메뉴 건너뛰기




Volumn 8, Issue 2, 2009, Pages 194-203

Isolation and characterization of glyceraldehyde-3-phosphate dehydrogenase gene of Trichoderma virens UKM1

Author keywords

Glyceraldehyde 3 phosphate dehydrogenase; Promoter; Trichoderma virens

Indexed keywords

AMINO ACID SEQUENCE; CDNA SEQUENCE; DNA WALKING; EXPRESSED SEQUENCE TAGS; FILAMENTOUS FUNGI; FLANKING REGIONS; FLANKING SEQUENCE; GENE SEQUENCES; GENETIC TOOLS; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; HETEROLOGOUS GENES; ISOLATION AND CHARACTERIZATION; NON-CODING REGION; OPEN READING FRAME; PHYLOGENETIC ANALYSIS; POLYPEPTIDE CHAIN; PROMOTER; REVERSE TRANSCRIPTION-POLYMERASE CHAIN REACTION; SEQUENCE COMPARISONS; TRANSCRIPTION START SITE; TRICHODERMA VIRENS;

EID: 68049135796     PISSN: 1682296X     EISSN: 16822978     Source Type: Journal    
DOI: 10.3923/biotech.2009.194.203     Document Type: Article
Times cited : (10)

References (40)
  • 1
    • 67349133467 scopus 로고    scopus 로고
    • Effect of agitation and aeration rates on chitinase production Using Trichoderma virens UKM1 in 2-1 stirred tank reactor
    • Abd-Aziz, S., C. C. Fernandez, M. M. Salleh, R. M. Illias and M. A. Hassan, 2008a. Effect of agitation and aeration rates on chitinase production Using Trichoderma virens UKM1 in 2-1 stirred tank reactor. Applied Biochem. Biotechnol., 150:193-204.
    • (2008) Applied Biochem. Biotechnol , vol.150 , pp. 193-204
    • Abd-Aziz, S.1    Fernandez, C.C.2    Salleh, M.M.3    Illias, R.M.4    Hassan, M.A.5
  • 2
    • 42449142998 scopus 로고    scopus 로고
    • Microbial degradation of chitin materials by Trichoderma virens UKM1
    • Abd-Aziz, S., L. S. Teoh, N. Alitheen, N. Shahab and K. Kamaruddin, 2008b. Microbial degradation of chitin materials by Trichoderma virens UKM1. J. Biol. Sci., 8:52-59.
    • (2008) J. Biol. Sci , vol.8 , pp. 52-59
    • Abd-Aziz, S.1    Teoh, L.S.2    Alitheen, N.3    Shahab, N.4    Kamaruddin, K.5
  • 3
    • 0033057503 scopus 로고    scopus 로고
    • The role of extracellular chitinase from Trichoderma virens Gv29-8 in the biocontrol of Rhizoctonia solani
    • Baek, J. M., C. R. Howell and C. M. Kenerley, 1999. The role of extracellular chitinase from Trichoderma virens Gv29-8 in the biocontrol of Rhizoctonia solani. Curr. Genet., 35:41-50.
    • (1999) Curr. Genet , vol.35 , pp. 41-50
    • Baek, J.M.1    Howell, C.R.2    Kenerley, C.M.3
  • 4
    • 29644437769 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase of Paracoccidioides brasiliensis is a cell surface protein involved in fungal adhesion to extracellular matrix proteins and interaction with cells
    • Barbosa, M. S., S. N. Ba'o, P. F. Andreotti, F. P. De Faria, M. S. S. Felipe, L. D. S. Feitosa, M. J. S. Mendes-Giannini and C. M. D. A. Soares, 2006. Glyceraldehyde-3-phosphate dehydrogenase of Paracoccidioides brasiliensis is a cell surface protein involved in fungal adhesion to extracellular matrix proteins and interaction with cells. Infect. Immunol., 74:382-389.
    • (2006) Infect. Immunol , vol.74 , pp. 382-389
    • Barbosa, M.S.1    Ba'o, S.N.2    Andreotti, P.F.3    De Faria, F.P.4    Felipe, M.S.S.5    Feitosa, L.D.S.6    Mendes-Giannini, M.J.S.7    Soares, C.M.D.A.8
  • 6
    • 33746225243 scopus 로고    scopus 로고
    • Sml, a proteinaceous elicitor secreted by the biocontrol fungus Trichoderma virens induces plant defense responses and systemic resistance
    • Djonovic, S., M. Pozo, L. J. Dangott, C. R. Howell and CM. Kenerley, 2006. Sml, a proteinaceous elicitor secreted by the biocontrol fungus Trichoderma virens induces plant defense responses and systemic resistance. Mol. Plant Microbe Interact, 19:838-853.
