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Volumn 7, Issue 5, 2012, Pages

Disruption of the Eng18b ENGase gene in the fungal biocontrol agent Trichoderma atroviride affects growth, conidiation and antagonistic ability

Author keywords

[No Author keywords available]

Indexed keywords

N ACETYL BETA GLUCOSAMINIDASE; CHITIN; GLYCOPROTEIN; GLYCOSIDASE;

EID: 84860636100     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0036152     Document Type: Article
Times cited : (37)

References (50)
  • 2
    • 0015973205 scopus 로고
    • The release of intact oligosaccharides from specific glycoproteins by endo-beta-N-acetylglucosaminidase H
    • Tarentino AL, Plummer TH Jr, Maley F, (1974) The release of intact oligosaccharides from specific glycoproteins by endo-beta-N-acetylglucosaminidase H. J Biol Chem 249: 818-824.
    • (1974) J Biol Chem , vol.249 , pp. 818-824
    • Tarentino, A.L.1    Plummer Jr., T.H.2    Maley, F.3
  • 3
    • 7044274809 scopus 로고    scopus 로고
    • Molecular cloning of Mucor hiemalis endo-beta-N-acetylglucosaminidase and some properties of the recombinant enzyme
    • Fujita K, Kobayashi K, Iwamatsu A, Takeuchi M, Kumagai H, et al. (2004) Molecular cloning of Mucor hiemalis endo-beta-N-acetylglucosaminidase and some properties of the recombinant enzyme. Arch Biochem Biophys 432: 41-49.
    • (2004) Arch Biochem Biophys , vol.432 , pp. 41-49
    • Fujita, K.1    Kobayashi, K.2    Iwamatsu, A.3    Takeuchi, M.4    Kumagai, H.5
  • 4
    • 74349123190 scopus 로고    scopus 로고
    • Identification of a gene coding for a deglycosylating enzyme in Hypocrea jecorina
    • Stals I, Samyn B, Sergeant K, White T, Hoorelbeke K, et al. (2010) Identification of a gene coding for a deglycosylating enzyme in Hypocrea jecorina. Fems Microbiol Lett 303: 9-17.
    • (2010) Fems Microbiol Lett , vol.303 , pp. 9-17
    • Stals, I.1    Samyn, B.2    Sergeant, K.3    White, T.4    Hoorelbeke, K.5
  • 5
    • 77952295841 scopus 로고    scopus 로고
    • Purification, characterization and molecular cloning of a novel endo-beta-N-acetylglucosaminidase from the basidiomycete, Flammulina velutipes
    • Hamaguchi T, Ito T, Inoue Y, Limpaseni T, Pongsawasdi P, et al. (2010) Purification, characterization and molecular cloning of a novel endo-beta-N-acetylglucosaminidase from the basidiomycete, Flammulina velutipes. Glycobiology 20: 420-432.
    • (2010) Glycobiology , vol.20 , pp. 420-432
    • Hamaguchi, T.1    Ito, T.2    Inoue, Y.3    Limpaseni, T.4    Pongsawasdi, P.5
  • 6
    • 41749111783 scopus 로고    scopus 로고
    • Comparative evolutionary histories of the fungal chitinase gene family reveal non-random size expansions and contractions due to adaptive natural selection
    • Karlsson M, Stenlid J, (2008) Comparative evolutionary histories of the fungal chitinase gene family reveal non-random size expansions and contractions due to adaptive natural selection. Evol Bioinform 4: 47-60.
    • (2008) Evol Bioinform , vol.4 , pp. 47-60
    • Karlsson, M.1    Stenlid, J.2
  • 7
    • 60149095281 scopus 로고    scopus 로고
    • Evolution of family 18 glycoside hydrolases: Diversity, domain structures and phylogenetic relationships
    • Karlsson M, Stenlid J, (2009) Evolution of family 18 glycoside hydrolases: Diversity, domain structures and phylogenetic relationships. J Mol Microbiol Biotechnol 16: 208-223.
