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Volumn 2010, Issue 6, 2010, Pages 1-26

Comparative molecular evolution of Trichoderma chitinases in response to mycoparasitic interactions

Author keywords

Chitinase; Mycoparasitism; Protein evolution; Trichoderma

Indexed keywords

CHITINASE; SIGNAL PEPTIDE;

EID: 77951266103     PISSN: None     EISSN: 11769343     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (49)

References (68)
  • 1
    • 0000163023 scopus 로고    scopus 로고
    • Tronsmo A
    • In: Harman GE, Kubicek CP, editors, Taylor and Francis
    • Hjeljord L, Tronsmo A. In: Harman GE, Kubicek CP, editors. Trichoderma and Gliocladium. Taylor and Francis. 1998; p. 131-51.
    • (1998) Trichoderma and Gliocladium , pp. 131-151
    • Hjeljord, L.1
  • 2
    • 1842591134 scopus 로고    scopus 로고
    • Lorito M. Trichoderma species- Opportunistic, avirulent plant symbionts
    • Harman GE, Howell CR, Viterbo A, Chet I, Lorito M. Trichoderma species- Opportunistic, avirulent plant symbionts. Nature Rev Microbiol. 2004;2:43-56.
    • (2004) Nature Rev Microbiol , vol.2 , pp. 43-56
    • Harman, G.E.1    Howell, C.R.2    Viterbo, A.3    Chet, I.4
  • 3
    • 0002669714 scopus 로고
    • Baker R. Trichoderma hamatum-Its hyphal interactions with Rhizoctonia solani and Pythium spp
    • Chet I, Harman GE, Baker R. Trichoderma hamatum-Its hyphal interactions with Rhizoctonia solani and Pythium spp. Microb Ecol. 1981; 7:29-38.
    • (1981) Microb Ecol , vol.7 , pp. 29-38
    • Chet, I.1    Harman, G.E.2
  • 4
    • 0028100107 scopus 로고
    • Parallel formation and synergism of hydrolytic enzymes and peptaibol antibiotics, molecular mechanisms involved in the antagonistic action of Trichoderma harzianum against phytopathogenic fungi
    • Schirmbock M, Lorito M, Wang YL, et al. Parallel formation and synergism of hydrolytic enzymes and peptaibol antibiotics, molecular mechanisms involved in the antagonistic action of Trichoderma harzianum against phytopathogenic fungi. Appl Environ Microb. 1994;60:4364-70.
    • (1994) Appl Environ Microb , vol.60 , pp. 4364-4370
    • Schirmbock, M.1    Lorito, M.2    Wang, Y.L.3
  • 5
    • 0037226578 scopus 로고    scopus 로고
    • Mechanisms employed by Trichoderma species in the biological control of plant diseases: The history and evolution of current concepts
    • Howell CR. Mechanisms employed by Trichoderma species in the biological control of plant diseases: The history and evolution of current concepts. Plant Dis. 2003;87:4-10.
    • (2003) Plant Dis , vol.87 , pp. 4-10
    • Howell, C.R.1
  • 7
    • 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. Comparative evolutionary histories of the fungal chitinase gene family reveal non-random size expansions and contractions due to adaptive natural selection. Evol Bioinform. 2008:47-60.
    • (2008) Evol Bioinform , pp. 47-60
    • Karlsson, M.1    Stenlid, J.2
  • 8
    • 33745039979 scopus 로고    scopus 로고
    • Review of fungal chitinases
    • Duo-Chuan L. Review of fungal chitinases. Mycopathologia. 2006; 161:345-60.
    • (2006) Mycopathologia , vol.161 , pp. 345-360
    • Duo-Chuan, L.1
  • 9
    • 44449145113 scopus 로고    scopus 로고
    • Chitinases of filamentous fungi: A large group of diverse proteins with multiple physiological functions
    • Seidl V. Chitinases of filamentous fungi: a large group of diverse proteins with multiple physiological functions. Fungal Biol Rev. 2008;22:36-42.
