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Volumn 171, Issue 2, 2011, Pages 123-131

Sequence Analysis and Structural Characterization of a Glyceraldehyde-3-Phosphate Dehydrogenase Gene from the Phytopathogenic Fungus Eremothecium ashbyi

Author keywords

Codon bias; Eremothecium ashbyi; Gene isolation; Glyceraldehyde 3 phosphate dehydrogenase; Homology model

Indexed keywords

ASCOMYCOTA; EREMOTHECIUM; EREMOTHECIUM ASHBYI; EREMOTHECIUM GOSSYPII; FUNGI; GLYCINE MAX; GOSSYPIUM HIRSUTUM;

EID: 78651385201     PISSN: 0301486X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11046-010-9357-7     Document Type: Article
Times cited : (5)

References (28)
  • 1
    • 48349085382 scopus 로고    scopus 로고
    • Eremothecium ashbyi causes soybean yeast-spot and is associated with stink bug, Riptortus clavatus
    • Kimura S, Tokumaru S, Kuge K. Eremothecium ashbyi causes soybean yeast-spot and is associated with stink bug, Riptortus clavatus. J Gen Plant Pathol. 2008; 74: 275-80.
    • (2008) J Gen Plant Pathol , vol.74 , pp. 275-280
    • Kimura, S.1    Tokumaru, S.2    Kuge, K.3
  • 2
    • 70349438735 scopus 로고    scopus 로고
    • Eremothecium coryli and E. ashbyi cause yeast spot of azuki bean
    • Kimura S, Tokumaru S, Kuge K. Eremothecium coryli and E. ashbyi cause yeast spot of azuki bean. J Gen Plant Pathol. 2009; 75: 322-4.
    • (2009) J Gen Plant Pathol , vol.75 , pp. 322-324
    • Kimura, S.1    Tokumaru, S.2    Kuge, K.3
  • 3
    • 0034091478 scopus 로고    scopus 로고
    • Three biotechnical processes using Ashbya gossypii, Candida famata or Bacillus subtilis compete with chemical riboflavin production
    • Stahmann KP, Revuelta JL, Seulberger H. Three biotechnical processes using Ashbya gossypii, Candida famata or Bacillus subtilis compete with chemical riboflavin production. Appl Microbiol Biotechnol. 2000; 53: 509-16.
    • (2000) Appl Microbiol Biotechnol , vol.53 , pp. 509-516
    • Stahmann, K.P.1    Revuelta, J.L.2    Seulberger, H.3
  • 4
    • 11144355642 scopus 로고    scopus 로고
    • The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome
    • Dietrich FS, Voegeli S, Brachat S, Lerch A, Gates K, Steiner S, et al. The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome. Science. 2004; 304: 304-7.
    • (2004) Science , vol.304 , pp. 304-307
    • Dietrich, F.S.1    Voegeli, S.2    Brachat, S.3    Lerch, A.4    Gates, K.5    Steiner, S.6
  • 5
    • 0037540048 scopus 로고    scopus 로고
    • Phylogenetic relationships among yeasts of the 'Saccharomyces complex' determined from multigene sequence analyses
    • Kurtzman CP, Robnett CJ. Phylogenetic relationships among yeasts of the 'Saccharomyces complex' determined from multigene sequence analyses. FEMS Yeast Res. 2003; 3: 417-32.
    • (2003) FEMS Yeast Res , vol.3 , pp. 417-432
    • Kurtzman, C.P.1    Robnett, C.J.2
  • 6
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • Sirover MA. New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim Biophys Acta. 1999; 1432: 159-84.
    • (1999) Biochim Biophys Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 7
    • 51649088881 scopus 로고    scopus 로고
    • Cloning and characterisation of the glyceraldehyde 3-phosphate dehydrogenase gene of Candida bombicola and use of its promoter
    • van Bogaert INA, De Maeseneire SL, Develter D, Soetaert W, Vandamme EJ. Cloning and characterisation of the glyceraldehyde 3-phosphate dehydrogenase gene of Candida bombicola and use of its promoter. J Ind Microbiol Biotechnol. 2008; 35: 1085-92.
    • (2008) J Ind Microbiol Biotechnol , vol.35 , pp. 1085-1092
    • van Bogaert, I.N.A.1    de Maeseneire, S.L.2    Develter, D.3    Soetaert, W.4    Vandamme, E.J.5
