메뉴 건너뛰기




Volumn 64, Issue , 2014, Pages 58-66

Functional analysis of the C-II subgroup killer toxin-like chitinases in the filamentous ascomycete Aspergillus nidulans

Author keywords

Aspergillus nidulans; Botrytis cinerea; C II subgroup; Chitinases; Fungal fungal interactions; Gene deletion

Indexed keywords

CHITINASE; CHITINASE C; YEAST KILLER FACTOR;

EID: 84893817954     PISSN: 10871845     EISSN: 10960937     Source Type: Journal    
DOI: 10.1016/j.fgb.2013.12.009     Document Type: Article
Times cited : (18)

References (46)
  • 1
    • 4344713045 scopus 로고    scopus 로고
    • Fungal cell wall chitinases and glucanases
    • Adams D.J. Fungal cell wall chitinases and glucanases. Microbiol. Rev. 2004, 150:2029-2035.
    • (2004) Microbiol. Rev. , vol.150 , pp. 2029-2035
    • Adams, D.J.1
  • 2
    • 33748920925 scopus 로고    scopus 로고
    • The structure and synthesis of the fungal cell wall
    • Bowman S.M., Free S.J. The structure and synthesis of the fungal cell wall. BioEssays 2006, 28:799-808.
    • (2006) BioEssays , vol.28 , pp. 799-808
    • Bowman, S.M.1    Free, S.J.2
  • 3
    • 0025783066 scopus 로고
    • Kluyveromyces lactis toxin has an essential chitinase activity
    • Butler A.R., et al. Kluyveromyces lactis toxin has an essential chitinase activity. Eur. J. Biochem. 1991, 199:483-488.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 483-488
    • Butler, A.R.1
  • 4
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate Active Enzymes database (CAZy): an expert resource for glycogenomics
    • Cantarel B.L., et al. The Carbohydrate Active Enzymes database (CAZy): an expert resource for glycogenomics. Nucl. Acids Res. 2009, 37:233-238.
    • (2009) Nucl. Acids Res. , vol.37 , pp. 233-238
    • Cantarel, B.L.1
  • 5
    • 0034254868 scopus 로고    scopus 로고
    • Cell wall maintenance in fungi
    • de Nobel H., et al. Cell wall maintenance in fungi. Trends Microbiol. 2000, 8:344-345.
    • (2000) Trends Microbiol. , vol.8 , pp. 344-345
    • de Nobel, H.1
  • 6
    • 0024730362 scopus 로고
    • Gene transfer system for Aspergillus oryzae using the homologous pyrG as a selection system
    • de Ruiter-Jacobs B.M., et al. Gene transfer system for Aspergillus oryzae using the homologous pyrG as a selection system. Curr. Genet. 1989, 16:159-163.
    • (1989) Curr. Genet. , vol.16 , pp. 159-163
    • de Ruiter-Jacobs, B.M.1
  • 7
    • 84860636100 scopus 로고    scopus 로고
    • Disruption of the Eng18B ENGase gene in the fungal biocontrol agent Trichoderma atroviride affetcs growth conidation and antagonistic ability
    • Dubey M., et al. Disruption of the Eng18B ENGase gene in the fungal biocontrol agent Trichoderma atroviride affetcs growth conidation and antagonistic ability. PLoS ONE 2012, 7:e36152.
    • (2012) PLoS ONE , vol.7
    • Dubey, M.1
  • 8
    • 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., et al. 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. 2004, 337:243-253.
    • (2004) J. Mol. Biol. , vol.337 , pp. 243-253
    • Eisenhaber, B.1
  • 9
    • 0000759564 scopus 로고
    • Physiology of microbial degradation of chitin and chitosan
    • Gooday G.W. Physiology of microbial degradation of chitin and chitosan. Biodegradation 1990, 1:177-190.
    • (1990) Biodegradation , vol.1 , pp. 177-190
    • Gooday, G.W.1
  • 10
    • 84855245605 scopus 로고    scopus 로고
    • Self versus non-self: fungal cell wall degradation in Trichoderma
    • Gruber S., Seidl-Seiboth V. Self versus non-self: fungal cell wall degradation in Trichoderma. Microbiology-SGM 2012, 158:26-34.
    • (2012) Microbiology-SGM , vol.158 , pp. 26-34
    • Gruber, S.1    Seidl-Seiboth, V.2
  • 11
    • 82955206449 scopus 로고    scopus 로고
    • Differential regulation of orthologous chitinase genes in mycoparasitic Trichoderma species
    • Gruber S., et al. Differential regulation of orthologous chitinase genes in mycoparasitic Trichoderma species. Appl. Environ. Microb. 2011, 77:7217-7226.
