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Volumn 34, Issue 5, 1998, Pages 393-398

A single amino-acid substitution in the iron-sulphur protein subunit of succinate dehydrogenase determines resistance to carboxin in Mycosphaerella graminicola

Author keywords

Antifungal; Fungicide; Mitochondrial electron transport; Mutant

Indexed keywords

CARBOXIN; CYSTEINE; FUNGICIDE; GREEN FLUORESCENT PROTEIN; HISTIDINE; IRON SULFUR PROTEIN; PROTEIN SUBUNIT; SUCCINATE DEHYDROGENASE; TYROSINE;

EID: 0032425075     PISSN: 01728083     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002940050412     Document Type: Article
Times cited : (104)

References (27)
  • 2
    • 0030451029 scopus 로고    scopus 로고
    • Isolation of a carbon source-regulated gene from Ustilago maydis
    • Bottin A, Kamper J, Kahmann R (1996) Isolation of a carbon source-regulated gene from Ustilago maydis. Mol Gen Genet 253:342-352
    • (1996) Mol Gen Genet , vol.253 , pp. 342-352
    • Bottin, A.1    Kamper, J.2    Kahmann, R.3
  • 3
    • 0026681174 scopus 로고
    • A single amino-acid change in the iron-sulphur protein subunit of succinate dehydrogenase confers resistance to carboxin in Ustilago maydis
    • Broomfield PLE, Hargreaves JA (1992) A single amino-acid change in the iron-sulphur protein subunit of succinate dehydrogenase confers resistance to carboxin in Ustilago maydis. Curr Genet 22:117-121
    • (1992) Curr Genet , vol.22 , pp. 117-121
    • Broomfield, P.L.E.1    Hargreaves, J.A.2
  • 4
    • 0014149945 scopus 로고
    • Fungitoxic spectrum of oxanthiin compounds
    • Edgington LV, Baron GL (1967) Fungitoxic spectrum of oxanthiin compounds. Phytopathology 57:1256-1257
    • (1967) Phytopathology , vol.57 , pp. 1256-1257
    • Edgington, L.V.1    Baron, G.L.2
  • 5
    • 0015350825 scopus 로고
    • Genetic evidence for the action of oxathiin and thiazole derivatives on the succinate dehydrogenase system of Ustilago maydis mitochondria
    • Georgopoulos SG, Alexandri E, Chrysayi M (1972) Genetic evidence for the action of oxathiin and thiazole derivatives on the succinate dehydrogenase system of Ustilago maydis mitochondria. J Bacteriol 110:809-817
    • (1972) J Bacteriol , vol.110 , pp. 809-817
    • Georgopoulos, S.G.1    Alexandri, E.2    Chrysayi, M.3
  • 6
    • 9344232077 scopus 로고
    • Carboxin resistance in the haploid, the heterozygous diploid and the plant-parasitic dicaryotic phase of Ustilago maydis
    • Georgopoulos SG, Chrysayi M, White GA (1975) Carboxin resistance in the haploid, the heterozygous diploid and the plant-parasitic dicaryotic phase of Ustilago maydis. Pestic Biochem Physiol 5:543-551
    • (1975) Pestic Biochem Physiol , vol.5 , pp. 543-551
    • Georgopoulos, S.G.1    Chrysayi, M.2    White, G.A.3
  • 7
    • 0016803737 scopus 로고
    • Three genes determine the carboxin sensitivity of mitochondrial succinate oxidation in Aspergillus nidulans
    • Gunatilleke IAUN, Arst HN, Scazzocchio C (1976) Three genes determine the carboxin sensitivity of mitochondrial succinate oxidation in Aspergillus nidulans. Genet Res 26:297-305
    • (1976) Genet Res , vol.26 , pp. 297-305
    • Gunatilleke, I.A.U.N.1    Arst, H.N.2    Scazzocchio, C.3
  • 8
    • 0002949582 scopus 로고
    • The structure and organization of nuclear genes of filamentous fungi
    • Kinghorn, JR (ed) (1987) IRL Press, Oxford Washington
    • Gurr SJ, Unkles SE, Kinghorn JR (1987) The structure and organization of nuclear genes of filamentous fungi. In: Kinghorn, JR (ed) Gene structure in eukaryotic microbes (1987) IRL Press, Oxford Washington, pp 93-139
    • (1987) Gene Structure in Eukaryotic Microbes , pp. 93-139
    • Gurr, S.J.1    Unkles, S.E.2    Kinghorn, J.R.3
  • 9
    • 0029002342 scopus 로고
    • The trinuclear iron-sulfur cluster S3 in Bacillus subtilis succinate-menaquinone reductase - Effects of a mutation in the putative cluster ligation motif on enzyme activity and EPR properties