    • (2006) Mol. Plant Microbe Interact , vol.19 , pp. 838-853
    • Djonovic, S.1    Pozo, M.2    Dangott, L.J.3    Howell, C.R.4    Kenerley, C.M.5
  • 7
    • 15944405006 scopus 로고    scopus 로고
    • Phylogenetic divergence in a local population of the ectomycorrhizal fungus Cenococcum geophilum
    • Douhan, G. W. and D. M. Rizzo, 2005. Phylogenetic divergence in a local population of the ectomycorrhizal fungus Cenococcum geophilum. New Phytol., 166:263-271.
    • (2005) New Phytol , vol.166 , pp. 263-271
    • Douhan, G.W.1    Rizzo, D.M.2
  • 8
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson, O., S. Brunak, G. von Heijne and H. Nielsen, 2007. Locating proteins in the cell using TargetP, SignalP and related tools. Nat. Protocols, 2:953-971.
    • (2007) Nat. Protocols , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 9
    • 33947106626 scopus 로고    scopus 로고
    • Cloning and sequence analysis of a glyceraldehyde-3-phosphate dehydrogenase gene from Ganoderma lucidum
    • Fei, X., M. W. Zhao and Y. X. Li, 2006. Cloning and sequence analysis of a glyceraldehyde-3-phosphate dehydrogenase gene from Ganoderma lucidum. J. Microbiol., 44:512-522.
    • (2006) J. Microbiol , vol.44 , pp. 512-522
    • Fei, X.1    Zhao, M.W.2    Li, Y.X.3
  • 10
    • 0030034795 scopus 로고    scopus 로고
    • A Hidden Markov Model approach to variation among sites in rates of evolution
    • Felsenstein, J. and G. A. Churchill, 1996. A Hidden Markov Model approach to variation among sites in rates of evolution. Mol. Biol. Evol., 13:93-104.
    • (1996) Mol. Biol. Evol , vol.13 , pp. 93-104
    • Felsenstein, J.1    Churchill, G.A.2
  • 11
    • 24944575227 scopus 로고    scopus 로고
    • Commercialization and implementation of biocontrol
    • Fravel, D., 2005. Commercialization and implementation of biocontrol. Annu. Rev. Phytopathol., 43:337-359.
    • (2005) Annu. Rev. Phytopathol , vol.43 , pp. 337-359
    • Fravel, D.1
  • 12
    • 0024358130 scopus 로고    scopus 로고
    • The major parasite surface antigen associated with human resistence to schistosomiasis is a 37 kDa glyceraldehyde-3-P-dehydrogenase
    • Goudout-Crozel, V., D. Caillol, M. Djabali and A. J. Dessein, 2004. The major parasite surface antigen associated with human resistence to schistosomiasis is a 37 kDa glyceraldehyde-3-P-dehydrogenase. J. Exp. Med., 170:2065-2074.
    • (2004) J. Exp. Med , vol.170 , pp. 2065-2074
    • Goudout-Crozel, V.1    Caillol, D.2    Djabali, M.3    Dessein, A.J.4
  • 13
    • 33645716883 scopus 로고    scopus 로고
    • Cloning and characterization of a tyrosinase gene from the white-rot fungus Pycnoporus sanguineus and overproduction of the recombinant protein in Aspergillus niger
    • Halaouli, S., E. Record, L. Casalot, M. Hamdi, J. C. Sigoillot, M. Asther and A. Lomascolo, 2006. Cloning and characterization of a tyrosinase gene from the white-rot fungus Pycnoporus sanguineus and overproduction of the recombinant protein in Aspergillus niger. Applied Microbiol. Biotechnol., 70:580-589.