    • (2008) Fungal Biol Rev , vol.22 , pp. 36-42
    • Seidl, V.1
  • 10
    • 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. A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases. FEBS J. 2005;272:5923-39.
    • (2005) FEBS J , vol.272 , pp. 5923-5939
    • Seidl, V.1    Huemer, B.2    Seiboth, B.3    Kubicek, C.P.4
  • 12
    • 60149095281 scopus 로고    scopus 로고
    • Evolution of family 18 glycoside hydrolases:Diversity, domain structures and phylogenetic relationships
    • Karlsson M, Stenlid J. Evolution of family 18 glycoside hydrolases:Diversity, domain structures and phylogenetic relationships. J Mol Microbiol Biotechnol. 2009;16:208-23.
    • (2009) J Mol Microbiol Biotechnol , vol.16 , pp. 208-223
    • Karlsson, M.1    Stenlid, J.2
  • 13
    • 0035917427 scopus 로고    scopus 로고
    • Addition of substrate- binding domains increases substrate-binding capacity and specific activity of a chitinase from Trichoderma harzianum
    • Limon MC, Margolles-Clark E, Benitez T, Penttila M. Addition of substrate- binding domains increases substrate-binding capacity and specific activity of a chitinase from Trichoderma harzianum. FEMS Microbiol Lett. 2001;198:57-63.
    • (2001) FEMS Microbiol Lett , vol.198 , pp. 57-63
    • Limon, M.C.1    Margolles-Clark, E.2    Benitez, T.3    Penttila, M.4
  • 14
    • 33644819734 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and expression studies of a novel chitinase gene (ech30) from the mycoparasite Trichoderma atroviride strain P 1
    • Klemsdal SS, Clarke JHL, Hoell IA, Eijsink VGH, Brurberg MB. Molecular cloning, characterization, and expression studies of a novel chitinase gene (ech30) from the mycoparasite Trichoderma atroviride strain P 1. FEMS Microbiol Lett. 2006;256:282-9.
    • (2006) FEMS Microbiol Lett , vol.256 , pp. 282-289
    • Klemsdal, S.S.1    Clarke, J.H.L.2    Hoell, I.A.3    Eijsink, V.G.H.4    Brurberg, M.B.5
  • 15
    • 0036227209 scopus 로고    scopus 로고
    • Cloning and characterization of multiple glycosyl hydrolase genes from Trichoderma virens
    • Kim DJ, Baek JM, Uribe P, Kenerley CM, Cook DR. Cloning and characterization of multiple glycosyl hydrolase genes from Trichoderma virens. Curr Genet. 2002;40:374-84.
    • (2002) Curr Genet , vol.40 , pp. 374-384
    • Kim, D.J.1    Baek, J.M.2    Uribe, P.3    Kenerley, C.M.4    Cook, D.R.5
  • 16
    • 0036873374 scopus 로고    scopus 로고
    • Expression regulation of the endochitinase chit36 from Trichoderma asperellum (T. harzianum T-203)
    • Viterbo A, Montero M, Ramot O, et al. Expression regulation of the endochitinase chit36 from Trichoderma asperellum (T. harzianum T-203). Curr Genet. 2002;42:114-22.
    • (2002) Curr Genet , vol.42 , pp. 114-122
    • Viterbo, A.1    Montero, M.2    Ramot, O.3
  • 17
    • 0035187729 scopus 로고    scopus 로고
    • Regulation of chitinase 33 (chit33) gene expression in Trichoderma harzianum
    • de las Mercedes Dana M, Carmen Limón M, Mejias R, et al. Regulation of chitinase 33 (chit33) gene expression in Trichoderma harzianum. Curr Genet. 2001;38:335-42.
    • (2001) Curr Genet , vol.38 , pp. 335-342
    • Carmen Limón, M.1    Mejias, R.2
  • 18
    • 0032847740 scopus 로고    scopus 로고
    • Chitinase gene expression during mycoparasitic interaction of Trichoderma harzianum with its host
    • Zeilinger S, Galhaup C, Payer K, et al. Chitinase gene expression during mycoparasitic interaction of Trichoderma harzianum with its host. Fungal Genet Biol. 1999;26:131-40.