    • (2011) Appl. Environ. Microb. , vol.77 , pp. 7217-7226
    • Gruber, S.1
  • 12
    • 79951977985 scopus 로고    scopus 로고
    • Analysis of subgroup C of fungal chitinases containing chitin-binding and LysM modules in the mycoparasite Trichoderma atroviride
    • Gruber S., et al. Analysis of subgroup C of fungal chitinases containing chitin-binding and LysM modules in the mycoparasite Trichoderma atroviride. Glycobiology 2011, 21:122-133.
    • (2011) Glycobiology , vol.21 , pp. 122-133
    • Gruber, S.1
  • 13
    • 33644935876 scopus 로고    scopus 로고
    • Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens
    • Horn S.J., et al. Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens. FEBS J. 2006, 273:491-503.
    • (2006) FEBS J. , vol.273 , pp. 491-503
    • Horn, S.J.1
  • 14
    • 84856406536 scopus 로고    scopus 로고
    • Quantification of Phytophthora pisi DNA and RNA transcripts during in planta infection of pea
    • Hosseini S., et al. Quantification of Phytophthora pisi DNA and RNA transcripts during in planta infection of pea. Eur. J. Plant Pathol. 2012, 132:455-468.
    • (2012) Eur. J. Plant Pathol. , vol.132 , pp. 455-468
    • Hosseini, S.1
  • 15
    • 84898032474 scopus 로고    scopus 로고
    • Zoospore chemotaxis of closely related legume-root infecting Phytophthora species towards host isoflavones
    • Hosseini S., et al. Zoospore chemotaxis of closely related legume-root infecting Phytophthora species towards host isoflavones. Plant Pathol 2013, 10.1111/ppa.12137.
    • (2013) Plant Pathol
    • Hosseini, S.1
  • 16
    • 0036209121 scopus 로고    scopus 로고
    • Comparative degradation of oomycete, ascomycete, and basidiomycete cell walls by mycoparasitic and biocontrol fungi
    • Inglis G.D., Kawchuk L.M. Comparative degradation of oomycete, ascomycete, and basidiomycete cell walls by mycoparasitic and biocontrol fungi. Can. J. Microbiol. 2002, 48:60-70.
    • (2002) Can. J. Microbiol. , vol.48 , pp. 60-70
    • Inglis, G.D.1    Kawchuk, L.M.2
  • 17
    • 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, 4:47-60.
    • (2008) Evol. Bioinform. , vol.4 , pp. 47-60
    • Karlsson, M.1    Stenlid, J.2
  • 18
    • 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. Microb. Biotechnol. 2009, 16:208-223.
    • (2009) J. Mol. Microb. Biotechnol. , vol.16 , pp. 208-223
    • Karlsson, M.1    Stenlid, J.2
  • 19
    • 0036024578 scopus 로고    scopus 로고
    • Dynamics of cell wall structure in Saccharomyces cerevisiae
    • Klis F.M., et al. Dynamics of cell wall structure in Saccharomyces cerevisiae. FEMS Microbiol. Rev. 2002, 26:239-256.
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 239-256
    • Klis, F.M.1
  • 20
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A., et al. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 2001, 305:567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1
  • 21
    • 34748873304 scopus 로고    scopus 로고
    • The cell wall: a carbohydrate armour for the fungal cell
    • Latge J.P. The cell wall: a carbohydrate armour for the fungal cell. Mol. Microbiol. 2007, 66:279-290.
    • (2007) Mol. Microbiol. , vol.66 , pp. 279-290
    • Latge, J.P.1
  • 22
    • 0030812118 scopus 로고    scopus 로고
    • The in planta-produced extracellular proteins ECP1 and ECP2 of Cladosporium fulvum are virulence factors
    • Lauge R., et al. The in planta-produced extracellular proteins ECP1 and ECP2 of Cladosporium fulvum are virulence factors. Mol. Plant Microbe. In. 1997, 10:725-734.
    • (1997) Mol. Plant Microbe. In. , vol.10 , pp. 725-734
    • Lauge, R.1
  • 23
    • 58149194624 scopus 로고    scopus 로고
    • SMART 6: recent updates and new developments
    • Letunic I., et al. SMART 6: recent updates and new developments. Nucl. Acids Res. 2009, 37:229-232.
    • (2009) Nucl. Acids Res. , vol.37 , pp. 229-232
    • Letunic, I.1
  • 24
    • 0030832407 scopus 로고    scopus 로고
    • Yeast killer systems
