R.3
  • 31
    • 29544449035 scopus 로고    scopus 로고
    • Biogenesis of cytochrome c oxidase
    • DOI 10.1016/j.mito.2005.08.002, PII S1567724905000966
    • Khalimonchuk O, Rö del G. 2005. Biogenesis of cytochrome c oxidase. Mitochondrion 5, 363-388. (Pubitemid 43013019)
    • (2005) Mitochondrion , vol.5 , Issue.6 , pp. 363-388
    • Khalimonchuk, O.1    Rodel, G.2
  • 32
    • 41449117631 scopus 로고    scopus 로고
    • Function and redox state of mitochondrial localized cysteine-rich proteins important in the assembly of cytochrome c oxidase
    • Khalimonchuk O, Winge DR. 2008. Function and redox state of mitochondrial localized cysteine-rich proteins important in the assembly of cytochrome c oxidase. Biochimica et Biophysica Acta 1783, 618-628.
    • (2008) Biochimica et Biophysica Acta , vol.1783 , pp. 618-628
    • Khalimonchuk, O.1    Winge, D.R.2
  • 33
    • 0031887041 scopus 로고    scopus 로고
    • Control of seed development in Arabidopsis thaliana by atmospheric oxygen
    • DOI 10.1046/j.1365-3040.1998.00244.x
    • Kuang A, Crispi M, Musgrave ME. 1998. Control of seed development in Arabidopsis thaliana by atmospheric oxygen. Plan, Cell and Environment 21, 71-78. (Pubitemid 28131804)
    • (1998) Plant, Cell and Environment , vol.21 , Issue.1 , pp. 71-78
    • Kuang, A.1    Crispi, M.2    Musgrave, M.E.3
  • 36
    • 66149139796 scopus 로고    scopus 로고
    • Human SCO2 is required for the synthesis of CO II and as a thiol-disulphide oxidoreductase for SCO1
    • Leary SC, Sasarman F, Nishimura T, Shoubridge EA. 2009. Human SCO2 is required for the synthesis of CO II and as a thiol-disulphide oxidoreductase for SCO1. Human Molecular Genetics 18, 2230-2240.
    • (2009) Human Molecular Genetics , vol.18 , pp. 2230-2240
    • Leary, S.C.1    Sasarman, F.2    Nishimura, T.3    Shoubridge, E.A.4
  • 37
    • 33750478011 scopus 로고    scopus 로고
    • Transcriptional changes in powdery mildew infected wheat and Arabidopsis leaves undergoing syringolin-triggered hypersensitive cell death at infection sites
    • DOI 10.1007/s11103-006-9045-7
    • Michel K, Abderhalden O, Bruggmann R, Dudler R. 2006. Transcriptional changes in powdery mildew infected wheat and Arabidopsis leaves undergoing syringolin-triggered hypersensitive cell death at infection sites. Plant Molecular Biology 62, 561-578. (Pubitemid 44652250)
    • (2006) Plant Molecular Biology , vol.62 , Issue.4-5 , pp. 561-578
    • Michel, K.1    Abderhalden, O.2    Bruggmann, R.3    Dudler, R.4
  • 38
    • 67651083573 scopus 로고    scopus 로고
    • Common sets of promoter elements determine the expression characteristics of three Arabidopsis genes encoding isoforms of mitochondrial cytochrome c oxidase subunit 6b
    • Mufarrege EF, Curi GC, Gonzalez DH. 2009. Common sets of promoter elements determine the expression characteristics of three Arabidopsis genes encoding isoforms of mitochondrial cytochrome c oxidase subunit 6b. Plant and Cell Physiology 50, 1393-1399.
    • (2009) Plant and Cell Physiology , vol.50 , pp. 1393-1399
    • Mufarrege, E.F.1    Curi, G.C.2    Gonzalez, D.H.3
  • 39
    • 0035834661 scopus 로고    scopus 로고
    • Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein
    • Nittis T, George GN, Winge DR. 2001. Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein. Journal of Biological Chemistry 276, 42520-42526.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 42520-42526
    • Nittis, T.1    George, G.N.2    Winge, D.R.3
  • 40
    • 84948084827 scopus 로고    scopus 로고
    • Mitochondrial metabolism
    • Logan DC, ed Plant mitochondria. Oxford, UK: Blackwell Publishing Ltd
    • Nunes-Nesi A, Fernie AR. 2007. Mitochondrial metabolism. In: Logan DC, ed. Annual plant reviews, Vol. 31. Plant mitochondria. Oxford, UK: Blackwell Publishing Ltd, 212-277.
