메뉴 건너뛰기




Volumn 15, Issue 9, 2002, Pages 907-921

Characterization and evolutionary analysis of a large polygalacturonase gene family in the oomycete plant pathogen Phytophthora cinnamomi

Author keywords

[No Author keywords available]

Indexed keywords

FUNGI; PHYTOPHTHORA; PHYTOPHTHORA CINNAMOMI;

EID: 0036751423     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/MPMI.2002.15.9.907     Document Type: Article
Times cited : (75)

References (93)
  • 2
    • 0031020876 scopus 로고    scopus 로고
    • Recent advances in the molecular genetics of plant cell wall-degrading enzymes produced by plant pathogenic fungi
    • Annis, S. L., and Goodwin, P. H. 1997. Recent advances in the molecular genetics of plant cell wall-degrading enzymes produced by plant pathogenic fungi. Eur. J. Plant Pathol. 103:1-14.
    • (1997) Eur. J. Plant Pathol. , vol.103 , pp. 1-14
    • Annis, S.L.1    Goodwin, P.H.2
  • 4
    • 0033083712 scopus 로고    scopus 로고
    • Kinetic characterization of Aspergillus niger N400 endopolygalacturonases I, II, and C
    • Benen, J. A. E., Kester, H. C. M., and Visser, J. 1999. Kinetic characterization of Aspergillus niger N400 endopolygalacturonases I, II, and C. Eur. J. Biochem. 259:577-585.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 577-585
    • Benen, J.A.E.1    Kester, H.C.M.2    Visser, J.3
  • 6
    • 0028877924 scopus 로고
    • Gene inactivation in the plant pathogen Glomerella cingulata: Three strategies for the disruption of the pectin lyase gene pnlA
    • Bowen, J. K., Templeton, M. D., Sharrock, K. R., Crowhurst, R. N., and Rikkerink. E. H. A. 1995. Gene inactivation in the plant pathogen Glomerella cingulata: three strategies for the disruption of the pectin lyase gene pnlA. Mol. Gen. Genet. 246:196-205.
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 196-205
    • Bowen, J.K.1    Templeton, M.D.2    Sharrock, K.R.3    Crowhurst, R.N.4    Rikkerink, E.H.A.5
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-binding dye
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-binding dye. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0026646374 scopus 로고
    • The polygalacturonases of Aspergillus niger are encoded by a family of diverged genes
    • Bussink, H. J. D., Buxton, F. P., Fraaye, B. A., de Graaff, L. H., and Visser, J. 1992. The polygalacturonases of Aspergillus niger are encoded by a family of diverged genes. Eur. J. Biochem. 208:83-90.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 83-90
    • Bussink, H.J.D.1    Buxton, F.P.2    Fraaye, B.A.3    De Graaff, L.H.4    Visser, J.5
  • 9
    • 0030237034 scopus 로고    scopus 로고
    • Mutagenesis of endopolygalacturonase from Fusarium moniliforme: Histidine residue 234 is critical for enzymatic and macerating activities and not for binding to polygalacturonase-inhibiting protein (PGIP)
    • Caprari, C., Mattei, B., Basile, M. L., Salvi, G., Crescenzi, V., De Lorenzo, G., and Cervone, F. 1996. Mutagenesis of endopolygalacturonase from Fusarium moniliforme: Histidine residue 234 is critical for enzymatic and macerating activities and not for binding to polygalacturonase-inhibiting protein (PGIP). Mol. Plant-Microbe Interact. 9:617-624.
    • (1996) Mol. Plant-Microbe Interact. , vol.9 , pp. 617-624
    • Caprari, C.1    Mattei, B.2    Basile, M.L.3    Salvi, G.4    Crescenzi, V.5    De Lorenzo, G.6    Cervone, F.7
  • 10
    • 0027351945 scopus 로고
    • Structural models of primary cell walls in flowering plants: Consistency of molecular structure with the physical properties of the walls during growth
    • Carpita, N. C., and Gibeaut, D. M. 1993. Structural models of primary cell walls in flowering plants: Consistency of molecular structure with the physical properties of the walls during growth. Plant J. 3:1-30.
    • (1993) Plant J. , vol.3 , pp. 1-30
    • Carpita, N.C.1    Gibeaut, D.M.2
  • 11
    • 0000218991 scopus 로고
    • Host-pathogen interactions XXXIII. A plant protein converts a fungal pathogenesis factor into an elicitor of plant defense responses
    • Cervone, F., Hahn, M. G., De Lorenzo, G., Darvill, A., and Albersheim, P. 1989. Host-pathogen interactions XXXIII. A plant protein converts a fungal pathogenesis factor into an elicitor of plant defense responses. Plant Physiol. 90:542-548.