    • (2006) Applied Microbiol. Biotechnol , vol.70 , pp. 580-589
    • Halaouli, S.1    Record, E.2    Casalot, L.3    Hamdi, M.4    Sigoillot, J.C.5    Asther, M.6    Lomascolo, A.7
  • 15
    • 0026440132 scopus 로고
    • Sequence analysis of the glyceraldehyde-3- phosphate dehydrogenase genes from the basidiomycetes Schizophyllum commune, Phanerochaete chrysosporium and Agaricus bisporus
    • Harmsen, M. C., F. H. J. Schuren, S. M. Moukha, CM. Van Zuilen, P. J. Punt and J. G. H. Wessels, 1992. Sequence analysis of the glyceraldehyde-3- phosphate dehydrogenase genes from the basidiomycetes Schizophyllum commune, Phanerochaete chrysosporium and Agaricus bisporus. Curr. Genet., 22:447-454.
    • (1992) Curr. Genet , vol.22 , pp. 447-454
    • Harmsen, M.C.1    Schuren, F.H.J.2    Moukha, S.M.3    Van Zuilen, C.M.4    Punt, P.J.5    Wessels, J.G.H.6
  • 16
    • 0018679538 scopus 로고
    • The primary structure of a glyceraldehyde-3-phosphate dehydrogenase gene from Saccharomyces cerevisiae
    • Holland, J. P. and M. J. Holland, 1979. The primary structure of a glyceraldehyde-3-phosphate dehydrogenase gene from Saccharomyces cerevisiae. J. Biol. Chem., 254:9839-9845.
    • (1979) J. Biol. Chem , vol.254 , pp. 9839-9845
    • Holland, J.P.1    Holland, M.J.2
  • 17
    • 0032834582 scopus 로고    scopus 로고
    • Trichoderma virens-inoculated composted chicken manure for biological weed control
    • Hutchinson, C. M., 1999. Trichoderma virens-inoculated composted chicken manure for biological weed control. Biol. Control, 16:217-222.
    • (1999) Biol. Control , vol.16 , pp. 217-222
    • Hutchinson, C.M.1
  • 18
    • 0345393195 scopus 로고    scopus 로고
    • Molecular markers reveal genetic isolation and phylogeography of the S and F intersterility groups of the wood-decay fungus Heterobasidium annosum
    • Johannesson, H. and J. Stenlid, 2003. Molecular markers reveal genetic isolation and phylogeography of the S and F intersterility groups of the wood-decay fungus Heterobasidium annosum. Mol. Phylogenet. Evol., 29:94-101.
    • (2003) Mol. Phylogenet. Evol , vol.29 , pp. 94-101
    • Johannesson, H.1    Stenlid, J.2
  • 19
    • 33745168682 scopus 로고    scopus 로고
    • Comparison of GPD genes and their protein products in basidiomycetes
    • Kilaru, S. and U. Kües, 2005. Comparison of GPD genes and their protein products in basidiomycetes. Fungal Genet. Newslett., 52:18-23.
    • (2005) Fungal Genet. Newslett , vol.52 , pp. 18-23
    • Kilaru, S.1    Kües, U.2
  • 20
    • 0024546509 scopus 로고
    • The scanning model for translation: An update
    • Kozak, M., 1989. The scanning model for translation: An update. J. Cell Biol., 108:229-241.
    • (1989) J. Cell Biol , vol.108 , pp. 229-241
    • Kozak, M.1
  • 21
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar, S., K. Tamura and M. Nei, 2004. MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinform., 5:150-163.
    • (2004) Brief. Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 22
    • 34250341196 scopus 로고    scopus 로고
    • Cloning, characterization and computational analysis of the 5' regulatory region of ovine glucose 6-phosphate dehydrogenase gene
    • Laliotis, G. P., I. Bizelis, A. Argyrokastritis and E. Rogdakis, 2007. Cloning, characterization and computational analysis of the 5' regulatory region of ovine glucose 6-phosphate dehydrogenase gene. Comp. Biochem. Physiol. Biochem. Mol. Biol., 147:627-634.
    • (2007) Comp. Biochem. Physiol. Biochem. Mol. Biol , vol.147 , pp. 627-634
    • Laliotis, G.P.1    Bizelis, I.2    Argyrokastritis, A.3    Rogdakis, E.4
  • 23
    • 36448991500 scopus 로고    scopus 로고
    • Larkin, M. A, G. Blackshields, N. P. Brown, R. Chenna and P. A McGettigan et al, 2007. Clustal W and Clustal X version 2.0. Bioinformatics, 23:2947-2948
    • Larkin, M. A., G. Blackshields, N. P. Brown, R. Chenna and P. A McGettigan et al., 2007. Clustal W and Clustal X version 2.0. Bioinformatics, 23:2947-2948.
