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Volumn 50, Issue 3, 1997, Pages 197-212

Pectate lyase of Colletotrichum gloeosporioides attacking avocado fruits: cDNA cloning and involvement in pathogenicity

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); CARICA PAPAYA; COLLETOTRICHUM; COLLETOTRICHUM GLOEOSPORIOIDES; COLLETOTRICHUM MUSAE; FUNGI; GLOMERELLA CINGULATA; MANGIFERA INDICA; PERSEA AMERICANA;

EID: 0030841224     PISSN: 08855765     EISSN: None     Source Type: Journal    
DOI: 10.1006/pmpp.1997.0080     Document Type: Article
Times cited : (39)

References (36)
  • 1
    • 0025938675 scopus 로고
    • A 30-residue-long "export initiation domain" adjacent to the signal sequence is critical for protein translocation across the inner membrane ofEscherichia coli.
    • Anderson H, von Heijne G. A 30-residue-long "export initiation domain" adjacent to the signal sequence is critical for protein translocation across the inner membrane ofEscherichia coli. Proceedings of the National Academy of Science USA. 88:1991;9751-9754.
    • (1991) Proceedings of the National Academy of Science USA , vol.88 , pp. 9751-9754
    • Anderson, H.1    Von Heijne, G.2
  • 2
    • 0037985959 scopus 로고
    • Extracellular enzymes produced byColletotrichum lindemuthianumHelminthosporium maydis
    • Anderson AJ. Extracellular enzymes produced byColletotrichum lindemuthianumHelminthosporium maydis. Phytopathology. 68:1978;1585-1589.
    • (1978) Phytopathology , vol.68 , pp. 1585-1589
    • Anderson, A.J.1
  • 3
    • 0001137346 scopus 로고
    • Degradation of plant cell walls and membranes by microbial enzymes
    • Springer-Verlage
    • Bateman DF, Basham GH. Degradation of plant cell walls and membranes by microbial enzymes. Encyclopedia of Plant Physiology. 1976;Springer-Verlage.
    • (1976) Encyclopedia of Plant Physiology
    • Bateman, D.F.1    Basham, G.H.2
  • 6
  • 8
    • 0024619547 scopus 로고
    • Regulation of theAspergillus nidulansPLA
    • Dean RA, Timberlake WA. Regulation of theAspergillus nidulansPLA. Plant Cell. 1:1989;275-284.
    • (1989) Plant Cell , vol.1 , pp. 275-284
    • Dean, R.A.1    Timberlake, W.A.2
  • 9
    • 0005708639 scopus 로고
    • A cell wall degrading endopolygalacturonase secreted byColletotrichum lindemuthianum.
    • English PD, Maglothin A, Keegstra K, Albershem P. A cell wall degrading endopolygalacturonase secreted byColletotrichum lindemuthianum. Plant Physiology. 49:1972;293-297.
    • (1972) Plant Physiology , vol.49 , pp. 293-297
    • English, P.D.1    Maglothin, A.2    Keegstra, K.3    Albershem, P.4
  • 10
    • 0026702554 scopus 로고
    • Isolation and analysis of a novel inducible pectate lyase gene from the phytopathogenic fungusFusarium solanipisi
    • Gonzalez-Candelas L, Kolattukudy PE. Isolation and analysis of a novel inducible pectate lyase gene from the phytopathogenic fungusFusarium solanipisi. Journal of Bacteriology. 174:1992;6343-6349.
    • (1992) Journal of Bacteriology , vol.174 , pp. 6343-6349
    • Gonzalez-Candelas, L.1    Kolattukudy, P.E.2
  • 11
    • 0028894866 scopus 로고
    • Cloning of constitutively expressed pectate lyase genepelFusarium solanipisiNectria haematococca,Pichia pastoris.
    • Guo W, Gonzalez-Candelas L, Kolattukudy PE. Cloning of constitutively expressed pectate lyase genepelFusarium solanipisiNectria haematococca,Pichia pastoris. Journal of Bacteriology. 177:1995;7070-7077.