    • (2009) J Mol Microbiol Biotechnol , vol.16 , pp. 208-223
    • Karlsson, M.1    Stenlid, J.2
  • 8
    • 77951266103 scopus 로고    scopus 로고
    • Comparative molecular evolution of Trichoderma chitinases in response to mycoparasitic interactions
    • Ihrmark K, Asmail N, Ubhayasekera W, Melin P, Stenlid J, et al. (2010) Comparative molecular evolution of Trichoderma chitinases in response to mycoparasitic interactions. Evol Bioinform 6: 1-26.
    • (2010) Evol Bioinform , vol.6 , pp. 1-26
    • Ihrmark, K.1    Asmail, N.2    Ubhayasekera, W.3    Melin, P.4    Stenlid, J.5
  • 9
    • 84863711034 scopus 로고    scopus 로고
    • Free N-linked oligosaccharide chains: formation and degradation
    • Suzuki T, Funakoshi Y, (2006) Free N-linked oligosaccharide chains: formation and degradation. Glycoconj J 23: 291-302.
    • (2006) Glycoconj J , vol.23 , pp. 291-302
    • Suzuki, T.1    Funakoshi, Y.2
  • 10
    • 40549122304 scopus 로고    scopus 로고
    • Free oligosaccharide regulation during mammalian protein N-glycosylation
    • Chantret I, Moore SE, (2008) Free oligosaccharide regulation during mammalian protein N-glycosylation. Glycobiology 18: 210-224.
    • (2008) Glycobiology , vol.18 , pp. 210-224
    • Chantret, I.1    Moore, S.E.2
  • 12
    • 0025426605 scopus 로고
    • Biochemical and genetic analysis of an alpha-mannosidase mutant from Saccharomyces cerevisiae
    • Cueva R, Bordallo C, Suarez Rendueles P, (1990) Biochemical and genetic analysis of an alpha-mannosidase mutant from Saccharomyces cerevisiae. Fems Microbiol Lett 57: 153-157.
    • (1990) Fems Microbiol Lett , vol.57 , pp. 153-157
    • Cueva, R.1    Bordallo, C.2    Suarez Rendueles, P.3
  • 13
    • 0345687346 scopus 로고    scopus 로고
    • The genetic basis of cellular morphogenesis in the filamentous fungus Neurospora crassa
    • Seiler S, Plamann M, (2003) The genetic basis of cellular morphogenesis in the filamentous fungus Neurospora crassa. Mol Biol Cell 14: 4352-4364.
    • (2003) Mol Biol Cell , vol.14 , pp. 4352-4364
    • Seiler, S.1    Plamann, M.2
  • 14
    • 77449127431 scopus 로고    scopus 로고
    • The Neurospora peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity
    • Maerz S, Funakoshi Y, Negishi Y, Suzuki T, Seiler S, (2010) The Neurospora peptide:N-glycanase ortholog PNG1 is essential for cell polarity despite its lack of enzymatic activity. J Biol Chem 285: 2326-2332.
    • (2010) J Biol Chem , vol.285 , pp. 2326-2332
    • Maerz, S.1    Funakoshi, Y.2    Negishi, Y.3    Suzuki, T.4    Seiler, S.5
  • 15
    • 0000163023 scopus 로고    scopus 로고
    • Trichoderma and Gliocladium in biological control: an overview
    • In: Harman GE, Kubicek CP, editors
    • Hjeljord L, Tronsmo A, (1998) Trichoderma and Gliocladium in biological control: an overview. In: Harman GE, Kubicek CP, editors. Trichoderma and Gliocladium: Taylor and Francis pp. 131-151.
    • (1998) Trichoderma and Gliocladium: Taylor and Francis , pp. 131-151
    • Hjeljord, L.1    Tronsmo, A.2
  • 16
    • 58149194624 scopus 로고    scopus 로고
    • SMART 6: recent updates and new developments
    • Bork P, Letunic I, Doerks T, (2009) SMART 6: recent updates and new developments. Nucleic Acids Res 37: D229-D232.
