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Volumn 510, Issue 2, 2012, Pages 107-112

Functional characterization and gene expression profiling of superoxide dismutase from plant pathogenic phytoplasma

Author keywords

Antioxidant enzyme; Mycoplasma; Plant pathogenic bacteria; Reactive oxygen species

Indexed keywords

MANGANESE; METAL ION; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE;

EID: 84867337079     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2012.09.001     Document Type: Article
Times cited : (28)

References (51)
  • 1
    • 63749116365 scopus 로고    scopus 로고
    • Gene expression in grapevine cultivars in response to Bois Noir phytoplasma infection
    • Albertazzi G., et al. Gene expression in grapevine cultivars in response to Bois Noir phytoplasma infection. Plant Sci. 2009, 176:792-804.
    • (2009) Plant Sci. , vol.176 , pp. 792-804
    • Albertazzi, G.1
  • 2
    • 0033513358 scopus 로고    scopus 로고
    • The water-water cycle in chloroplasts: scavenging of active oxygen and dissipation of excess photons
    • Asada K. The water-water cycle in chloroplasts: scavenging of active oxygen and dissipation of excess photons. Annu. Rev. Plant Physiol. Plant Mol. Biol. 1999, 50:601-639.
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 601-639
    • Asada, K.1
  • 3
    • 33644847226 scopus 로고    scopus 로고
    • Living with genome instability: the adaptation of phytoplasmas to diverse environments of their insect and plant hosts
    • Bai X., et al. Living with genome instability: the adaptation of phytoplasmas to diverse environments of their insect and plant hosts. J. Bacteriol. 2006, 188:3682-3696.
    • (2006) J. Bacteriol. , vol.188 , pp. 3682-3696
    • Bai, X.1
  • 4
    • 0023463279 scopus 로고
    • Aspects of the structure, function, and applications of superoxide dismutase
    • Bannister J.V., Bannister W.H., Rotilio G. Aspects of the structure, function, and applications of superoxide dismutase. CRC Crit. Rev. Biochem. 1987, 22:111-180.
    • (1987) CRC Crit. Rev. Biochem. , vol.22 , pp. 111-180
    • Bannister, J.V.1    Bannister, W.H.2    Rotilio, G.3
  • 5
    • 0015153416 scopus 로고
    • Superoxide dismutase: improved assays and an assay applicable to acrylamide gels
    • Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 1971, 44:276-287.
    • (1971) Anal. Biochem. , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 6
    • 0028032403 scopus 로고
    • Escherichia coli expresses a copper- and zinc-containing superoxide dismutase
    • Benov L.T., Fridovich I. Escherichia coli expresses a copper- and zinc-containing superoxide dismutase. J. Biol. Chem. 1994, 269:25310-25314.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25310-25314
    • Benov, L.T.1    Fridovich, I.2
  • 8
    • 0034636391 scopus 로고    scopus 로고
    • Identification of the copper-zinc superoxide dismutase activity in Mycoplasma hyopneumoniae
    • Chen J.R., Weng C.N., Ho T.Y., Cheng I.C., Lai S.S. Identification of the copper-zinc superoxide dismutase activity in Mycoplasma hyopneumoniae. Vet. Microbiol. 2000, 73:301-310.
    • (2000) Vet. Microbiol. , vol.73 , pp. 301-310
    • Chen, J.R.1    Weng, C.N.2    Ho, T.Y.3    Cheng, I.C.4    Lai, S.S.5
  • 9
    • 0030574273 scopus 로고    scopus 로고
    • The oxidative burst protects plants against pathogen attack: mechanism and role as an emergency signal for plant bio-defence - a review
    • Doke N., et al. The oxidative burst protects plants against pathogen attack: mechanism and role as an emergency signal for plant bio-defence - a review. Gene 1996, 179:45-51.
    • (1996) Gene , vol.179 , pp. 45-51
    • Doke, N.1
  • 10
    • 0033958343 scopus 로고    scopus 로고
    • Purification and characterization of an iron superoxide dismutase and a catalase from the sulfate-reducing bacterium Desulfovibrio gigas
    • Dos Santos W.G., Pacheco I., Liu M.Y., Teixeira M., Xavier A.V., LeGall J. Purification and characterization of an iron superoxide dismutase and a catalase from the sulfate-reducing bacterium Desulfovibrio gigas. J. Bacteriol. 2000, 182:796-804.
    • (2000) J. Bacteriol. , vol.182 , pp. 796-804
    • Dos Santos, W.G.1    Pacheco, I.2    Liu, M.Y.3    Teixeira, M.4    Xavier, A.V.5    LeGall, J.6