  • 24
    • 1642576432 scopus 로고    scopus 로고
    • Characterization of the Mucor circinelloides regulated promoter GPDlp
    • Larsen, G. G., K. F. Appel, A. M. Wolff, J. Nielsen and J. Arnau, 2004. Characterization of the Mucor circinelloides regulated promoter GPDlp. Curr. Genet., 45:225-234.
    • (2004) Curr. Genet , vol.45 , pp. 225-234
    • Larsen, G.G.1    Appel, K.F.2    Wolff, A.M.3    Nielsen, J.4    Arnau, J.5
  • 25
    • 1642277932 scopus 로고    scopus 로고
    • Functional production and secretion of the Gluconacetobacter diazotrophicus fructosereleasing exo-levanase (LsdB) in Pichia pastoris
    • Menéndez, C., L. Herna'ndez, A. Banguela and J. Pai's, 2004. Functional production and secretion of the Gluconacetobacter diazotrophicus fructosereleasing exo-levanase (LsdB) in Pichia pastoris. Enzyme Microbial. Technol., 34:446-452.
    • (2004) Enzyme Microbial. Technol , vol.34 , pp. 446-452
    • Menéndez, C.1    Herna'ndez, L.2    Banguela, A.3    Pai's, J.4
  • 26
    • 0035640164 scopus 로고    scopus 로고
    • Application of Burkholderia cepacia and Trichoderma virens, alone and in combinations, against Meloidogyne incognita on bell pepper
    • Meyer, S. L. F., D. P. Roberts, D. J. Chitwood, L. K. Carta, R. D. Lumsden and W. L. Mao, 2001. Application of Burkholderia cepacia and Trichoderma virens, alone and in combinations, against Meloidogyne incognita on bell pepper. Nematropica, 31:75-86.
    • (2001) Nematropica , vol.31 , pp. 75-86
    • Meyer, S.L.F.1    Roberts, D.P.2    Chitwood, D.J.3    Carta, L.K.4    Lumsden, R.D.5    Mao, W.L.6
  • 27
    • 0032975361 scopus 로고    scopus 로고
    • The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase
    • Modun, B. and P. Williams, 1999. The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase. Infect. Immunol, 67:1086-1092.
    • (1999) Infect. Immunol , vol.67 , pp. 1086-1092
    • Modun, B.1    Williams, P.2
  • 28
    • 3042631009 scopus 로고    scopus 로고
    • Molecular cloning of the promoter region of the glyceraldehyde-3-phosphate dehydrogenase gene that contributes to the construction of a new transformation system in Coriolus versicolor
    • Nitta, Y., Y. Miyazaki, M. Nakamura, Y. Iimura, K. Shishido, S. Kajita and N. Morohoshi, 2004. Molecular cloning of the promoter region of the glyceraldehyde-3-phosphate dehydrogenase gene that contributes to the construction of a new transformation system in Coriolus versicolor. Mycoscience, 45:131-136.
    • (2004) Mycoscience , vol.45 , pp. 131-136
    • Nitta, Y.1    Miyazaki, Y.2    Nakamura, M.3    Iimura, Y.4    Shishido, K.5    Kajita, S.6    Morohoshi, N.7
  • 29
    • 0016828716 scopus 로고
    • Sequence variability and structure of D glyceraldehyde-3-phosphate dehydrogenase
    • Olsen, K. W., D. Moras and M. G. Rossmann, 1975. Sequence variability and structure of D glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem., 250:9313-9321.
    • (1975) J. Biol. Chem , vol.250 , pp. 9313-9321
    • Olsen, K.W.1    Moras, D.2    Rossmann, M.G.3
  • 30
    • 0027171158 scopus 로고
    • Mediprep method for isolation of DNA from plant samples with a high content of polyphenolics
    • Pich, U. and I. Schubert 1993. Mediprep method for isolation of DNA from plant samples with a high content of polyphenolics. Nucl. Acids Res., 21:3328-3328.
    • (1993) Nucl. Acids Res , vol.21 , pp. 3328-3328
    • Pich, U.1    Schubert, I.2
  • 31
    • 0023777869 scopus 로고
    • Isolation and characterization of the glyceraldehyde-3-phosphate dehydrogenase gene of Aspergillus nidulans
    • Punt, P. J., M. A. Dingemanse, B. J. M. Jacobs-Meijsing, P. H. Pouwels, C. A. M. J. J. van den Hondel, 1988. Isolation and characterization of the glyceraldehyde-3-phosphate dehydrogenase gene of Aspergillus nidulans. Gene, 69:49-57.