    • (2007) Annual Plant Reviews , vol.31 , pp. 212-277
    • Nunes-Nesi, A.1    Fernie, A.R.2
  • 42
    • 33846591865 scopus 로고    scopus 로고
    • Copper and iron homeostasis in Arabidopsis: Responses to metal deficiencies, interactions and biotechnological applications
    • DOI 10.1111/j.1365-3040.2007.01642.x
    • Puig S, Andrés-Colás N, Garća-Molina A, Peñ arrubia L. 2007. Copper and iron homeostasis in Arabidopsis: responses to metal deficiencies, interactions and biotechnological applications. Plant, Cell and Environment 30, 271-290. (Pubitemid 46184430)
    • (2007) Plant, Cell and Environment , vol.30 , Issue.3 , pp. 271-290
    • Puig, S.1    Andres-Colas, N.2    Garcia-Molina, A.3    Penarrubia, L.4
  • 43
    • 0033025125 scopus 로고    scopus 로고
    • Mitochondrial copper metabolism in yeast: Mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase
    • DOI 10.1007/s002940050438
    • Rentzsch A, Krummeck-Weiss G, Hofer A, Bartuschka A, Ostermann K, Rö del G. 1999. Mitochondrial copper metabolism in yeast: mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase. Current Genetics 35, 103-108. (Pubitemid 29141252)
    • (1999) Current Genetics , vol.35 , Issue.2 , pp. 103-108
    • Rentzsch, A.1    Krummeck-Weiss, G.2    Hofer, A.3    Bartuschka, A.4    Ostermann, K.5    Rodel, G.6
  • 44
    • 0642283837 scopus 로고    scopus 로고
    • Cytochrome c oxidase: Structure, function, and physiology of a redox-driven molecular machine
    • Richter OM, Ludwig B. 2003. Cytochrome c oxidase: structure, function, and physiology of a redox-driven molecular machine. Reviews of Physiology, Biochemistry and Pharmacology 147, 47-74.
    • (2003) Reviews of Physiology, Biochemistry and Pharmacology , vol.147 , pp. 47-74
    • Richter, O.M.1    Ludwig, B.2
  • 45
    • 47249146596 scopus 로고    scopus 로고
    • Mapping the functional interaction of Sco1 and Cox2 in cytochrome oxidase biogenesis
    • Rigby K, Cobine PA, Khalimonchuk O, Winge DR. 2008. Mapping the functional interaction of Sco1 and Cox2 in cytochrome oxidase biogenesis. Journal of Biological Chemistry 283, 15015-15022.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 15015-15022
    • Rigby, K.1    Cobine, P.A.2    Khalimonchuk, O.3    Winge, D.R.4
  • 47
    • 0000301881 scopus 로고
    • SCO1, a yeast nuclear gene essential for accumulation of mitochondrial cytochrome c oxidase subunit II
    • Schulze M, Rö del G. 1988. SCO1, a yeast nuclear gene essential for accumulation of mitochondrial cytochrome c oxidase subunit II. Molecular and General Genetics 211, 492-498. (Pubitemid 18083405)
    • (1988) Molecular and General Genetics , vol.211 , Issue.3 , pp. 492-498
    • Schulze, M.1    Rodel, G.2
  • 48
    • 0017390556 scopus 로고
    • A rapid, sensitive, and versatile assay for protein using coomassie brilliant blue G250
    • Sedmak J, Grossberg S. 1977. A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G-250. Analytical Biochemistry 79, 544-552. (Pubitemid 8105123)
    • (1977) Analytical Biochemistry , vol.79 , Issue.1-2 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 49
    • 0037781037 scopus 로고    scopus 로고
    • PAA1, a P-type ATPase of arabidopsis, functions in copper transport in chloroplasts
    • Shikanai T, Mü ller-Moulé P, Munekage Y, Niyogi KK, Pilon M. 2003. PAA1, a P-type ATPase of Arabidopsis, functions in copper transport in chloroplasts. The Plant Cell 15, 1333-1346. (Pubitemid 36715176)