    • Magliani W., et al. Yeast killer systems. Clin. Microbiol. Rev. 1997, 10:369-400.
    • (1997) Clin. Microbiol. Rev. , vol.10 , pp. 369-400
    • Magliani, W.1
  • 25
    • 58149203237 scopus 로고    scopus 로고
    • CDD: specific functional annotation with the conserved domain database
    • Marchler-Bauer A., et al. CDD: specific functional annotation with the conserved domain database. Nucl. Acids Res. 2009, 37:205-210.
    • (2009) Nucl. Acids Res. , vol.37 , pp. 205-210
    • Marchler-Bauer, A.1
  • 26
    • 0041472360 scopus 로고    scopus 로고
    • The fungal genetics stock center: from molds to molecules
    • McCluskey K. The fungal genetics stock center: from molds to molecules. Adv. Appl. Microbiol. 2003, 52:245-262.
    • (2003) Adv. Appl. Microbiol. , vol.52 , pp. 245-262
    • McCluskey, K.1
  • 27
    • 0242269023 scopus 로고    scopus 로고
    • Characterization of phiA, a gene essential for phialide development in Aspergillus nidulans
    • Melin P., et al. Characterization of phiA, a gene essential for phialide development in Aspergillus nidulans. Fungal Genet. Biol. 2003, 40:234-241.
    • (2003) Fungal Genet. Biol. , vol.40 , pp. 234-241
    • Melin, P.1
  • 28
    • 33645223703 scopus 로고    scopus 로고
    • A versatile and efficient gene targeting system for Aspergillus nidulans
    • Nayak T., et al. A versatile and efficient gene targeting system for Aspergillus nidulans. Genetics 2006, 172:1557-1566.
    • (2006) Genetics , vol.172 , pp. 1557-1566
    • Nayak, T.1
  • 29
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen T.N., et al. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 2011, 8:785-786.
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1
  • 30
    • 77954143053 scopus 로고    scopus 로고
    • The decarboxylation of the weak-acid preservative, sorbic acid, is encoded by linked genes in Aspergillus spp
    • Plumridge A., et al. The decarboxylation of the weak-acid preservative, sorbic acid, is encoded by linked genes in Aspergillus spp. Fungal Genet. Biol. 2010, 47:683-692.
    • (2010) Fungal Genet. Biol. , vol.47 , pp. 683-692
    • Plumridge, A.1
  • 31
    • 23144458473 scopus 로고    scopus 로고
    • InterProScan: protein domains identifier
    • Quevillon E., et al. InterProScan: protein domains identifier. Nucl. Acids Res. 2005, 33:116-120.
    • (2005) Nucl. Acids Res. , vol.33 , pp. 116-120
    • Quevillon, E.1
  • 32
    • 0001194009 scopus 로고
    • Plant and bacterial chitinases differ in antifungal activity
    • Roberts W.K., Selitrennikoff C.P. Plant and bacterial chitinases differ in antifungal activity. J. Gen. Microbiol. 1988, 134:169-176.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 169-176
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 33
    • 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
  • 34
    • 28044450149 scopus 로고    scopus 로고
    • A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases
    • Seidl V., et al. A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases. FEBS J. 2005, 272:5923-5939.
    • (2005) FEBS J. , vol.272 , pp. 5923-5939
    • Seidl, V.1
  • 35
    • 84874505204 scopus 로고    scopus 로고
    • Spore germination of Trichoderma atroviride is inhibited by its LysM protein TAL6
    • Seidl-Seiboth V., et al. Spore germination of Trichoderma atroviride is inhibited by its LysM protein TAL6. FEBS J. 2013, 280:1226-1236.
    • (2013) FEBS J. , vol.280 , pp. 1226-1236
    • Seidl-Seiboth, V.1
  • 36
    • 0030174870 scopus 로고    scopus 로고
    • The chsD and chsE genes of Aspergillus nidulans and their roles in chitin synthesis
    • Specht C.A., et al. The chsD and chsE genes of Aspergillus nidulans and their roles in chitin synthesis. Fungal Genet. Biol. 1996, 20:153-167.
    • (1996) Fungal Genet. Biol. , vol.20 , pp. 153-167
    • Specht, C.A.1
  • 37
    • 74349123190 scopus 로고    scopus 로고
    • Identification of a gene coding fora deglycosylating enzyme in Hypocrea jecorina