    • (1988) Gene , vol.69 , pp. 49-57
    • Punt, P.J.1    Dingemanse, M.A.2    Jacobs-Meijsing, B.J.M.3    Pouwels, P.H.4    van den Hondel, C.A.M.J.J.5
  • 33
    • 0024728477 scopus 로고
    • Disparate evolution of yeasts and filamentous fungi indicated by phylogenetic analysis of glyceraldehyde-3-phosphate dehydrogenase genes
    • Smith, T. L., 1989. Disparate evolution of yeasts and filamentous fungi indicated by phylogenetic analysis of glyceraldehyde-3-phosphate dehydrogenase genes. Proc. Natl. Acad. Sci. USA., 86:7063-7066.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7063-7066
    • Smith, T.L.1
  • 34
    • 0025052577 scopus 로고
    • Isolation and characterization of an Ustilago maydis glyceraldehyde-3-phosphate dehydrogenaseencoding gene
    • Smith, T. L. and S. A. Leong, 1990. Isolation and characterization of an Ustilago maydis glyceraldehyde-3-phosphate dehydrogenaseencoding gene. Gene, 93:111-117.
    • (1990) Gene , vol.93 , pp. 111-117
    • Smith, T.L.1    Leong, S.A.2
  • 36
    • 0026448561 scopus 로고
    • Cloning and molecular characterization of the glyceraldehyde-3-phosphate dehydrogenase-encoding gene and cDNA from the plant pathogenic fungus Glomerella cingulata
    • Templeton, M. D., E. H. Rikkerink, S. L. Solon and R. N. Crowhurst, 1992. Cloning and molecular characterization of the glyceraldehyde-3-phosphate dehydrogenase-encoding gene and cDNA from the plant pathogenic fungus Glomerella cingulata. Gene, 122:225-230.
    • (1992) Gene , vol.122 , pp. 225-230
    • Templeton, M.D.1    Rikkerink, E.H.2    Solon, S.L.3    Crowhurst, R.N.4
  • 37
    • 0035371191 scopus 로고    scopus 로고
    • Expression of hepatitis B surface antigen in the methylotrophic yeast Pichia pastoris using the GAP promoter
    • Vassileva, A., D. A. Chugh, S. Swaminathan and N. Khanna, 2001. Expression of hepatitis B surface antigen in the methylotrophic yeast Pichia pastoris using the GAP promoter. J. Biotechnol., 88:21-35.
    • (2001) J. Biotechnol , vol.88 , pp. 21-35
    • Vassileva, A.1    Chugh, D.A.2    Swaminathan, S.3    Khanna, N.4
  • 38
    • 4043181283 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the glyceraldehyde-3-phosphate dehydrogenase gene from the zygomycetes fungus Rhizomucor miehei
    • Vastag, M., Z. Kasza, K. ACS, T. Papp, H. Schwab and C. Vagvolgyi, 2004. Cloning and sequence analysis of the glyceraldehyde-3-phosphate dehydrogenase gene from the zygomycetes fungus Rhizomucor miehei. Antonie van Leeuwenhoek, 86:111-119.
    • (2004) Antonie van Leeuwenhoek , vol.86 , pp. 111-119
    • Vastag, M.1    Kasza, Z.2    ACS, K.3    Papp, T.4    Schwab, H.5    Vagvolgyi, C.6
  • 39
    • 0008146244 scopus 로고    scopus 로고
    • 3'-End processes of pre-mRNA in eukaryotes
    • Wahle, E. and U. Ruegsegger, 1999. 3'-End processes of pre-mRNA in eukaryotes. FEMS Microbiol. Rev., 23:277-295.
    • (1999) FEMS Microbiol. Rev , vol.23 , pp. 277-295
    • Wahle, E.1    Ruegsegger, U.2
  • 40
    • 0029949052 scopus 로고    scopus 로고
    • Enhanced expression of a bacterial gene for pesticide degradation in a common soil fungus
    • Xu, B., J. R. Wild and CM. Kenerley, 1996. Enhanced expression of a bacterial gene for pesticide degradation in a common soil fungus. J. Ferment. Bioeng., 81:473-481.
    • (1996) J. Ferment. Bioeng , vol.81 , pp. 473-481
    • Xu, B.1    Wild, J.R.2    Kenerley, C.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.