  • 11
    • 0016414528 scopus 로고
    • Superoxide dismutase
    • Fridovich I. Superoxide dismutase. Annu. Rev. Biochem. 1975, 44:147-159.
    • (1975) Annu. Rev. Biochem. , vol.44 , pp. 147-159
    • Fridovich, I.1
  • 12
    • 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
  • 13
    • 84908739973 scopus 로고
    • Superoxide dismutase, catalase and glutathione peroxidase: solutions to the problems of living with oxygen
    • Halliwell B. Superoxide dismutase, catalase and glutathione peroxidase: solutions to the problems of living with oxygen. New Phytol. 1974, 73:1075-1086.
    • (1974) New Phytol. , vol.73 , pp. 1075-1086
    • Halliwell, B.1
  • 14
    • 0033548095 scopus 로고    scopus 로고
    • Export of recombinant Mycobacterium tuberculosis superoxide dismutase is dependent upon both information in the protein and mycobacterial export machinery. A model for studying export of leaderless proteins by pathogenic mycobacteria
    • Harth G., Horwitz M.A. Export of recombinant Mycobacterium tuberculosis superoxide dismutase is dependent upon both information in the protein and mycobacterial export machinery. A model for studying export of leaderless proteins by pathogenic mycobacteria. J. Biol. Chem. 1999, 274:4281-4292.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4281-4292
    • Harth, G.1    Horwitz, M.A.2
  • 15
    • 0034319185 scopus 로고    scopus 로고
    • Molecular biology of oxygen tolerance in lactic acid bacteria: functions of NADH oxidases and Dpr in oxidative stress
    • Higuchi M., Yamamoto Y., Kamio Y. Molecular biology of oxygen tolerance in lactic acid bacteria: functions of NADH oxidases and Dpr in oxidative stress. J. Biosci. Bioeng. 2000, 90:484-493.
    • (2000) J. Biosci. Bioeng. , vol.90 , pp. 484-493
    • Higuchi, M.1    Yamamoto, Y.2    Kamio, Y.3
  • 17
    • 65549108282 scopus 로고    scopus 로고
    • A unique virulence factor for proliferation and dwarfism in plants identified from a phytopathogenic bacterium
    • Hoshi A., et al. A unique virulence factor for proliferation and dwarfism in plants identified from a phytopathogenic bacterium. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:6416-6421.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 6416-6421
    • Hoshi, A.1
  • 18
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay J.A. Pathways of oxidative damage. Annu. Rev. Microbiol. 2003, 57:395-418.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 19
    • 0029958917 scopus 로고    scopus 로고
    • Cloning and analysis of sodC, encoding the copper-zinc superoxide dismutase of Escherichia coli
    • Imlay K.R.C., Imlay J.A. Cloning and analysis of sodC, encoding the copper-zinc superoxide dismutase of Escherichia coli. J. Bacteriol. 1996, 178:2564-2571.
    • (1996) J. Bacteriol. , vol.178 , pp. 2564-2571
    • Imlay, K.R.C.1    Imlay, J.A.2
  • 20
    • 67650723103 scopus 로고    scopus 로고
    • In the non-insect-transmissible line of onion yellows phytoplasma (OY-NIM), the plasmid-encoded transmembrane protein ORF3 lacks the major promoter region
    • Ishii Y., et al. In the non-insect-transmissible line of onion yellows phytoplasma (OY-NIM), the plasmid-encoded transmembrane protein ORF3 lacks the major promoter region. Microbiology 2009, 155:2058-2067.
    • (2009) Microbiology , vol.155 , pp. 2058-2067
    • Ishii, Y.1
  • 21
    • 40549139820 scopus 로고    scopus 로고
    • Structural and functional characterization of an organic hydroperoxide resistance protein from Mycoplasma gallisepticum
    • Jenkins C., Samudrala R., Geary S.J., Djordjevic S.P. Structural and functional characterization of an organic hydroperoxide resistance protein from Mycoplasma gallisepticum. J. Bacteriol. 2008, 190:2206-2216.
    • (2008) J. Bacteriol. , vol.190 , pp. 2206-2216
    • Jenkins, C.1    Samudrala, R.2    Geary, S.J.3    Djordjevic, S.P.4
  • 22
    • 0037613797 scopus 로고    scopus 로고
    • First complete nucleotide sequence and heterologous gene organization of the two rRNA operons in the phytoplasma genome
    • Jung H.Y., et al. First complete nucleotide sequence and heterologous gene organization of the two rRNA operons in the phytoplasma genome. DNA Cell Biol. 2003, 22:209-215.
    • (2003) DNA Cell Biol. , vol.22 , pp. 209-215