    • (1989) Plant Physiol. , vol.90 , pp. 542-548
    • Cervone, F.1    Hahn, M.G.2    De Lorenzo, G.3    Darvill, A.4    Albersheim, P.5
  • 13
    • 0011003826 scopus 로고
    • Pectic enzyme activity from Phytophthora infestans
    • Cole, A. L. J. 1970. Pectic enzyme activity from Phytophthora infestans. Phytochem. 9:337-340.
    • (1970) Phytochem. , vol.9 , pp. 337-340
    • Cole, A.L.J.1
  • 15
    • 0033180109 scopus 로고    scopus 로고
    • Fungal polygalacturonases exhibit different substrate degradation patterns and differ in their susceptibilities to polygalacturonase-inhibiting proteins
    • Cook, B. J., Clay, R. P., Bergmann, C. W., Albersheim, P., and Darvill, A. G. 1999. Fungal polygalacturonases exhibit different substrate degradation patterns and differ in their susceptibilities to polygalacturonase-inhibiting proteins. Mol. Plant-Microbe Interact. 12:703-711.
    • (1999) Mol. Plant-Microbe Interact. , vol.12 , pp. 703-711
    • Cook, B.J.1    Clay, R.P.2    Bergmann, C.W.3    Albersheim, P.4    Darvill, A.G.5
  • 16
    • 0003019287 scopus 로고
    • The mechanisms and significance of enzymic degradation of host cell walls by parasites
    • J. A. Callow, ed. John Wiley & Sons, Chichester, U.K
    • Cooper, R. M. 1983. The mechanisms and significance of enzymic degradation of host cell walls by parasites. Pages 101-135 in: Biochemical Plant Pathology. J. A. Callow, ed. John Wiley & Sons, Chichester, U.K.
    • (1983) Biochemical Plant Pathology , pp. 101-135
    • Cooper, R.M.1
  • 20
    • 0025398312 scopus 로고
    • The single-copy actin gene of Phytophthora megasperma encodes a protein considerably diverged from any other known actin
    • Dudler, D. 1990. The single-copy actin gene of Phytophthora megasperma encodes a protein considerably diverged from any other known actin. Plant Mol. Biol. 14:415-422.
    • (1990) Plant Mol. Biol. , vol.14 , pp. 415-422
    • Dudler, D.1
  • 21
    • 0033946441 scopus 로고    scopus 로고
    • Structure, function and evolution of plant disease resistance genes
    • Ellis, J., Dodds, P., and Pryor, T. 2000. Structure, function and evolution of plant disease resistance genes. Curr. Opin. Plant Biol. 3:278-284.
    • (2000) Curr. Opin. Plant Biol. , vol.3 , pp. 278-284
    • Ellis, J.1    Dodds, P.2    Pryor, T.3
  • 23
    • 0034069786 scopus 로고    scopus 로고
    • Cell wall degrading enzymes, inhibitory proteins, and oligosaccharides participate in the molecular dialogue between plants and pathogens
    • Esquerré-Tugayé, M.-T., Boudart, G. and Dumas, B. 2000. Cell wall degrading enzymes, inhibitory proteins, and oligosaccharides participate in the molecular dialogue between plants and pathogens. Plant Physiol. Biochem. 38:157-163.
    • (2000) Plant Physiol. Biochem. , vol.38 , pp. 157-163
    • Esquerré-Tugayé, M.-T.1    Boudart, G.2    Dumas, B.3
  • 25
    • 0000167965 scopus 로고
    • Sequence analysis of the small subunit ribosomal RNAs of three zoosporic fungi and implications for fungal evolution
    • Förster, H., Coffey, M. D., Elwood, H., and Sogin, M. L. 1990. Sequence analysis of the small subunit ribosomal RNAs of three zoosporic fungi and implications for fungal evolution. Mycologia 82:306-312.
    • (1990) Mycologia , vol.82 , pp. 306-312
    • Förster, H.1    Coffey, M.D.2    Elwood, H.3    Sogin, M.L.4
  • 26
    • 0029591982 scopus 로고
    • Characterization of a multigene family encoding an endopolygalacturonase in Sclerotinia sclerotiorum
    • Fraissinet-Tachet, L., Reymond-Cotton, P., and Fevre, M. 1995. Characterization of a multigene family encoding an endopolygalacturonase in Sclerotinia sclerotiorum. Curr. Genet. 29:96-100.