    • (1999) Fungal Genet Biol , vol.26 , pp. 131-140
    • Zeilinger, S.1    Galhaup, C.2    Payer, K.3
  • 19
    • 0034625046 scopus 로고    scopus 로고
    • Rapid evolution in plant chitinases: Molecular targets of selection in plant-pathogen coevolution
    • Bishop JG, Dean AM, Mitchell-Olds T. Rapid evolution in plant chitinases: Molecular targets of selection in plant-pathogen coevolution. Proc Natl Acad Sci U S A. 2000;97:5322-7.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 5322-5327
    • Bishop, J.G.1    Dean, A.M.2    Mitchell-Olds, T.3
  • 20
    • 3843052542 scopus 로고    scopus 로고
    • Comparative evolutionary histories of chitinase genes in the genus Zea and family Poaceae
    • Tiffin P. Comparative evolutionary histories of chitinase genes in the genus Zea and family Poaceae. Genetics. 2004;167:1331-40.
    • (2004) Genetics , vol.167 , pp. 1331-1340
    • Tiffin, P.1
  • 21
    • 0027580147 scopus 로고
    • Its primers with enhanced specificity for basidiomycetes- Application to the identification of mycorrhizae and rusts
    • Gardes M, Bruns TD. Its primers with enhanced specificity for basidiomycetes- Application to the identification of mycorrhizae and rusts. Mol Ecol. 1993;2:113-8.
    • (1993) Mol Ecol , vol.2 , pp. 113-118
    • Gardes, M.1    Bruns, T.D.2
  • 23
    • 24944435502 scopus 로고    scopus 로고
    • An oligonucleotide barcode for species identification in Trichoderma and Hypocrea
    • Druzhinina IS, Kopchinskiy AG, Komon M, et al. An oligonucleotide barcode for species identification in Trichoderma and Hypocrea. Fungal Genet Biol. 2005;42:813-28.
    • (2005) Fungal Genet Biol , vol.42 , pp. 813-828
    • Druzhinina, I.S.1    Kopchinskiy, A.G.2    Komon, M.3
  • 24
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit:A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall TA. BioEdit:a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucl Acids Symp Ser. 1999;41:95-8.
    • (1999) Nucl Acids Symp Ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 26
    • 33646856440 scopus 로고    scopus 로고
    • CAFE: A computational tool for the study of gene family evolution
    • De Bie T, Cristianini N, Demuth JP, Hahn MW. CAFE: a computational tool for the study of gene family evolution. Bioinformatics. 2006;22:1269-71.
    • (2006) Bioinformatics , vol.22 , pp. 1269-1271
    • de Bie, T.1    Cristianini, N.2    Demuth, J.P.3    Hahn, M.W.4
  • 27
    • 23744452485 scopus 로고    scopus 로고
    • Estimating the tempo and mode of gene family evolution from comparative genomic data
    • Hahn MW, De Bie T, Stajich JE, Nguyen C, Cristianini N. Estimating the tempo and mode of gene family evolution from comparative genomic data. Genome Res. 2005;15:1153-60.
    • (2005) Genome Res , vol.15 , pp. 1153-1160
    • Hahn, M.W.1    de Bie, T.2    Stajich, J.E.3    Nguyen, C.4    Cristianini, N.5
  • 28
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSIBLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schäffer AA, et al. Gapped BLAST and PSIBLAST: a new generation of protein database search programs. Nucleic Acids Res. 1997;25:3389-402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schäffer, A.A.3
  • 29
    • 0034800374 scopus 로고    scopus 로고
    • InterProScan-an integration platform for the signature-recognition methods in InterPro
    • Zdobnov EM, Apweiler R. InterProScan-an integration platform for the signature-recognition methods in InterPro. Bioinformatics. 2001;17:847-8.
    • (2001) Bioinformatics , vol.17 , pp. 847-848
    • Zdobnov, E.M.1    Apweiler, R.2
  • 30
    • 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. Clustal-W-Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994;22:4673-80.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 31
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4. 0
    • Tamura K, Dudley J, Nei M, Kumar S. MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4. 0. Mol Biol Evol. 2007;24:1596-9.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 32
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM. The rapid generation of mutation data matrices from protein sequences. Comp Appl Biosci. 1992;8:275-82.