    • (2009) Nucleic Acids Res , vol.37
    • Bork, P.1    Letunic, I.2    Doerks, T.3
  • 20
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh A, Larsson B, von Heijne G, Sonnhammer ELL, (2001) Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. J Mol Biol 305: 567-580.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.L.4
  • 21
    • 1442348239 scopus 로고    scopus 로고
    • A sensitive predictor for potential GPI lipid modification sites in fungal protein sequences and its application to genome-wide studies for Aspergillus nidulans, Candida albicans, Neurospora crassa, Saccharomyces cerevisiae and Schizosaccharomyces pombe
    • Eisenhaber B, Schneider G, Wildpaner M, Eisenhaber F, (2004) A sensitive predictor for potential GPI lipid modification sites in fungal protein sequences and its application to genome-wide studies for Aspergillus nidulans, Candida albicans, Neurospora crassa, Saccharomyces cerevisiae and Schizosaccharomyces pombe. J Mol Biol 337: 243-253.
    • (2004) J Mol Biol , vol.337 , pp. 243-253
    • Eisenhaber, B.1    Schneider, G.2    Wildpaner, M.3    Eisenhaber, F.4
  • 23
    • 41049103102 scopus 로고    scopus 로고
    • Reverse conservation analysis reveals the specificity determining residues of cytochrome P450 family 2 (CYP 2)
    • Lee T, (2008) Reverse conservation analysis reveals the specificity determining residues of cytochrome P450 family 2 (CYP 2). Evol Bioinform 4: 7-16.
    • (2008) Evol Bioinform , vol.4 , pp. 7-16
    • Lee, T.1
  • 25
    • 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, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 27
    • 0004293491 scopus 로고    scopus 로고
    • The PyMOL User's Manual
    • San Carlos, DeLano Scientific
    • DeLano WL, (2002) The PyMOL User's Manual. San Carlos DeLano Scientific.
    • (2002)
    • DeLano, W.L.1
  • 28
    • 0001963674 scopus 로고
    • A convenient growth medium for Neurospora (medium N)
    • Vogel HJ, (1956) A convenient growth medium for Neurospora (medium N). Microbiol Gen Bull 13: 42-43.
    • (1956) Microbiol Gen Bull , vol.13 , pp. 42-43
    • Vogel, H.J.1
  • 29
    • 0001194009 scopus 로고
    • Plant and bacterial chitinases differ in antifungal activity
    • Roberts WK, Selitrennikoff CP, (1988) Plant and bacterial chitinases differ in antifungal activity. J Gen Microbiol 134: 169-176.
    • (1988) J Gen Microbiol , vol.134 , pp. 169-176
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 30
    • 0036209121 scopus 로고    scopus 로고
    • Comparative degradation of oomycete, ascomycete, and basidiomycete cell walls by mycoparasitic and biocontrol fungi
    • Inglis GD, Kawchuk LM, (2002) Comparative degradation of oomycete, ascomycete, and basidiomycete cell walls by mycoparasitic and biocontrol fungi. Can J Microbiol 48: 60-70.
    • (2002) Can J Microbiol , vol.48 , pp. 60-70
    • Inglis, G.D.1    Kawchuk, L.M.2
  • 31
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M, (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29: 2001-2007.
    • (2001) Nucleic Acids Res , vol.29 , pp. 2001-2007
    • Pfaffl, M.1
  • 32
    • 55649084654 scopus 로고    scopus 로고
    • Growth on nitrate and occurrence of nitrate reductase-encoding genes in a phylogenetically diverse range of ectomycorrhizal fungi
    • Nygren CMR, Eberhardt U, Karlsson M, Parrent JL, Lindahl BD, et al. (2008) Growth on nitrate and occurrence of nitrate reductase-encoding genes in a phylogenetically diverse range of ectomycorrhizal fungi. New Phytol 180: 875-889.