    • Hargerhall C, Sled V, Hederstedt L, Ohnishi T (1995) The trinuclear iron-sulfur cluster S3 in Bacillus subtilis succinate-menaquinone reductase - effects of a mutation in the putative cluster ligation motif on enzyme activity and EPR properties. Biochem Biophys Acta - Bioenergetics 1229:356-362
    • (1995) Biochem Biophys Acta - Bioenergetics , vol.1229 , pp. 356-362
    • Hargerhall, C.1    Sled, V.2    Hederstedt, L.3    Ohnishi, T.4
  • 10
    • 0002671043 scopus 로고
    • Gene transformation in plant pathogenic fungi
    • Gurr SJ, McPherson MJ, Bowles DJ (eds) IRL Press, Oxford Washington DC
    • Hargreaves JA, Turner G (1992) Gene transformation in plant pathogenic fungi. In: Gurr SJ, McPherson MJ, Bowles DJ (eds) Molecular plant pathology: a practical approach, Vol. 1. IRL Press, Oxford Washington DC, pp 79-98
    • (1992) Molecular Plant Pathology: A Practical Approach , vol.1 , pp. 79-98
    • Hargreaves, J.A.1    Turner, G.2
  • 11
    • 0000164862 scopus 로고
    • How proteins find mitochondria and intramitochondrial compartments
    • Hurt EC, van Loon AP (1986) How proteins find mitochondria and intramitochondrial compartments. Trends Biochem Sci 11:204-207
    • (1986) Trends Biochem Sci , vol.11 , pp. 204-207
    • Hurt, E.C.1    Van Loon, A.P.2
  • 12
    • 0032523087 scopus 로고    scopus 로고
    • Isolation and heterologous expression of a gene encoding 4-hydroxyphenylpyruvate dioxygenase from the wheat leaf-spot pathogen, Mycosphaerella graminicola
    • Keon J, Hargreaves J (1998) Isolation and heterologous expression of a gene encoding 4-hydroxyphenylpyruvate dioxygenase from the wheat leaf-spot pathogen, Mycosphaerella graminicola. FEMS Microbiol Lett 161:337-343
    • (1998) FEMS Microbiol Lett , vol.161 , pp. 337-343
    • Keon, J.1    Hargreaves, J.2
  • 13
    • 0025759021 scopus 로고
    • Isolation, characterization and sequence of a gene conferring resistance to the systemic fungicide carboxin from the maize smut pathogen, Ustilago maydis
    • Keon JPR, White GA, Hargreaves JA (1991) Isolation, characterization and sequence of a gene conferring resistance to the systemic fungicide carboxin from the maize smut pathogen, Ustilago maydis. Curr Genet 19:475-481
    • (1991) Curr Genet , vol.19 , pp. 475-481
    • Keon, J.P.R.1    White, G.A.2    Hargreaves, J.A.3
  • 14
    • 0025021310 scopus 로고
    • Human Complex II (succinate-ubiquinone oxidoreductase): CDNA cloning of an iron sulfur (Ip) subunit of liver mitochondria
    • Kita K, Oya H, Gennis RB, Ackrell BAC, Kasahara M (1990) Human Complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of an iron sulfur (Ip) subunit of liver mitochondria. Biochem Biophys Res Commun 166:101-108
    • (1990) Biochem Biophys Res Commun , vol.166 , pp. 101-108
    • Kita, K.1    Oya, H.2    Gennis, R.B.3    Ackrell, B.A.C.4    Kasahara, M.5
  • 16
    • 0025299986 scopus 로고
    • Cloning and characterization of the iron-sulfur subunit gene of succinate dehydrogenase from Saccharomyces cerevisiae
    • Lombardo A, Carine K, Scheffler IE (1990) Cloning and characterization of the iron-sulfur subunit gene of succinate dehydrogenase from Saccharomyces cerevisiae. J Biol Chem 265:10419-10423
    • (1990) J Biol Chem , vol.265 , pp. 10419-10423
    • Lombardo, A.1    Carine, K.2    Scheffler, I.E.3
  • 17
    • 13344278025 scopus 로고    scopus 로고
    • Two hydrophobic units are essential for the heme-b ligation and functional assembly of Complex II (succinate-ubiquinone oxidoreductase) from Escherichia coli
    • Nakamura K, Yamaki M, Sarada M, Nakayama S, Vibat CRT, Gennis RB, Nakayashiki T, Inokuchi H, Kojima S, Kita K (1996) Two hydrophobic units are essential for the heme-b ligation and functional assembly of Complex II (succinate-ubiquinone oxidoreductase) from Escherichia coli. J Biol Chem 271:521-527
    • (1996) J Biol Chem , vol.271 , pp. 521-527
    • Nakamura, K.1    Yamaki, M.2    Sarada, M.3    Nakayama, S.4    Vibat, C.R.T.5    Gennis, R.B.6    Nakayashiki, T.7    Inokuchi, H.8    Kojima, S.9    Kita, K.10
  • 18
    • 0026097299 scopus 로고