  • 8
    • 0033159364 scopus 로고    scopus 로고
    • Isolation and characterization of the glyceraldehyde-3-phosphate dehydrogenase gene of Lentinus edodes
    • Hirano T, Sato T, Okawa K, Kanda K, Yaegashi K, Enei H. Isolation and characterization of the glyceraldehyde-3-phosphate dehydrogenase gene of Lentinus edodes. Biosci Biotechnol Biochem. 1999; 63: 1223-7.
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 1223-1227
    • Hirano, T.1    Sato, T.2    Okawa, K.3    Kanda, K.4    Yaegashi, K.5    Enei, H.6
  • 9
    • 6944232058 scopus 로고    scopus 로고
    • Cloning of glyceraldehyde-3-phosphate dehydrogenase gene and use of the gpd promoter for transformation in Flammulina velutipes
    • Kuo CY, Chou SY, Huang CT. Cloning of glyceraldehyde-3-phosphate dehydrogenase gene and use of the gpd promoter for transformation in Flammulina velutipes. Appl Microbiol Biotechnol. 2004; 65: 593-9.
    • (2004) Appl Microbiol Biotechnol , vol.65 , pp. 593-599
    • Kuo, C.Y.1    Chou, S.Y.2    Huang, C.T.3
  • 10
    • 0025812548 scopus 로고
    • Genome analysis of imperfect fungi: electrophoretic karyotyping and characterization of the nuclear gene coding for glyceraldehyde-3-phosphate dehydrogenase (gpd) of Curvularia lunata
    • Osiewacz HD, Ridder R. Genome analysis of imperfect fungi: electrophoretic karyotyping and characterization of the nuclear gene coding for glyceraldehyde-3-phosphate dehydrogenase (gpd) of Curvularia lunata. Curr Genet. 1991; 20: 151-5.
    • (1991) Curr Genet , vol.20 , pp. 151-155
    • Osiewacz, H.D.1    Ridder, R.2
  • 11
    • 77951079485 scopus 로고    scopus 로고
    • Origin and fate of pseudogenes in Hemiascomycetes: a comparative analysis
    • Lafontaine I, Dujon B. Origin and fate of pseudogenes in Hemiascomycetes: a comparative analysis. BMC Genomics. 2010; 11: 260.
    • (2010) BMC Genomics , vol.11 , pp. 260
    • Lafontaine, I.1    Dujon, B.2
  • 12
    • 0024389002 scopus 로고
    • Human glyceraldehyde-3-phosphate dehydrogenase pseudogenes: molecular evolution and a possible mechanism for amplification
    • Arcari P, Martinelli R, Salvatore F. Human glyceraldehyde-3-phosphate dehydrogenase pseudogenes: molecular evolution and a possible mechanism for amplification. Biochem Genet. 1989; 27: 439-50.
    • (1989) Biochem Genet , vol.27 , pp. 439-450
    • Arcari, P.1    Martinelli, R.2    Salvatore, F.3
  • 13
    • 33845918427 scopus 로고    scopus 로고
    • The crystal and solution structures of glyceraldehyde-3-phosphate dehydrogenase reveal different quaternary structures
    • Ferreira-da-Silva F, Pereira PJB, Gales L, Roessle M, Svergun DI, Moradas Ferreira P, et al. The crystal and solution structures of glyceraldehyde-3-phosphate dehydrogenase reveal different quaternary structures. J Biol Chem. 2006; 281(44): 33433-40.
    • (2006) J Biol Chem , vol.281 , Issue.44 , pp. 33433-33440
    • Ferreira-Da-Silva, F.1    Pereira, P.J.B.2    Gales, L.3    Roessle, M.4    Svergun, D.I.5    Moradas, F.P.6
  • 16
    • 0019797407 scopus 로고
    • Evolutionary trees from DNA sequences: a maximum likelihood approach
    • Felsenstein J. Evolutionary trees from DNA sequences: a maximum likelihood approach. J Mol Evol. 1981; 17(6): 368-76.
    • (1981) J Mol Evol , vol.17 , Issue.6 , pp. 368-376
    • Felsenstein, J.1
  • 17
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A, Blundell TL. Comparative protein modeling by satisfaction of spatial restraints. J Mol Biol. 1993; 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 18
    • 3042581007 scopus 로고    scopus 로고
    • Flexible structure alignment by chaining aligned fragment pairs allowing twists