    • (2008) New Phytol , vol.180 , pp. 875-889
    • Nygren, C.M.R.1    Eberhardt, U.2    Karlsson, M.3    Parrent, J.L.4    Lindahl, B.D.5
  • 35
    • 33746183968 scopus 로고    scopus 로고
    • Application of the nourseothricin acetyltransferase gene (nat1) as dominant marker for the transformation of filamentous fungi
    • Kück U, Hoff B, (2006) Application of the nourseothricin acetyltransferase gene (nat1) as dominant marker for the transformation of filamentous fungi. Fungal Genet Newsl 53: 9-11.
    • (2006) Fungal Genet Newsl , vol.53 , pp. 9-11
    • Kück, U.1    Hoff, B.2
  • 36
    • 40149110669 scopus 로고    scopus 로고
    • Protocol: Streamline cloning of genes into binary vectors in Agrobacterium via the Gateway (R) TOPO vector system
    • Xu RQ, Li QSQ, (2008) Protocol: Streamline cloning of genes into binary vectors in Agrobacterium via the Gateway (R) TOPO vector system. Plant Methods 4.
    • (2008) Plant Methods , vol.4
    • Xu, R.Q.1    Li, Q.S.Q.2
  • 37
    • 84886752034 scopus 로고    scopus 로고
    • Genetic transformation of filamentous fungi by Agrobacterium tumefaciens
    • Utermark J, Karlovsky P, (2008) Genetic transformation of filamentous fungi by Agrobacterium tumefaciens. Nature Protocols Online.
    • (2008) Nature Protocols Online
    • Utermark, J.1    Karlovsky, P.2
  • 38
    • 69449098260 scopus 로고    scopus 로고
    • The beta-N-acetylglucosaminidases NAG1 and NAG2 are essential for growth of Trichoderma atroviride on chitin
    • Lopez-Mondejar R, Catalano V, Kubicek CP, Seidl V, (2009) The beta-N-acetylglucosaminidases NAG1 and NAG2 are essential for growth of Trichoderma atroviride on chitin. Febs J 276: 5137-5148.
    • (2009) Febs J , vol.276 , pp. 5137-5148
    • Lopez-Mondejar, R.1    Catalano, V.2    Kubicek, C.P.3    Seidl, V.4
  • 39
    • 33748920925 scopus 로고    scopus 로고
    • The structure and synthesis of the fungal cell wall
    • Bowman SM, Free SJ, (2006) The structure and synthesis of the fungal cell wall. Bioessays 28: 799-808.
    • (2006) Bioessays , vol.28 , pp. 799-808
    • Bowman, S.M.1    Free, S.J.2
  • 40
    • 28044450149 scopus 로고    scopus 로고
    • A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases
    • Seidl V, Huemer B, Seiboth B, Kubicek CP, (2005) A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases. Febs J 272: 5923-5939.
    • (2005) Febs J , vol.272 , pp. 5923-5939
    • Seidl, V.1    Huemer, B.2    Seiboth, B.3    Kubicek, C.P.4
  • 41
    • 0035875889 scopus 로고    scopus 로고
    • EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG
    • Collin M, Olsen A, (2001) EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG. EMBO J 20: 3046-3055.
    • (2001) EMBO J , vol.20 , pp. 3046-3055
    • Collin, M.1    Olsen, A.2
  • 42
    • 0033532085 scopus 로고    scopus 로고
    • Cytosol-to-lysosome transport of free polymannose-type oligosaccharides. Kinetic and specificity studies using rat liver lysosomes
    • Saint-Pol A, Codogno P, Moore SE, (1999) Cytosol-to-lysosome transport of free polymannose-type oligosaccharides. Kinetic and specificity studies using rat liver lysosomes. J Biol Chem 274: 13547-13555.
    • (1999) J Biol Chem , vol.274 , pp. 13547-13555
    • Saint-Pol, A.1    Codogno, P.2    Moore, S.E.3
  • 43
    • 0030036051 scopus 로고    scopus 로고
    • The glucose repressor gene cre1 of Trichoderma: isolation and expression of a full-length and a truncated mutant form
    • Ilmen M, Thrane C, Penttila M, (1996) The glucose repressor gene cre1 of Trichoderma: isolation and expression of a full-length and a truncated mutant form. Mol Gen Genet 251: 451-460.