    • (2003) Plant Cell , vol.15 , Issue.6 , pp. 1333-1346
    • Shikanai, T.1    Muller-Moule, P.2    Munekage, Y.3    Niyogi, K.K.4    Pilon, M.5
  • 53
    • 33747505089 scopus 로고    scopus 로고
    • Posttranscriptional induction of two Cu/Zn superoxide dismutase genes in Arabidopsis is mediated by downregulation of miR398 and important for oxidative stress tolerance
    • DOI 10.1105/tpc.106.041673
    • Sunkar R, Kapoor A, Zhu JK. 2006. Posttranscriptional induction of two Cu/Zn superoxide dismutase genes in Arabidopsis is mediated by downregulation of miR398 and important for oxidative stress tolerance. The Plant Cell 18, 2051-2065. (Pubitemid 44260196)
    • (2006) Plant Cell , vol.18 , Issue.8 , pp. 2051-2065
    • Sunkar, R.1    Kapoor, A.2    Zhu, J.-K.3
  • 54
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Research 22, 4673-4680. (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 56
    • 4544249972 scopus 로고    scopus 로고
    • The promoter of the Arabidopsis nuclear gene COX5b-1, encoding subunit 5b of the mitochondrial cytochrome c oxidase, directs tissue-specific expression by a combination of positive and negative regulatory elements
    • DOI 10.1093/jxb/erh223
    • Welchen E, Chan RL, Gonzalez DH. 2004. The promoter of the Arabidopsis nuclear gene COX5b-1, encoding subunit 5b of the mitochondrial cytochrome coxidase, directs tissue-specific expression by a combination of positive and negative regulatory elements. Journal of Experimental Botany 55, 1997-2004. (Pubitemid 39211157)
    • (2004) Journal of Experimental Botany , vol.55 , Issue.405 , pp. 1997-2004
    • Welchen, E.1    Chan, R.L.2    Gonzalez, D.H.3
  • 57
    • 29544438551 scopus 로고    scopus 로고
    • Differential expression of the Arabidopsis cytochrome c genes Cytc-1 and Cytc-2. Evidence for the involvement of TCP-domain protein-binding elements in anther- and meristem-specific expression of the Cytc-1 gene
    • DOI 10.1104/pp.105.065920
    • Welchen E, Gonzalez DH. 2005. Differential expression of the Arabidopsis cytochrome c genes Cytc-1 and Cytc-2: evidence for the involvement of TCP-domain protein binding elements in anther-and meristem-specific expression of the Cytc-1 gene. Plant Physiology 139, 88-100. (Pubitemid 43951594)
    • (2005) Plant Physiology , vol.139 , Issue.1 , pp. 88-100
    • Welchen, E.1    Gonzalez, D.H.2
  • 58
    • 0018358930 scopus 로고
    • Changes in the visual system of monocularly sutured or enucleated cats demonstrable with cytochrome oxidase histochemistry
    • DOI 10.1016/0006-8993(79)90728-5
    • Wong-Riley M. 1979. Changes in the visual system of monocularly sutured or enucleated cats demonstrable with cytochrome oxidase histochemistry. Brain Research 171, 11-28. (Pubitemid 9211579)
    • (1979) Brain Research , vol.171 , Issue.1 , pp. 11-28
    • Wong-Riley, M.1
  • 60
    • 62549146646 scopus 로고    scopus 로고
    • SQUAMOSA promoter binding protein-like 7 is a central regulator for copper homeostasis in Arabidopsis
    • Yamasaki H, Hayashi M, Fukazawa M, Kobayashi Y, Shikanai T. 2009. SQUAMOSA promoter binding protein-like 7 is a central regulator for copper homeostasis in Arabidopsis. The Plant Cell 21, 347-361.
    • (2009) The Plant Cell , vol.21 , pp. 347-361
    • Yamasaki, H.1    Hayashi, M.2    Fukazawa, M.3    Kobayashi, Y.4    Shikanai, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.