    • Stals I., et al. Identification of a gene coding fora deglycosylating enzyme in Hypocrea jecorina. FEMS Microbiol. Lett. 2010, 303:9-17.
    • (2010) FEMS Microbiol. Lett. , vol.303 , pp. 9-17
    • Stals, I.1
  • 38
    • 0022763345 scopus 로고
    • The killer toxin of Kluyveromyces lactis. Characterization of the toxin subunits and identification of the genes which encode them
    • Stark M.J.R., Boyd A. The killer toxin of Kluyveromyces lactis. Characterization of the toxin subunits and identification of the genes which encode them. EMBO J. 1986, 5:1995-2002.
    • (1986) EMBO J. , vol.5 , pp. 1995-2002
    • Stark, M.J.R.1    Boyd, A.2
  • 39
    • 77952190425 scopus 로고    scopus 로고
    • Tomato Cf resistance proteins mediate recognition of cognate homologous effectors from fungi pathogenic on dicots and monocots
    • Stergiopoulos I., et al. Tomato Cf resistance proteins mediate recognition of cognate homologous effectors from fungi pathogenic on dicots and monocots. Proc. Natl. Acad. Sci. USA 2010, 107:7610-7615.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 7610-7615
    • Stergiopoulos, I.1
  • 40
    • 84867820378 scopus 로고    scopus 로고
    • In silico characterization and molecular evolutionary analysis of a novel superfamily of fungal effector proteins
    • Stergiopoulos I., et al. In silico characterization and molecular evolutionary analysis of a novel superfamily of fungal effector proteins. Mol. Biol. Evol. 2012, 29:3371-3384.
    • (2012) Mol. Biol. Evol. , vol.29 , pp. 3371-3384
    • Stergiopoulos, I.1
  • 41
    • 84873997436 scopus 로고    scopus 로고
    • Intracellular trehalase activity is required for development, germination and heat-stress resistance of Aspergillus niger conidia
    • Svanström A., Melin P. Intracellular trehalase activity is required for development, germination and heat-stress resistance of Aspergillus niger conidia. Res. Microbiol. 2013, 164:91-99.
    • (2013) Res. Microbiol. , vol.164 , pp. 91-99
    • Svanström, A.1    Melin, P.2
  • 42
    • 34248562159 scopus 로고    scopus 로고
    • Fusion PCR and gene targeting in Aspergillus nidulans
    • Szewczyk E., et al. Fusion PCR and gene targeting in Aspergillus nidulans. Nat. Protoc. 2006, 1:3111-3120.
    • (2006) Nat. Protoc. , vol.1 , pp. 3111-3120
    • Szewczyk, E.1
  • 43
    • 84865198114 scopus 로고    scopus 로고
    • Functional analysis of glycoside hydrolase family 18 and 20 genes in Neurospora crassa
    • Tzelepis G.D., et al. Functional analysis of glycoside hydrolase family 18 and 20 genes in Neurospora crassa. Fungal Genet. Biol. 2012, 49:717-730.
    • (2012) Fungal Genet. Biol. , vol.49 , pp. 717-730
    • Tzelepis, G.D.1
  • 44
    • 0035979240 scopus 로고    scopus 로고
    • Structural insights into the catalytic mechanism of a family 18 exo-chitinase
    • van Aalten D.M.F., et al. Structural insights into the catalytic mechanism of a family 18 exo-chitinase. Proc. Natl. Acad. Sci. USA 2001, 98:8979-8984.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8979-8984
    • van Aalten, D.M.F.1
  • 45
    • 84865628856 scopus 로고    scopus 로고
    • Biochemical characterization of Aspergillus niger CfcI, a glycoside hydrolase family 18 chitinase that releases monomers during substrate hydrolysis
    • van Munster J.M., et al. Biochemical characterization of Aspergillus niger CfcI, a glycoside hydrolase family 18 chitinase that releases monomers during substrate hydrolysis. Microbiology-SGM 2012, 158:2168-2179.
    • (2012) Microbiology-SGM , vol.158 , pp. 2168-2179
    • van Munster, J.M.1
  • 46
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute-solution in the presence of detergents and lipids
    • Wessel D., Flugge U.I. A method for the quantitative recovery of protein in dilute-solution in the presence of detergents and lipids. Anal. Biochem. 1984, 138:141-143.
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Flugge, U.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.