    • Jung, H.Y.1
  • 23
    • 0034830368 scopus 로고    scopus 로고
    • Cloning and expression analysis of Phytoplasma protein translocation genes
    • Kakizawa S., et al. Cloning and expression analysis of Phytoplasma protein translocation genes. Mol. Plant Microbe Interact. 2001, 14:1043-1050.
    • (2001) Mol. Plant Microbe Interact. , vol.14 , pp. 1043-1050
    • Kakizawa, S.1
  • 24
    • 9144259966 scopus 로고    scopus 로고
    • Secretion of immunodominant membrane protein from onion yellows phytoplasma through the Sec protein-translocation system in Escherichia coli
    • Kakizawa S., et al. Secretion of immunodominant membrane protein from onion yellows phytoplasma through the Sec protein-translocation system in Escherichia coli. Microbiology 2004, 150:135-142.
    • (2004) Microbiology , vol.150 , pp. 135-142
    • Kakizawa, S.1
  • 25
    • 47249123775 scopus 로고    scopus 로고
    • The linear chromosome of the plant-pathogenetic mycoplasma 'Candidatus Phytoplasma mali'
    • Kube M., et al. The linear chromosome of the plant-pathogenetic mycoplasma 'Candidatus Phytoplasma mali'. BMC Genomics 2008, 9:306.
    • (2008) BMC Genomics , vol.9 , pp. 306
    • Kube, M.1
  • 30
    • 80053583742 scopus 로고    scopus 로고
    • Phytoplasma effector SAP54 induces indeterminate leaf-like flower development in Arabidopsis plants
    • MacLean A.M., et al. Phytoplasma effector SAP54 induces indeterminate leaf-like flower development in Arabidopsis plants. Plant Physiol. 2011, 157:831-841.
    • (2011) Plant Physiol. , vol.157 , pp. 831-841
    • MacLean, A.M.1
  • 31
    • 0028170326 scopus 로고
    • Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress
    • Michiels C., Raes M., Toussaint O., Remacle J. Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress. Free Radic. Biol. Med. 1993, 17:235-248.
    • (1993) Free Radic. Biol. Med. , vol.17 , pp. 235-248
    • Michiels, C.1    Raes, M.2    Toussaint, O.3    Remacle, J.4
  • 32
    • 0042424841 scopus 로고    scopus 로고
    • Two different thymidylate kinase gene homologues, including one that has catalytic activity, are encoded in the onion yellows phytoplasma genome
    • Miyata S., et al. Two different thymidylate kinase gene homologues, including one that has catalytic activity, are encoded in the onion yellows phytoplasma genome. Microbiology 2003, 149:2243-2250.
    • (2003) Microbiology , vol.149 , pp. 2243-2250
    • Miyata, S.1
  • 33
    • 41249085856 scopus 로고    scopus 로고
    • Reactive oxygen species modulate Anopheles gambiae immunity against bacteria and Plasmodium
    • Molina-Cruz A., et al. Reactive oxygen species modulate Anopheles gambiae immunity against bacteria and Plasmodium. J. Biol. Chem. 2008, 283:3217-3223.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3217-3223
    • Molina-Cruz, A.1
  • 34
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species
    • Møller I.M. Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annu. Rev. Plant Physiol. Plant Mol. Biol. 2001, 52:561-591.
    • (2001) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.52 , pp. 561-591
    • Møller, I.M.1
  • 35
    • 1942489837 scopus 로고    scopus 로고
    • Recovery in apple trees infected with the apple proliferation phytoplasma: an ultrastructural and biochemical study
    • Musetti R., di Toppi L.S., Ermacora P., Favali M.A. Recovery in apple trees infected with the apple proliferation phytoplasma: an ultrastructural and biochemical study. Phytopathology 2004, 94:203-208.
    • (2004) Phytopathology , vol.94 , pp. 203-208
    • Musetti, R.1    di Toppi, L.S.2    Ermacora, P.3    Favali, M.A.4
  • 36
    • 23944444852 scopus 로고    scopus 로고
    • Hydrogen peroxide localization and antioxidant status in the recovery of apricot plants from European stone fruit yellows
    • Musetti R., et al. Hydrogen peroxide localization and antioxidant status in the recovery of apricot plants from European stone fruit yellows. Eur. J. Plant Pathol. 2005, 112:53-61.
    • (2005) Eur. J. Plant Pathol. , vol.112 , pp. 53-61
    • Musetti, R.1
  • 37
    • 0035153883 scopus 로고    scopus 로고
    • Isolation and characterization of derivative lines of the onion yellows phytoplasma that do not cause stunting or phloem hyperplasia