    • (1992) Comp Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 34
    • 41049103102 scopus 로고    scopus 로고
    • Reverse conservation analysis reveals the specificity determining residues of cytochrome P450 family 2 (CYP 2)
    • Lee T. Reverse conservation analysis reveals the specificity determining residues of cytochrome P450 family 2 (CYP 2). Evol Bioinform. 2008;4:7-16.
    • (2008) Evol Bioinform , vol.4 , pp. 7-16
    • Lee, T.1
  • 35
    • 4143051195 scopus 로고    scopus 로고
    • Comparison of site-specific rateinference methods for protein sequences: Empirical bayesian methods are superior
    • Mayrose I, Graur D, Ben-Tal N, Pupko T. Comparison of site-specific rateinference methods for protein sequences: Empirical bayesian methods are superior. Mol Biol Evol. 2004;21:1781-91.
    • (2004) Mol Biol Evol , vol.21 , pp. 1781-1791
    • Mayrose, I.1    Graur, D.2    Ben-Tal, N.3    Pupko, T.4
  • 36
    • 0002218484 scopus 로고    scopus 로고
    • Rate4Site: An algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues
    • Pupko T, Bell R, Mayrose I, Glaser F, Ben-Tal N. Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues. Bioinformatics. 2002;18:S71-7.
    • (2002) Bioinformatics , vol.18
    • Pupko, T.1    Bell, R.2    Mayrose, I.3    Glaser, F.4    Ben-Tal, N.5
  • 39
    • 30344452280 scopus 로고    scopus 로고
    • SAM-T04: What is new in protein-structure prediction for CASP 6
    • Karplus K, Katzman S, Shackleford G, et al. SAM-T04: what is new in protein-structure prediction for CASP 6. Proteins. 2005;61:135-42.
    • (2005) Proteins , vol.61 , pp. 135-142
    • Karplus, K.1    Katzman, S.2    Shackleford, G.3
  • 42
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr A. 1991;47:110-9.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 43
    • 12344317078 scopus 로고    scopus 로고
    • Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinases
    • Rao FV, Houston DR, Boot RG, et al. Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinases. Chem Biol. 2005;12:65-76.
    • (2005) Chem Biol , vol.12 , pp. 65-76
    • Rao, F.V.1    Houston, D.R.2    Boot, R.G.3
  • 44
    • 33747413686 scopus 로고    scopus 로고
    • Moreno FBB, da Rocha BAM, et al. cDNA cloning and 1.75 angstrom crystal structure determination of PPL2, an endochitinase and N-acetylglucosamine-binding hemagglutinin from Parkia platycephala seeds
    • Cavada BS, Moreno FBB, da Rocha BAM, et al. cDNA cloning and 1.75 angstrom crystal structure determination of PPL2, an endochitinase and N-acetylglucosamine-binding hemagglutinin from Parkia platycephala seeds. FEBS J. 2006;273:3962-74.
    • (2006) FEBS J , vol.273 , pp. 3962-3974
    • Cavada, B.S.1
  • 45
    • 34248596802 scopus 로고    scopus 로고
    • Structure of Saccharomyces cerevisiae chitinase 1 and screening-based discovery of potent inhibitors
    • Hurtado-Guerrero R, van Aalten DMF. Structure of Saccharomyces cerevisiae chitinase 1 and screening-based discovery of potent inhibitors. Chem Biol. 2007;14:589-99.
    • (2007) Chem Biol , vol.14 , pp. 589-599
    • Hurtado-Guerrero, R.1    van Aalten, D.M.F.2
  • 46
    • 0026244229 scopus 로고
    • Molscript-a program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. Molscript-a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr. 1991;24:946-50.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 47
    • 0034903751 scopus 로고    scopus 로고
    • Molray-a web interface between O and the POV-Ray ray tracer
    • Harris M, Jones TA. Molray-a web interface between O and the POV-Ray ray tracer. Acta Crystallogr D. 2001;57:1201-3.