    • (1995) Curr. Genet. , vol.29 , pp. 96-100
    • Fraissinet-Tachet, L.1    Reymond-Cotton, P.2    Fevre, M.3
  • 27
    • 0030014049 scopus 로고    scopus 로고
    • Regulation by galacturonic acid of pectinolytic enzyme production by Sclerotinia sclerotiorum
    • Fraissinet-Tachet, L., and Fevre, M. 1996. Regulation by galacturonic acid of pectinolytic enzyme production by Sclerotinia sclerotiorum. Curr. Microbiol. 33:49-53.
    • (1996) Curr. Microbiol. , vol.33 , pp. 49-53
    • Fraissinet-Tachet, L.1    Fevre, M.2
  • 28
    • 0029980809 scopus 로고    scopus 로고
    • Cloning and targeted disruption of enpg-1, encoding the major in vitro extracellular endopolygalacturonase of the chestnut blight fungus, Cryphonectria parasitica
    • Gao, S., Choi, G. H., Shain, L., and Nuss, D. L. 1996. Cloning and targeted disruption of enpg-1, encoding the major in vitro extracellular endopolygalacturonase of the chestnut blight fungus, Cryphonectria parasitica. Appl. Environ. Microbiol. 62:1984-1990.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1984-1990
    • Gao, S.1    Choi, G.H.2    Shain, L.3    Nuss, D.L.4
  • 29
    • 0343963759 scopus 로고    scopus 로고
    • Cloning and disruption of pgx4 encoding an in planta expressed exopolygalacturonase from Fusarium oxysporum
    • García-Maceira, F. I., Di Pietro, A., and Roncero, M. I. G. 2000. Cloning and disruption of pgx4 encoding an in planta expressed exopolygalacturonase from Fusarium oxysporum. Mol. Plant-Microbe Interact. 13:359-365.
    • (2000) Mol. Plant-Microbe Interact. , vol.13 , pp. 359-365
    • García-Maceira, F.I.1    Di Pietro, A.2    Roncero, M.I.G.3
  • 30
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdbviewer: An environment for comparative protein modeling
    • Geux, N., and Peitsch, M. C. 1997. SWISS-MODEL and the Swiss-Pdbviewer: An environment for comparative protein modeling. Electrophoresis 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Geux, N.1    Peitsch, M.C.2
  • 31
    • 0033753825 scopus 로고    scopus 로고
    • Sister-Scanning: A Monte Carlo procedure for assessing signals in recombinant sequences
    • Gibbs, M. J., Armstrong, J. S., and Gibbs, A. J. 2000. Sister-Scanning: A Monte Carlo procedure for assessing signals in recombinant sequences. Bioinformatics 16:573-582.
    • (2000) Bioinformatics , vol.16 , pp. 573-582
    • Gibbs, M.J.1    Armstrong, J.S.2    Gibbs, A.J.3
  • 32
    • 0000816241 scopus 로고
    • A rapid and sensitive spectrophotometric method for assaying polygalacturonase using 2-cyanoacetamide
    • Gross, K. C. 1982. A rapid and sensitive spectrophotometric method for assaying polygalacturonase using 2-cyanoacetamide. HortScience 17:933-934.
    • (1982) HortScience , vol.17 , pp. 933-934
    • Gross, K.C.1
  • 34
    • 0025880684 scopus 로고
    • A review of methods for the production and use of monoclonal antibodies to study zoosporic plant pathogens
    • Hardham, A. R., Gubler, F., Duniec, J., and Elliott, J. 1991. A review of methods for the production and use of monoclonal antibodies to study zoosporic plant pathogens. J. Microsc. 162:305-318.
    • (1991) J. Microsc. , vol.162 , pp. 305-318
    • Hardham, A.R.1    Gubler, F.2    Duniec, J.3    Elliott, J.4
  • 35
    • 0001596351 scopus 로고
    • Potato cell wall polysaccharides: Degradation with enzymes from Phytophthora infestans
    • Jarvis, M. C., Threlfall, D. R., and Friend, J. 1981. Potato cell wall polysaccharides: Degradation with enzymes from Phytophthora infestans. J. Exp. Bot. 32:1309-1319.
    • (1981) J. Exp. Bot. , vol.32 , pp. 1309-1319
    • Jarvis, M.C.1    Threlfall, D.R.2    Friend, J.3
  • 36
    • 0036137328 scopus 로고    scopus 로고
    • Sequence type analysis and recombinational tests (START)
    • Jolley, K. A., Feil, E. J., Chan, M.-S., and Maiden, M. C. J. 2001. Sequence type analysis and recombinational tests (START). Bioinformatics 17:1230-1231.