    • (1995) Journal of Bacteriology , vol.177 , pp. 7070-7077
    • Guo, W.1    Gonzalez-Candelas, L.2    Kolattukudy, P.E.3
  • 12
  • 13
    • 0025290014 scopus 로고
    • Isolation and structure of the pectin lyase D-encoding gene fromAspergillus niger.
    • Gysler C, Harmsen JAM, Kester HCM, Visser J, Heim J. Isolation and structure of the pectin lyase D-encoding gene fromAspergillus niger. Gene. 89:1990;101-108.
    • (1990) Gene , vol.89 , pp. 101-108
    • Gysler, C.1    Harmsen, J.A.M.2    Kester, H.C.M.3    Visser, J.4    Heim, J.5
  • 14
    • 0029257437 scopus 로고
    • Functional implications of structural-based sequence alignment of proteins in the extracellular pectate lyase superfamily
    • Henrissat B, Heffron SE, Yoder MD, Lietzke SE, Jurnak F. Functional implications of structural-based sequence alignment of proteins in the extracellular pectate lyase superfamily. Plant Physiology. 107:1995;963-976.
    • (1995) Plant Physiology , vol.107 , pp. 963-976
    • Henrissat, B.1    Heffron, S.E.2    Yoder, M.D.3    Lietzke, S.E.4    Jurnak, F.5
  • 16
    • 0023036933 scopus 로고
    • Structure of two pectate lyase genes fromErwinia chrysanthemiEscherichia coli.
    • Keen NT, Tamaki S. Structure of two pectate lyase genes fromErwinia chrysanthemiEscherichia coli. Journal of Bacteriology. 168:1986;595-606.
    • (1986) Journal of Bacteriology , vol.168 , pp. 595-606
    • Keen, N.T.1    Tamaki, S.2
  • 17
    • 0027136944 scopus 로고
    • Compartmentalization of antifungal compounds in oil cells of avocado fruit mesocarp and its effect on susceptibility toColletotrichum gloeosporioides.
    • Kobiler I, Prusky D, Midland S, Sims JJ, Keen NT. Compartmentalization of antifungal compounds in oil cells of avocado fruit mesocarp and its effect on susceptibility toColletotrichum gloeosporioides. Physiological and Molecular Plant Pathology. 43:1993;319-328.
    • (1993) Physiological and Molecular Plant Pathology , vol.43 , pp. 319-328
    • Kobiler, I.1    Prusky, D.2    Midland, S.3    Sims, J.J.4    Keen, N.T.5
  • 18
    • 0000905412 scopus 로고
    • An extracellular pectate lyase is the pathogenicity factor of the soft rotting bacteriumPseudomonas viridiflava.
    • Liao C-H, Hung H-Y, Chatterjee AK. An extracellular pectate lyase is the pathogenicity factor of the soft rotting bacteriumPseudomonas viridiflava. Molecular Plant-Microbe Interactions. 1:1988;199-206.
    • (1988) Molecular Plant-Microbe Interactions , vol.1 , pp. 199-206
    • Liao C-H1    Hung H-Y2    Chatterjee, A.K.3
  • 21
    • 0001555486 scopus 로고
    • Involvement of preformed antifungal compounds in the resistance of subtropical fruits to fungal decay
    • Prusky D, Keen NT. Involvement of preformed antifungal compounds in the resistance of subtropical fruits to fungal decay. Plant Disease. 77:1993;114-119.
    • (1993) Plant Disease , vol.77 , pp. 114-119
    • Prusky, D.1    Keen, N.T.2
  • 22
    • 0001442191 scopus 로고
    • Further evidence for the involvement of a preformed antifungal compound in the latency ofColletotrichum gloeosporioides
    • Prusky D, Keen NT, Sims JJ, Eaks IL. Further evidence for the involvement of a preformed antifungal compound in the latency ofColletotrichum gloeosporioides. Physiological and Molecular Plant Pathology. 22:1983;189-198.