    • (2001) Acta Crystallogr D , vol.57 , pp. 1201-1203
    • Harris, M.1    Jones, T.A.2
  • 48
    • 17744396121 scopus 로고    scopus 로고
    • Not so different after all: A comparison of methods for detecting amino acid sites under selection
    • Pond SLK, Frost SDW. Not so different after all: A comparison of methods for detecting amino acid sites under selection. Mol Biol Evol. 2005;22:1208-22.
    • (2005) Mol Biol Evol , vol.22 , pp. 1208-1222
    • Pond, S.L.K.1    Frost, S.D.W.2
  • 50
    • 17744395033 scopus 로고    scopus 로고
    • Datamonkey: Rapid detection of selective pressure on individual sites of codon alignments
    • Pond SLK, Frost SDW. Datamonkey: rapid detection of selective pressure on individual sites of codon alignments. Bioinformatics. 2005;21:2531-3.
    • (2005) Bioinformatics , vol.21 , pp. 2531-2533
    • Pond, S.L.K.1    Frost, S.D.W.2
  • 51
    • 12344314451 scopus 로고    scopus 로고
    • A simple hierarchical approach to modeling distributions of substitution rates
    • Pond SLK, Frost SDW. A simple hierarchical approach to modeling distributions of substitution rates. Mol Biol Evol. 2005;22:223-34.
    • (2005) Mol Biol Evol , vol.22 , pp. 223-234
    • Pond, S.L.K.1    Frost, S.D.W.2
  • 52
    • 0021277009 scopus 로고
    • A new method for calculating evolutionary substitution rates
    • Lanave C, Preparata G, Saccone C, Serio G. A new method for calculating evolutionary substitution rates. J Mol Evol. 1984;20:86-93.
    • (1984) J Mol Evol , vol.20 , pp. 86-93
    • Lanave, C.1    Preparata, G.2    Saccone, C.3    Serio, G.4
  • 53
    • 0002671410 scopus 로고
    • Some probabilistic and statistical problems in the analysis of DNA sequences
    • Tavaré S. Some probabilistic and statistical problems in the analysis of DNA sequences. Lect Math Life Sci. 1986;17:57-86.
    • (1986) Lect Math Life Sci , vol.17 , pp. 57-86
    • Tavaré, S.1
  • 54
  • 55
    • 36948998606 scopus 로고    scopus 로고
    • An evolutionary-network model reveals stratified interactions in the V3 loop of the HIV-1 envelope
    • Poon A, Lewis F, Pond SLK, Frost S. An evolutionary-network model reveals stratified interactions in the V3 loop of the HIV-1 envelope. PLoS Comp Biol. 2007;3:e231.
    • (2007) PLoS Comp Biol , vol.e231 , pp. 3
    • Poon, A.1    Lewis, F.2    Pond, S.L.K.3    Frost, S.4
  • 57
    • 13644274633 scopus 로고    scopus 로고
    • Species concepts and biodiversity in Trichoderma and Hypocrea: From aggregate species to species clusters
    • Druzhinina I, Kubicek CP. Species concepts and biodiversity in Trichoderma and Hypocrea: from aggregate species to species clusters. J Zhejiang Univ. 2005;6B:100-12.
    • (2005) J Zhejiang Univ , vol.6 B , pp. 100-112
    • Druzhinina, I.1    Kubicek, C.P.2
  • 58
    • 34548501747 scopus 로고    scopus 로고
    • Natural history and evolutionary principles of gene duplication in fungi
    • Wapinski I, Pfeffer A, Friedman N, Regev A. Natural history and evolutionary principles of gene duplication in fungi. Nature. 2007;449:54-U36.
    • (2007) Nature , vol.449
    • Wapinski, I.1    Pfeffer, A.2    Friedman, N.3    Regev, A.4
  • 60
    • 0026777916 scopus 로고
    • Isolation and characterization of 3 chitinases from Trichoderma harzianum
    • Delacruz J, Hidalgogallego A, Lora JM, et al. Isolation and characterization of 3 chitinases from Trichoderma harzianum. Eur J Biochem. 1992;206:859-67.