    • (2001) Bioinformatics , vol.17 , pp. 1230-1231
    • Jolley, K.A.1    Feil, E.J.2    Chan, M.-S.3    Maiden, M.C.J.4
  • 37
    • 0033394663 scopus 로고    scopus 로고
    • Initial assessment of gene diversity for the oomycete pathogen Phytophthora infestans based on expressed sequences
    • Kamoun, S., Hraber, P., Sobral, B., Nuss, D., and Govers, F. 1999. Initial assessment of gene diversity for the oomycete pathogen Phytophthora infestans based on expressed sequences. Fung. Genet. Biol. 28:94-106.
    • (1999) Fung. Genet. Biol. , vol.28 , pp. 94-106
    • Kamoun, S.1    Hraber, P.2    Sobral, B.3    Nuss, D.4    Govers, F.5
  • 38
    • 0034255126 scopus 로고    scopus 로고
    • Comparing sequenced segments of the tomato and Arabidopsis genomes: Large-scale duplication followed by selective gene loss creates a network of synteny
    • Ku, H.-M., Vision, T., Liu, J., and Tanksley, S. D. 2000. Comparing sequenced segments of the tomato and Arabidopsis genomes: Large-scale duplication followed by selective gene loss creates a network of synteny. Proc. Natl. Acad. Sci. U.S.A. 97:9121-9126.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 9121-9126
    • Ku, H.-M.1    Vision, T.2    Liu, J.3    Tanksley, S.D.4
  • 39
    • 0033522402 scopus 로고    scopus 로고
    • The specificity of polygalacturonase-inhibiting protein (PGIP): A single amino acid substitution in the solvent-exposed β-strand/β-turn region of the leucine-rich repeats (LRRs) confers a new recognition capability
    • Leckie, F., Mattei, B., Capodicasa, C., Hemmings, A., Nuss, L., Aracri, B., De Lorenzo, G., and Cervone, F. 1999. The specificity of polygalacturonase-inhibiting protein (PGIP): A single amino acid substitution in the solvent-exposed β-strand/β-turn region of the leucine-rich repeats (LRRs) confers a new recognition capability. EMBO (Eur. Mol. Biol. Organ.) J. 18:2352-2363.
    • (1999) EMBO (Eur. Mol. Biol. Organ.) J. , vol.18 , pp. 2352-2363
    • Leckie, F.1    Mattei, B.2    Capodicasa, C.3    Hemmings, A.4    Nuss, L.5    Aracri, B.6    De Lorenzo, G.7    Cervone, F.8
  • 40
    • 0029741776 scopus 로고    scopus 로고
    • Cloning and sequence analysis of elicitin genes of Phytophthora sojae
    • Mao, Y., and Tyler, B. M. 1996. Cloning and sequence analysis of elicitin genes of Phytophthora sojae. Fung. Genet. Biol. 20:169-172.
    • (1996) Fung. Genet. Biol. , vol.20 , pp. 169-172
    • Mao, Y.1    Tyler, B.M.2
  • 41
    • 0029799079 scopus 로고    scopus 로고
    • Purification of endo polygalacturonases from Sclerotinia sclerotiorum: Multiplicity of the complex enzyme system
    • Martel, M.-B., Létoublon, R., and Fèvre, M. 1996. Purification of endo polygalacturonases from Sclerotinia sclerotiorum: Multiplicity of the complex enzyme system. Curr. Microbiol. 33:243-248.
    • (1996) Curr. Microbiol. , vol.33 , pp. 243-248
    • Martel, M.-B.1    Létoublon, R.2    Fèvre, M.3
  • 42
    • 0031936749 scopus 로고    scopus 로고
    • Purification and characterization of two endopolygalacturonases secreted during the early stages of the saprophytic growth of Sclerotinia sclerotiorum
    • Martel, M.-B., Létoublon, R., and Fèvre, M. 1998. Purification and characterization of two endopolygalacturonases secreted during the early stages of the saprophytic growth of Sclerotinia sclerotiorum. FEMS (Fed. Eur. Microbiol. Soc.) Lett. 158:133-138.
    • (1998) FEMS (Fed. Eur. Microbiol. Soc.) Lett. , vol.158 , pp. 133-138
    • Martel, M.-B.1    Létoublon, R.2    Fèvre, M.3
  • 43
    • 0026708873 scopus 로고
    • Analyzing the structure of genes
    • Maynard Smith, J. 1992. Analyzing the structure of genes. J. Mol. Evol. 34:126-129.
    • (1992) J. Mol. Evol. , vol.34 , pp. 126-129
    • Maynard Smith, J.1
  • 44
    • 85032069287 scopus 로고
    • Infection structures of fungal plant pathogens - A cytological and physiological evaluation
    • Mendgen, K., and Deising, H. 1993. Infection structures of fungal plant pathogens-a cytological and physiological evaluation. New Phytol. 124:193-213.