    • (1983) Physiological and Molecular Plant Pathology , vol.22 , pp. 189-198
    • Prusky, D.1    Keen, N.T.2    Sims, J.J.3    Eaks, I.L.4
  • 23
    • 0026954827 scopus 로고
    • Isolation and characterization of a tobacco gene with homology to pectate lyase which is specifically expressed during microsporogenesis
    • Rogers HJ, Harvey A, Lonsdale DM. Isolation and characterization of a tobacco gene with homology to pectate lyase which is specifically expressed during microsporogenesis. Plant Molecular Biology. 20:1992;493-502.
    • (1992) Plant Molecular Biology , vol.20 , pp. 493-502
    • Rogers, H.J.1    Harvey, A.2    Lonsdale, D.M.3
  • 25
    • 0025576522 scopus 로고
    • Endopolygalacturonase is not required for pathogenicity ofCochliobolus carbonum
    • Scott-Craig JS, Panaccione DG, Cervone F, Walton JD. Endopolygalacturonase is not required for pathogenicity ofCochliobolus carbonum. Plant Cell. 2:1990;1191-1200.
    • (1990) Plant Cell , vol.2 , pp. 1191-1200
    • Scott-Craig, J.S.1    Panaccione, D.G.2    Cervone, F.3    Walton, J.D.4
  • 29
    • 0026448561 scopus 로고
    • Cloning and molecular characterization of the glyceraldehyde-3-phosphate dehydrogenase-encoding gene and cDNA from the plant pathogenic fungusGlomerella cingulata
    • Templeton MD, Rikkerink EHA, Solon SL, Crowhurst RN. Cloning and molecular characterization of the glyceraldehyde-3-phosphate dehydrogenase-encoding gene and cDNA from the plant pathogenic fungusGlomerella cingulata. Gene. 122:1992;225-330.
    • (1992) Gene , vol.122 , pp. 225-330
    • Templeton, M.D.1    Rikkerink, E.H.A.2    Solon, S.L.3    Crowhurst, R.N.4
  • 30
    • 0028007674 scopus 로고
    • Deconstructing the cell wall
    • Walton JD. Deconstructing the cell wall. Plant Physiology. 104:1994;1113-1118.
    • (1994) Plant Physiology , vol.104 , pp. 1113-1118
    • Walton, J.D.1
  • 31
    • 0028385026 scopus 로고
    • Purification of pectate lyase produced byColletotrichum gloeosporioides
    • Wattad C, Dinoor A, Prusky D. Purification of pectate lyase produced byColletotrichum gloeosporioides. Molecular Plant-Microbe Interactions. 7:1994;293-297.
    • (1994) Molecular Plant-Microbe Interactions , vol.7 , pp. 293-297
    • Wattad, C.1    Dinoor, A.2    Prusky, D.3
  • 34
    • 0025220288 scopus 로고
    • Molecular and genetic characterization of two pollen-expressed genes that have sequence similarity to pectate lyase of the plant pathogenErwinia.
    • Wing RA, Yamaguchi J, Larabell SK, Ursin VM, McCormick S. Molecular and genetic characterization of two pollen-expressed genes that have sequence similarity to pectate lyase of the plant pathogenErwinia. Plant Molecular Biology. 14:1989;17-28.
    • (1989) Plant Molecular Biology , vol.14 , pp. 17-28
    • Wing, R.A.1    Yamaguchi, J.2    Larabell, S.K.3    Ursin, V.M.4    McCormick, S.5
  • 35
    • 0027329090 scopus 로고
    • New domain motif: The structure of pectate lyase C: A secreted plant virulence factor
    • Yoder MD, Keen NT, Jurnak F. New domain motif: the structure of pectate lyase C: a secreted plant virulence factor. Science. 260:1993;1503-1507.
    • (1993) Science , vol.260 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3
  • 36
    • 0027918655 scopus 로고
    • Unusual structural features of the parallel β helix of the pectate lyases
    • Yoder MD, Lietzeke SE, Jurnak F. Unusual structural features of the parallel β helix of the pectate lyases. Structure. 1:1993;241-251.
    • (1993) Structure , vol.1 , pp. 241-251
    • Yoder, M.D.1    Lietzeke, S.E.2    Jurnak, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.