    • Yuzhen Y, Godzik A. Flexible structure alignment by chaining aligned fragment pairs allowing twists. Bioinformatics. 2003; 19(2): 246-55.
    • (2003) Bioinformatics , vol.19 , Issue.2 , pp. 246-255
    • Yuzhen, Y.1    Godzik, A.2
  • 19
  • 21
    • 0020024572 scopus 로고
    • Codon selection in yeast
    • Bennetzen JL, Hall BD. Codon selection in yeast. J Biol Chem. 1981; 257(6): 3026-31.
    • (1981) J Biol Chem , vol.257 , Issue.6 , pp. 3026-3031
    • Bennetzen, J.L.1    Hall, B.D.2
  • 22
    • 4043181283 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the glyceraldehyde-3-phosphate dehydrogenase gene from the zygomycetes fungus Rhizomucor miehei
    • Vastag M, Kasza Z, Ács K, Papp T, Schwab H. Cloning and sequence analysis of the glyceraldehyde-3-phosphate dehydrogenase gene from the zygomycetes fungus Rhizomucor miehei. Antonie Leeuwenhoek. 2004; 86: 111-9.
    • (2004) Antonie Leeuwenhoek , vol.86 , pp. 111-119
    • Vastag, M.1    Kasza, Z.2    Ács, K.3    Papp, T.4    Schwab, H.5
  • 23
    • 0033620625 scopus 로고    scopus 로고
    • Characterization of the glyceraldehyde-3-phosphate gene and the use of its promoter for heterologous expression in Cryptococcus neoformans, a human pathogen
    • Varma A, Kwon-Chung KJ. Characterization of the glyceraldehyde-3-phosphate gene and the use of its promoter for heterologous expression in Cryptococcus neoformans, a human pathogen. Gene. 1999; 232: 155-63.
    • (1999) Gene , vol.232 , pp. 155-163
    • Varma, A.1    Kwon-Chung, K.J.2
  • 24
    • 0031949299 scopus 로고    scopus 로고
    • Catalytically active monomers of E. coli glyceraldehyde-3-phosphate dehydrogenase
    • Levashov PA, Muronetz VI, Klyachko NL, Nagradova NK. Catalytically active monomers of E. coli glyceraldehyde-3-phosphate dehydrogenase. J Prot Chem. 1998; 17(3): 229-35.
    • (1998) J Prot Chem , vol.17 , Issue.3 , pp. 229-235
    • Levashov, P.A.1    Muronetz, V.I.2    Klyachko, N.L.3    Nagradova, N.K.4
  • 25
    • 33947106626 scopus 로고    scopus 로고
    • Cloning and sequence analysis of a glyceraldehyde-3-phosphate dehydrogenase gene from Ganoderma lucidum
    • Fei X, Zhao MW, Li YX. Cloning and sequence analysis of a glyceraldehyde-3-phosphate dehydrogenase gene from Ganoderma lucidum. J Microbiol. 2006; 44(5): 515-22.
    • (2006) J Microbiol , vol.44 , Issue.5 , pp. 515-522
    • Fei, X.1    Zhao, M.W.2    Li, Y.X.3
  • 26
    • 0346155809 scopus 로고    scopus 로고
    • PSEUDOGENES: Are they "Junk"or functional DNA?
    • Balakirev ES, Ayala FJ. PSEUDOGENES: are they "Junk"or functional DNA? Annu Rev Genet. 2003; 37: 123-51.
    • (2003) Annu Rev Genet , vol.37 , pp. 123-151
    • Balakirev, E.S.1    Ayala, F.J.2
  • 27
    • 70449552832 scopus 로고    scopus 로고
    • A Statistical model of protein sequence similarity and function similarity reveals overly-specific function predictions
    • doi: 10. 1371/journal. pone. 0007546pmid: 19844580
    • Louie B, Higdon R, Kolker E. A Statistical model of protein sequence similarity and function similarity reveals overly-specific function predictions. PLoS ONE. 2009; 4: e7546. doi: 10. 1371/journal. pone. 0007546pmid: 19844580.
    • (2009) PLoS ONE , vol.4 , pp. 7546
    • Louie, B.1    Higdon, R.2    Kolker, E.3
  • 28
    • 52649091290 scopus 로고    scopus 로고
    • Phosphoribosyl pyrophosphate synthetase activity affects growth and riboflavin production in Ashbya gossypii
    • Jiménez A, Santos MA, Revuelta JL. Phosphoribosyl pyrophosphate synthetase activity affects growth and riboflavin production in Ashbya gossypii. BMC Biotechnol. 2008; 8: 67.
    • (2008) BMC Biotechnol , vol.8 , pp. 67
    • Jiménez, A.1    Santos, M.A.2    Revuelta, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.