    • Involvement of a histidine residue in the interaction between membrane-anchoring proteins (Qps) and succinate dehydrogenase in mitochondrial succinate-ubiquinone reductase
    • Paudel HK, Yu Y, Yu C-A (1991) Involvement of a histidine residue in the interaction between membrane-anchoring proteins (Qps) and succinate dehydrogenase in mitochondrial succinate-ubiquinone reductase. Biochem Biophys Acta 1056:159-165
    • (1991) Biochem Biophys Acta , vol.1056 , pp. 159-165
    • Paudel, H.K.1    Yu, Y.2    Yu, C.-A.3
  • 19
    • 0028138965 scopus 로고
    • 556 in succinate:ubiquinone oxidoreductase from Escherichia coli
    • 556 in succinate:ubiquinone oxidoreductase from Escherichia coli. FEBS Lett 355:155-156
    • (1994) FEBS Lett , vol.355 , pp. 155-156
    • Peterson, J.1    Vilbat, C.2    Gennis, R.B.3
  • 20
    • 0023512725 scopus 로고
    • Transformation of Aspergillus based on the hygromycin-b resistance marker from Echerichia coli
    • Punt PJ, Oliver RP, Dingemanse MA, Pouwels PH, vandenHondel CAMJJ (1987) Transformation of Aspergillus based on the hygromycin-b resistance marker from Echerichia coli. Gene 56:117-124
    • (1987) Gene , vol.56 , pp. 117-124
    • Punt, P.J.1    Oliver, R.P.2    Dingemanse, M.A.3    Pouwels, P.H.4    VandenHondel, C.A.M.J.J.5
  • 21
    • 0014861568 scopus 로고
    • Metabolic effects related to fungi-toxicity of carboxin
    • Ragsdale NN, Sisler HD (1970) Metabolic effects related to fungi-toxicity of carboxin. Phytopathology 60:1422-1427
    • (1970) Phytopathology , vol.60 , pp. 1422-1427
    • Ragsdale, N.N.1    Sisler, H.D.2
  • 23
    • 0015333366 scopus 로고
    • Mode of action of oxathiin systemic fungicides. V. Effect on the electron transport system of Ustilago maydis and Saccharomyces cerevisiae
    • Ulrich JT, Mathre DE (1972) Mode of action of oxathiin systemic fungicides. V. Effect on the electron transport system of Ustilago maydis and Saccharomyces cerevisiae. J Bacteriol 110:628-632
    • (1972) J Bacteriol , vol.110 , pp. 628-632
    • Ulrich, J.T.1    Mathre, D.E.2
  • 24
    • 0002858205 scopus 로고
    • Gene organization in industrial filamentous fungi
    • Kinghorn JR, Turner G (eds) Blackie Academic and Professional, London Glasgow
    • Unkles SE (1992) Gene organization in industrial filamentous fungi. In: Kinghorn JR, Turner G (eds) Applied molecular genetics of filamentous fungi. Blackie Academic and Professional, London Glasgow, pp 28-53
    • (1992) Applied Molecular Genetics of Filamentous Fungi , pp. 28-53
    • Unkles, S.E.1
  • 25
    • 0030740917 scopus 로고    scopus 로고
    • Electron paramagnetic resonance of succinate:ubiquinone oxido-reductase from Paracoccus denitrificans - Evidence for a magnetic interaction between the 3Fe-4 S cluster and cytochrome b
    • Waldeck AR, Stowell MHB, Lee HK, Hung SC, Matsson M, Hederstedt L, Ackrell BAC, Chan SI (1997) Electron paramagnetic resonance of succinate:ubiquinone oxido-reductase from Paracoccus denitrificans - evidence for a magnetic interaction between the 3Fe-4 S cluster and cytochrome b. J Biol Chem 272:19373-19382
    • (1997) J Biol Chem , vol.272 , pp. 19373-19382
    • Waldeck, A.R.1    Stowell, M.H.B.2    Lee, H.K.3    Hung, S.C.4    Matsson, M.5    Hederstedt, L.6    Ackrell, B.A.C.7    Chan, S.I.8
  • 27
    • 84912706432 scopus 로고
    • Amino-acid sequence of the iron-sulfur protein subunit of beef heart succinate dehydrogenase
    • Matsubara H, Katsube Y, Wada K (eds) (1986) Japan Scientific Society Press, Tokyo/ Springer Verlag, Berlin
    • Yao Y, Wakabayashi S, Matsuda S, Matsubara H, Yu L, Yu C-A (1986) Amino-acid sequence of the iron-sulfur protein subunit of beef heart succinate dehydrogenase. In: Matsubara H, Katsube Y, Wada K (eds) Iron-sulfur protein research (1986) Japan Scientific Society Press, Tokyo/ Springer Verlag, Berlin, pp 240-244
    • (1986) Iron-sulfur Protein Research , pp. 240-244
    • Yao, Y.1    Wakabayashi, S.2    Matsuda, S.3    Matsubara, H.4    Yu, L.5    Yu, C.-A.6


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