    • (1993) New Phytol. , vol.124 , pp. 193-213
    • Mendgen, K.1    Deising, H.2
  • 45
    • 0029862029 scopus 로고    scopus 로고
    • Morphogenesis and mechanisms of penetration by plant pathogenic fungi
    • Mendgen, K., Hahn, M., and Deising, H. 1996. Morphogenesis and mechanisms of penetration by plant pathogenic fungi. Annu. Rev. Phytopathol. 34:367-386.
    • (1996) Annu. Rev. Phytopathol. , vol.34 , pp. 367-386
    • Mendgen, K.1    Hahn, M.2    Deising, H.3
  • 46
    • 0022507362 scopus 로고
    • Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions
    • Nei, M., and Gojobori, T. 1986. Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions. Mol. Biol. Evol. 3:418-426.
    • (1986) Mol. Biol. Evol. , vol.3 , pp. 418-426
    • Nei, M.1    Gojobori, T.2
  • 47
    • 0002973323 scopus 로고
    • Balanced polymorphism and evolution by the birth-and-death process in the MHC loci
    • K. Tsuji, M. Aizawa, and T. Sasazuki, eds. Oxford University Press, Oxford
    • Nei, M., and Hughes, A. L. 1992. Balanced polymorphism and evolution by the birth-and-death process in the MHC loci. Pages 27-38 in: Proceedings of the 11th International Histocompatibility Workshop and Conference, Vol. 2. K. Tsuji, M. Aizawa, and T. Sasazuki, eds. Oxford University Press, Oxford.
    • (1992) Proceedings of the 11th International Histocompatibility Workshop and Conference , vol.2 , pp. 27-38
    • Nei, M.1    Hughes, A.L.2
  • 48
    • 0031972161 scopus 로고    scopus 로고
    • Likelihood models for detecting positively selected amino acid sites and applications to the HIV-1 envelope gene
    • Nielsen, R., and Yang, Z. 1998. Likelihood models for detecting positively selected amino acid sites and applications to the HIV-1 envelope gene. Genetics 148:929-936.
    • (1998) Genetics , vol.148 , pp. 929-936
    • Nielsen, R.1    Yang, Z.2
  • 49
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S., and von Heijne, G. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 50
    • 0034703098 scopus 로고    scopus 로고
    • Subsite mapping of Aspergillus niger endopolygalacturonase II by site-directed mutagenesis
    • Pagès, S., Heijne, W. H. M., Kester, H. C. M., Visser, J., and Benen, J. A. E. 2000. Subsite mapping of Aspergillus niger endopolygalacturonase II by site-directed mutagenesis. J. Biol. Chem. 275:29348-29353.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29348-29353
    • Pagès, S.1    Heijne, W.H.M.2    Kester, H.C.M.3    Visser, J.4    Benen, J.A.E.5
  • 51
    • 0029411299 scopus 로고
    • Characterization of a gene cluster of Phytophthora cryptogea which codes for elicitins, proteins inducing a hypersensitive-like response in tobacco
    • Panabières, F., Marais, A., Le Berre, J.-Y., Penot, I., Fournier, D., and Ricci, P. 1995. Characterization of a gene cluster of Phytophthora cryptogea which codes for elicitins, proteins inducing a hypersensitive-like response in tobacco. Mol. Plant-Microbe Interact. 8:996-1003.
    • (1995) Mol. Plant-Microbe Interact. , vol.8 , pp. 996-1003
    • Panabières, F.1    Marais, A.2    Le Berre, J.-Y.3    Penot, I.4    Fournier, D.5    Ricci, P.6
  • 52
    • 0032518433 scopus 로고    scopus 로고
    • pgaE encodes a fourth member of the endopolygalacturonase gene family from Aspergillus niger
    • Pařenicová, L., Benen, J. A. E., Kester, H. C. M., and Visser, J. 1998. pgaE encodes a fourth member of the endopolygalacturonase gene family from Aspergillus niger. Eur. J. Biochem. 251:72-80.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 72-80
    • Pařenicová, L.1    Benen, J.A.E.2    Kester, H.C.M.3    Visser, J.4
  • 53
    • 0034142291 scopus 로고    scopus 로고
    • pgaA and pgaB encode two constitutively expressed endopolygalacturonases of Aspergillus niger
    • Pařenicová, L., Benen, J. A. E., Kester, H. C. M., and Visser, J. 2000a. pgaA and pgaB encode two constitutively expressed endopolygalacturonases of Aspergillus niger. Biochem. J. 345:637-644.