    • (1992) Eur J Biochem , vol.206 , pp. 859-867
    • Delacruz, J.1    Hidalgogallego, A.2    Lora, J.M.3
  • 61
    • 9744227158 scopus 로고    scopus 로고
    • Differential recognition of animal type beta 4-galactosylated and alpha 3-fucosylated chito-oligosaccharides by two family 18 chitinases from Trichoderma harzianum
    • Boer H, Munck N, Natunen J, et al. Differential recognition of animal type beta 4-galactosylated and alpha 3-fucosylated chito-oligosaccharides by two family 18 chitinases from Trichoderma harzianum. Glycobiology. 2004;14:1303-13.
    • (2004) Glycobiology , vol.14 , pp. 1303-1313
    • Boer, H.1    Munck, N.2    Natunen, J.3
  • 62
    • 0029849870 scopus 로고    scopus 로고
    • Differential expression of Trichoderma harzianum chitinases during mycoparasitism
    • Haran S, Schickler H, Oppenheim A, Chet I. Differential expression of Trichoderma harzianum chitinases during mycoparasitism. Phytopathology. 1996;86:980-5.
    • (1996) Phytopathology , vol.86 , pp. 980-985
    • Haran, S.1    Schickler, H.2    Oppenheim, A.3    Chet, I.4
  • 64
    • 0028135314 scopus 로고
    • Cloning and characterization of a chitinase (Chit42) cdna from the mycoparasitic fungus Trichoderma harzianum
    • Garcia I, Lora JM, Delacruz J, et al. Cloning and characterization of a chitinase (Chit42) cdna from the mycoparasitic fungus Trichoderma harzianum. Curr Genet. 1994;27:83-9.
    • (1994) Curr Genet , vol.27 , pp. 83-89
    • Garcia, I.1    Lora, J.M.2    Delacruz, J.3
  • 65
    • 0032948076 scopus 로고    scopus 로고
    • Expression of two major chitinase genes of Trichoderma atroviride (T. harzianum P1) is triggered by different regulatory signals
    • Mach RL, Peterbauer CK, Payer K, et al. Expression of two major chitinase genes of Trichoderma atroviride (T. harzianum P1) is triggered by different regulatory signals. Appl Environ Microbiol. 1999;65:1858-63.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 1858-1863
    • Mach, R.L.1    Peterbauer, C.K.2    Payer, K.3
  • 66
    • 0032984965 scopus 로고    scopus 로고
    • Role of the Trichoderma harzianum endochitinase gene, ech42, in mycoparasitism
    • Carsolio C, Benhamou N, Haran S, et al. Role of the Trichoderma harzianum endochitinase gene, ech42, in mycoparasitism. Appl Environ Microbiol. 1999;65:929-35.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 929-935
    • Carsolio, C.1    Benhamou, N.2    Haran, S.3
  • 67
    • 0032961637 scopus 로고    scopus 로고
    • Disruption of the ech42 (endochitinaseencoding) gene affects biocontrol activity in Trichoderma harzianum P 1
    • Woo SL, Donzelli B, Scala F, et al. Disruption of the ech42 (endochitinaseencoding) gene affects biocontrol activity in Trichoderma harzianum P 1. Mol Plant Microbe In. 1999;12:419-29.
    • (1999) Mol Plant Microbe In , vol.12 , pp. 419-429
    • Woo, S.L.1    Donzelli, B.2    Scala, F.3
  • 68
    • 0033057503 scopus 로고    scopus 로고
    • The role of an extracellular chitinase from Trichoderma virens Gv29-8 in the biocontrol of Rhizoctonia solani
    • Baek JM, Howell CR, Kenerley CM. The role of an extracellular chitinase from Trichoderma virens Gv29-8 in the biocontrol of Rhizoctonia solani. Curr Genet. 1999;35:41-50.
    • (1999) Curr Genet , vol.35 , pp. 41-50
    • Baek, J.M.1    Howell, C.R.2    Kenerley, C.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.