    • (1996) Mol Gen Genet , vol.251 , pp. 451-460
    • Ilmen, M.1    Thrane, C.2    Penttila, M.3
  • 44
    • 0042858149 scopus 로고    scopus 로고
    • Transcriptional regulation of biomass-degrading enzymes in the filamentous fungus Trichoderma reesei
    • Foreman PK, Brown D, Dankmeyer L, Dean R, Diener S, et al. (2003) Transcriptional regulation of biomass-degrading enzymes in the filamentous fungus Trichoderma reesei. J Biol Chem 278: 31988-31997.
    • (2003) J Biol Chem , vol.278 , pp. 31988-31997
    • Foreman, P.K.1    Brown, D.2    Dankmeyer, L.3    Dean, R.4    Diener, S.5
  • 45
    • 0000113162 scopus 로고
    • Chitinolytic enzymes of Trichoderma harzianum - Purification of chitobiosidase and endochitinase
    • Harman GE, Hayes CK, Lorito M, Broadway RM, Dipietro A, et al. (1993) Chitinolytic enzymes of Trichoderma harzianum- Purification of chitobiosidase and endochitinase. Phytopathology 83: 313-318.
    • (1993) Phytopathology , vol.83 , pp. 313-318
    • Harman, G.E.1    Hayes, C.K.2    Lorito, M.3    Broadway, R.M.4    Dipietro, A.5
  • 46
    • 33645120423 scopus 로고    scopus 로고
    • Cell wall assembly in Saccharomyces cerevisiae
    • Lesage G, Bussey H, (2006) Cell wall assembly in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 70: 317-343.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 317-343
    • Lesage, G.1    Bussey, H.2
  • 47
    • 0014243809 scopus 로고
    • Cell wall chemistry, morphogenesis and taxonomy of filamentous fungi
    • Bartnicki-Garcia S, (1968) Cell wall chemistry, morphogenesis and taxonomy of filamentous fungi. Ann Rev Microbiol 22: 97-108.
    • (1968) Ann Rev Microbiol , vol.22 , pp. 97-108
    • Bartnicki-Garcia, S.1
  • 48
    • 4344713045 scopus 로고    scopus 로고
    • Fungal cell wall chitinases and glucanases
    • Adams DJ, (2004) Fungal cell wall chitinases and glucanases. Microbiology-Sgm 150: 2029-2035.
    • (2004) Microbiology-Sgm , vol.150 , pp. 2029-2035
    • Adams, D.J.1
  • 49
    • 17644402110 scopus 로고    scopus 로고
    • A catalytic subunit of cyclic AMP-dependent protein kinase, PKAC-1, regulates asexual differentiation in Neurospora crassa
    • Banno S, Ochiai N, Noguchi R, Kimura M, Yamaguchi I, et al. (2005) A catalytic subunit of cyclic AMP-dependent protein kinase, PKAC-1, regulates asexual differentiation in Neurospora crassa. Genes Genet Syst 80: 25-34.
    • (2005) Genes Genet Syst , vol.80 , pp. 25-34
    • Banno, S.1    Ochiai, N.2    Noguchi, R.3    Kimura, M.4    Yamaguchi, I.5
  • 50
    • 0035109371 scopus 로고    scopus 로고
    • Genetic involvement of a cAMP-dependent protein kinase in a G protein signaling pathway regulating morphological and chemical transitions in Aspergillus nidulans
    • Shimizu K, Keller NP, (2001) Genetic involvement of a cAMP-dependent protein kinase in a G protein signaling pathway regulating morphological and chemical transitions in Aspergillus nidulans. Genetics 157: 591-600.
    • (2001) Genetics , vol.157 , pp. 591-600
    • Shimizu, K.1    Keller, N.P.2


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