    • (2000) Biochem. J. , vol.345 , pp. 637-644
    • Pařenicová, L.1    Benen, J.A.E.2    Kester, H.C.M.3    Visser, J.4
  • 54
    • 0343114331 scopus 로고    scopus 로고
    • Characterization of a novel endopolygalacturonase from Aspergillus niger with unique kinetic properties
    • Pařenicová, L., Kester, H. C. M., Benen, J. A. E., and Visser, J. 2000b. Characterization of a novel endopolygalacturonase from Aspergillus niger with unique kinetic properties. FEBS (Fed. Eur. Biochem. Soc.) Lett. 467:333-336.
    • (2000) FEBS (Fed. Eur. Biochem. Soc.) Lett. , vol.467 , pp. 333-336
    • Pařenicová, L.1    Kester, H.C.M.2    Benen, J.A.E.3    Visser, J.4
  • 55
    • 0033545987 scopus 로고    scopus 로고
    • Recombination between diverged clusters of the tomato Cf-9 plant disease resistance gene family
    • Parniske, M., and Jones, J. D. G. 1999. Recombination between diverged clusters of the tomato Cf-9 plant disease resistance gene family. Proc. Natl. Acad. Sci. U.S.A. 96:5850-5855.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 5850-5855
    • Parniske, M.1    Jones, J.D.G.2
  • 56
    • 0029004590 scopus 로고
    • Protein modeling by e-mail
    • Peitsch, M. C. 1995. Protein modeling by e-mail. Biotechnol. 13:658-660.
    • (1995) Biotechnol. , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 57
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling
    • Peitsch, M. C. 1996. ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling. Biochem. Soc. Trans. 24:274-279.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 274-279
    • Peitsch, M.C.1
  • 59
    • 0032544357 scopus 로고    scopus 로고
    • Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora
    • Pickersgill, R., Smith, D., Worboys, K., and Jenkins, J. 1998. Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora. J. Biol. Chem. 273:24660-24664.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24660-24664
    • Pickersgill, R.1    Smith, D.2    Worboys, K.3    Jenkins, J.4
  • 61
    • 0034662974 scopus 로고    scopus 로고
    • Requirement for either a host- or pectin-induced pectate lyase for infection of Pisum sativum by Nectria hematococca
    • Rogers, L. M., Kim, Y.-K., Guo, W. J., Gonzáles-Candelas, L., Li, D., and Kolattukudy, P. E. 2000. Requirement for either a host- or pectin-induced pectate lyase for infection of Pisum sativum by Nectria hematococca. Proc. Natl. Acad. Sci. U.S.A. 97:9813-9818.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 9813-9818
    • Rogers, L.M.1    Kim, Y.-K.2    Guo, W.J.3    Gonzáles-Candelas, L.4    Li, D.5    Kolattukudy, P.E.6
  • 64
    • 0028118252 scopus 로고
    • Involvement of suppressor-glucans and plant epidermal cells in host-selective pathogenesis of Phytophthora capsici
    • Sanchez, L. M., Doke, N., Ban, Y., and Kawakita, K. 1994. Involvement of suppressor-glucans and plant epidermal cells in host-selective pathogenesis of Phytophthora capsici. J. Phytopathol. 140:153-164.
    • (1994) J. Phytopathol. , vol.140 , pp. 153-164
    • Sanchez, L.M.1    Doke, N.2    Ban, Y.3    Kawakita, K.4
  • 68
    • 0028011593 scopus 로고
    • Polygalacturonase inhibitors of Bartlett pear fruits: Differential effects on Botrytis cinerea polygalacturonase isozymes, and influence on products of fungal hydrolysis of pear cell walls and on ethylene induction in cell culture
    • Sharrock, K. R., and Labavitch, J. M. 1994. Polygalacturonase inhibitors of Bartlett pear fruits: Differential effects on Botrytis cinerea polygalacturonase isozymes, and influence on products of fungal hydrolysis of pear cell walls and on ethylene induction in cell culture. Physiol. Mol. Plant Pathol. 45:305-319.
    • (1994) Physiol. Mol. Plant Pathol. , vol.45 , pp. 305-319
    • Sharrock, K.R.1    Labavitch, J.M.2
  • 69
    • 0030824374 scopus 로고    scopus 로고
    • Molecular genetic evidence for the involvement of a specific polygalacturonase, P2c, in the invasion and spread of Aspergillus flavus in cotton bolls
    • Shieh, M.-T., Brown, R. L., Whitehead, M. P., Cary, J. W., Cotty, P. J., Cleveland, T. E., and Dean, R. A. 1997. Molecular genetic evidence for the involvement of a specific polygalacturonase, P2c, in the invasion and spread of Aspergillus flavus in cotton bolls. Appl. Environ. Microbiol. 63:3548-3552.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3548-3552
    • Shieh, M.-T.1    Brown, R.L.2    Whitehead, M.P.3    Cary, J.W.4    Cotty, P.J.5    Cleveland, T.E.6    Dean, R.A.7
  • 70
    • 0031893975 scopus 로고    scopus 로고
    • Evolution of the protists and protistan parasites from the perspective of molecular systemics
    • Sogin, M. L., and Silberman, J. D. 1998. Evolution of the protists and protistan parasites from the perspective of molecular systemics. Int. J. Parasitol. 28:11-20.