    • Oshima K., et al. Isolation and characterization of derivative lines of the onion yellows phytoplasma that do not cause stunting or phloem hyperplasia. Phytopathology 2001, 91:1024-1029.
    • (2001) Phytopathology , vol.91 , pp. 1024-1029
    • Oshima, K.1
  • 38
    • 9144247750 scopus 로고    scopus 로고
    • Reductive evolution suggested from the complete genome sequence of a plant-pathogenic phytoplasma
    • Oshima K., et al. Reductive evolution suggested from the complete genome sequence of a plant-pathogenic phytoplasma. Nat. Genet. 2004, 36:27-29.
    • (2004) Nat. Genet. , vol.36 , pp. 27-29
    • Oshima, K.1
  • 39
    • 34250805450 scopus 로고    scopus 로고
    • Presence of two glycolytic gene clusters in a severe pathogenic line of Candidatus Phytoplasma asteris
    • Oshima K., et al. Presence of two glycolytic gene clusters in a severe pathogenic line of Candidatus Phytoplasma asteris. Mol. Plant Pathol. 2007, 7:481-489.
    • (2007) Mol. Plant Pathol. , vol.7 , pp. 481-489
    • Oshima, K.1
  • 40
    • 80051678909 scopus 로고    scopus 로고
    • Dramatic transcriptional changes in an intracellular parasite enable host switching between plant and insect
    • Oshima K., et al. Dramatic transcriptional changes in an intracellular parasite enable host switching between plant and insect. PLoS One 2011, 6:e2342.
    • (2011) PLoS One , vol.6
    • Oshima, K.1
  • 42
    • 0031770391 scopus 로고    scopus 로고
    • Molecular biology and pathogenicity of mycoplasmas
    • Razin S., Yogev D., Naot Y. Molecular biology and pathogenicity of mycoplasmas. Microbiol. Mol. Biol. Rev. 1998, 62:1094-1156.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1094-1156
    • Razin, S.1    Yogev, D.2    Naot, Y.3
  • 43
  • 44
    • 70350457960 scopus 로고    scopus 로고
    • The Mycoplasma genitalium MG_454 gene product resists killing by organic hydroperoxides
    • Saikolappan S., Sasindran S.J., Yu H.D., Baseman J.B., Dhandayuthapani S. The Mycoplasma genitalium MG_454 gene product resists killing by organic hydroperoxides. J. Bacteriol. 2009, 191:6675-6682.
    • (2009) J. Bacteriol. , vol.191 , pp. 6675-6682
    • Saikolappan, S.1    Sasindran, S.J.2    Yu, H.D.3    Baseman, J.B.4    Dhandayuthapani, S.5
  • 47
    • 82755186471 scopus 로고    scopus 로고
    • Phytoplasma protein effector SAP11 enhances insect vector reproduction by manipulating plant development and defense hormone biosynthesis
    • Sugio A., Kingdom H.N., Maclean A.M., Grieve V.M., Hogenhout S.A. Phytoplasma protein effector SAP11 enhances insect vector reproduction by manipulating plant development and defense hormone biosynthesis. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:E1254-E1263.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108
    • Sugio, A.1    Kingdom, H.N.2    Maclean, A.M.3    Grieve, V.M.4    Hogenhout, S.A.5
  • 48
    • 44349099865 scopus 로고    scopus 로고
    • Comparative genome analysis of "Candidatus Phytoplasma australiense" (subgroup tuf-Australia I; rp-A) and "Ca. Phytoplasma asteris" strains OY-M and AY-WB
    • Tran-Nguyen L.T.T., Kube M., Schneider B., Reinhardt R., Gibb K.S. Comparative genome analysis of "Candidatus Phytoplasma australiense" (subgroup tuf-Australia I; rp-A) and "Ca. Phytoplasma asteris" strains OY-M and AY-WB. J. Bacteriol. 2008, 190:3979-3991.
    • (2008) J. Bacteriol. , vol.190 , pp. 3979-3991
    • Tran-Nguyen, L.T.T.1    Kube, M.2    Schneider, B.3    Reinhardt, R.4    Gibb, K.S.5
  • 49
    • 2942711599 scopus 로고    scopus 로고
    • An antibody against the SecA membrane protein of one phytoplasma reacts with those of phylogenetically different phytoplasmas
    • Wei W., et al. An antibody against the SecA membrane protein of one phytoplasma reacts with those of phylogenetically different phytoplasmas. Phytopathology 2004, 94:683-686.
    • (2004) Phytopathology , vol.94 , pp. 683-686
    • Wei, W.1
  • 51
    • 0030948290 scopus 로고    scopus 로고
    • Oxidative burst: an early plant response to pathogen infection
    • Wojtaszek P. Oxidative burst: an early plant response to pathogen infection. Biochem. J. 1997, 322:681-692.
    • (1997) Biochem. J. , vol.322 , pp. 681-692
    • Wojtaszek, P.1


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