    • (1998) Int. J. Parasitol. , vol.28 , pp. 11-20
    • Sogin, M.L.1    Silberman, J.D.2
  • 71
  • 73
    • 0027475615 scopus 로고
    • Pectinase Aspergillus sp. polygalacturonase: Multiplicity, divergence, and structural patterns linking fungal, bacterial, and plant polygalacturonases
    • Stratilová, E., Markovič, O., Škrovinová, D., Rexová-Benková, L., and Jörnvall, H. 1993. Pectinase Aspergillus sp. polygalacturonase: Multiplicity, divergence, and structural patterns linking fungal, bacterial, and plant polygalacturonases. J. Protein Chem. 12:15-22.
    • (1993) J. Protein Chem. , vol.12 , pp. 15-22
    • Stratilová, E.1    Markovič, O.2    Škrovinová, D.3    Rexová-Benková, L.4    Jörnvall, H.5
  • 77
    • 0032190199 scopus 로고    scopus 로고
    • The endopolygalacturonase gene Bcpg 1 is required for full virulence of Botrytis cinerea
    • ten Have, A., Mulder, W., Visser, J., and van Kan, J. A. L. 1998. The endopolygalacturonase gene Bcpg 1 is required for full virulence of Botrytis cinerea. Mol. Plant-Microbe Interact. 11:1009-1016.
    • (1998) Mol. Plant-Microbe Interact. , vol.11 , pp. 1009-1016
    • Ten Have, A.1    Mulder, W.2    Visser, J.3    Van Kan, J.A.L.4
  • 78
    • 0035571423 scopus 로고    scopus 로고
    • Botrytis cinerea endopolygalacturonase genes are differentially expressed in various plant tissues
    • ten Have, A., Breuil, W. O., Wubben, J. P., Visser, J., and van Kan, J. A. L. 2001. Botrytis cinerea endopolygalacturonase genes are differentially expressed in various plant tissues. Fungal Genet. Biol. 33:97-105.
    • (2001) Fungal Genet. Biol. , vol.33 , pp. 97-105
    • Ten Have, A.1    Breuil, W.O.2    Wubben, J.P.3    Visser, J.4    Van Kan, J.A.L.5
  • 79
    • 0029977534 scopus 로고    scopus 로고
    • Structure and expression of two polygalacturonase genes of Claviceps purpurea oriented in tandem and cytological evidence for pectinolytic enzyme activity during infection of rye
    • Tenberge, K. B., Homann, V., Oeser, B., and Tudzynski, P. 1996. Structure and expression of two polygalacturonase genes of Claviceps purpurea oriented in tandem and cytological evidence for pectinolytic enzyme activity during infection of rye. Phytopathology 86:1084-1097.
    • (1996) Phytopathology , vol.86 , pp. 1084-1097
    • Tenberge, K.B.1    Homann, V.2    Oeser, B.3    Tudzynski, P.4
  • 80
    • 0033978739 scopus 로고    scopus 로고
    • Characterization of a ubiquitous expressed gene family encoding polygalacturonase in Arabidopsis thaliana
    • Torki, M., Mandaron, P., Mache, R., and Falconet, D. 2000. Characterization of a ubiquitous expressed gene family encoding polygalacturonase in Arabidopsis thaliana. Gene 242:427-436.
    • (2000) Gene , vol.242 , pp. 427-436
    • Torki, M.1    Mandaron, P.2    Mache, R.3    Falconet, D.4
  • 81
    • 0036010552 scopus 로고    scopus 로고
    • The pipg 1 gene of the oomycete Phytophthora infestans encodes a fungal-like endopolygalacturonase
    • Torto, T. A., Rauser, L., and Kamoun, S. 2002. The pipg 1 gene of the oomycete Phytophthora infestans encodes a fungal-like endopolygalacturonase. Curr. Genet. 40:385-390.
    • (2002) Curr. Genet. , vol.40 , pp. 385-390
    • Torto, T.A.1    Rauser, L.2    Kamoun, S.3
  • 83
    • 0032589464 scopus 로고    scopus 로고
    • 1.68-Å crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis
    • van Santen, Y., Benen, J. A. E., Schröter, K.-H., Kalk, K. H., Armand, S., Visser, J., and Dijkstra, B. W. 1999. 1.68-Å crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis. J. Biol. Chem. 274:30474-30480.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30474-30480
    • Van Santen, Y.1    Benen, J.A.E.2    Schröter, K.-H.3    Kalk, K.H.4    Armand, S.5    Visser, J.6    Dijkstra, B.W.7
  • 85
    • 0031892518 scopus 로고    scopus 로고
    • Phylogenetic profiles: A graphical method for detecting genetic recombinations in homologous sequences
    • Weiller, G. F. 1998. Phylogenetic profiles: A graphical method for detecting genetic recombinations in homologous sequences. Mol. Biol. Evol. 15:326-335.
    • (1998) Mol. Biol. Evol. , vol.15 , pp. 326-335
    • Weiller, G.F.1
  • 86
    • 0032949792 scopus 로고    scopus 로고
    • Cloning and partial characterization of endopolygalacturonase genes from Botrytis cinerea
    • Wubben, J. P., Mulder, W., ten Have, A., van Kan, J. A. L., and Visser, J. 1999. Cloning and partial characterization of endopolygalacturonase genes from Botrytis cinerea. Appl. Environ. Microbiol. 65:1596-1602.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1596-1602
    • Wubben, J.P.1    Mulder, W.2    Ten Have, A.3    Van Kan, J.A.L.4    Visser, J.5
  • 87
    • 0034060901 scopus 로고    scopus 로고
    • Regulation of endopolygalacturonase gene expression in Botrytis cinerea by galacturonic acid, ambient pH and carbon catabolite repression
    • Wubben, J. P., ten Have, A., van Kan, J. A. L., and Visser, J. 2000. Regulation of endopolygalacturonase gene expression in Botrytis cinerea by galacturonic acid, ambient pH and carbon catabolite repression. Curr. Genet. 37:152-157.
    • (2000) Curr. Genet. , vol.37 , pp. 152-157
    • Wubben, J.P.1    Ten Have, A.2    Van Kan, J.A.L.3    Visser, J.4
  • 88
    • 0030220095 scopus 로고    scopus 로고
    • The structural role of sugars in glycoproteins
    • Wyss, D. F., and Wagner, G. 1996. The structural role of sugars in glycoproteins. Curr. Opin. Biotechnol. 7:409-416.
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 409-416
    • Wyss, D.F.1    Wagner, G.2
  • 89
    • 0033639150 scopus 로고    scopus 로고
    • Statistical methods for detecting molecular adaptation
    • Yang, Z., and Bielawski, J. P. 2000. Statistical methods for detecting molecular adaptation. Trends Ecol. Evol. 15:496-503.
    • (2000) Trends Ecol. Evol. , vol.15 , pp. 496-503
    • Yang, Z.1    Bielawski, J.P.2
  • 90
    • 0033979433 scopus 로고    scopus 로고
    • Estimating synonymous and nonsynonymous substitution rates under realistic evolutionary models
    • Yang, Z., and Nielsen, R. 2000. Estimating synonymous and nonsynonymous substitution rates under realistic evolutionary models. Mol. Biol. Evol. 17:32-43.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 32-43
    • Yang, Z.1    Nielsen, R.2
  • 91
    • 0034097381 scopus 로고    scopus 로고
    • Codon-substitution models for heterogeneous selection pressure at amino acid sites
    • Yang, Z., Nielsen, R., Goldman, N., and Pedersen, A.-M. K. 2000. Codon-substitution models for heterogeneous selection pressure at amino acid sites. Genetics 155:431-449.
    • (2000) Genetics , vol.155 , pp. 431-449
    • Yang, Z.1    Nielsen, R.2    Goldman, N.3    Pedersen, A.-M.K.4
  • 92
    • 0029202114 scopus 로고
    • Purification and characterization of a polygalacturonase-inhibiting protein from apple fruit
    • Yao, C., Conway, W. S., and Sams, C. E. 1995. Purification and characterization of a polygalacturonase-inhibiting protein from apple fruit. Phytopathology 85:1373-1377.
    • (1995) Phytopathology , vol.85 , pp. 1373-1377
    • Yao, C.1    Conway, W.S.2    Sams, C.E.3
  • 93
    • 0011052091 scopus 로고
    • A non-pectolytic protein from Phytophthora capsici that macerates plant tissue
    • Yoshikawa, M., Tsukadaira, T., Masago, H., and Minoura, S. 1977. A non-pectolytic protein from Phytophthora capsici that macerates plant tissue. Physiol. Plant Pathol. 11:61-70.
    • (1977) Physiol. Plant Pathol. , vol.11 , pp. 61-70
    • Yoshikawa, M.1    Tsukadaira, T.2    Masago, H.3    Minoura, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.