메뉴 건너뛰기




Volumn 179, Issue 8, 1997, Pages 2503-2511

Comparative analysis of the five major Erwinia chrysanthemi pectate lyases: Enzyme characteristics and potential inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

PECTATE LYASE;

EID: 0030944441     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.8.2503-2511.1997     Document Type: Article
Times cited : (129)

References (49)
  • 1
    • 34250100367 scopus 로고
    • Resolution of four pectate lyase structural genes of Erwinia chrysanthemi (EC16) and characterization of the enzymes produced in Escherichia coli
    • Barras, F., K. K. Thurn, and A. K. Chatterjee. 1987. Resolution of four pectate lyase structural genes of Erwinia chrysanthemi (EC16) and characterization of the enzymes produced in Escherichia coli. Mol. Gen. Genet. 209:319-325.
    • (1987) Mol. Gen. Genet. , vol.209 , pp. 319-325
    • Barras, F.1    Thurn, K.K.2    Chatterjee, A.K.3
  • 2
    • 0029059886 scopus 로고
    • Synergism between Erwinia pectate lyase isoenzymes that depolymerized both pectate and pectin
    • Bartling, S., C. Wegener, and O. Olsen. 1995. Synergism between Erwinia pectate lyase isoenzymes that depolymerized both pectate and pectin. Microbiology 141:873-881.
    • (1995) Microbiology , vol.141 , pp. 873-881
    • Bartling, S.1    Wegener, C.2    Olsen, O.3
  • 3
    • 0011870380 scopus 로고
    • Relationship of cell death in plant tissue treated with a homogeneous endo-pectate lyase to cell wall degradation
    • Basham, H. G., and D. F. Bateman. 1975. Relationship of cell death in plant tissue treated with a homogeneous endo-pectate lyase to cell wall degradation. Physiol. Plant Pathol. 5:249-262.
    • (1975) Physiol. Plant Pathol. , vol.5 , pp. 249-262
    • Basham, H.G.1    Bateman, D.F.2
  • 4
    • 0000424838 scopus 로고
    • Pathogenic behavior of pectinase-defective Erwinia chrysanthemi mutants on different plants
    • Beaulieu, C., M. Boccara, and F. Van Gijsegem. 1993. Pathogenic behavior of pectinase-defective Erwinia chrysanthemi mutants on different plants. Mol. Plant-Microbe Interact. 6:197-202.
    • (1993) Mol. Plant-Microbe Interact. , vol.6 , pp. 197-202
    • Beaulieu, C.1    Boccara, M.2    Van Gijsegem, F.3
  • 5
    • 0021215813 scopus 로고
    • Detection of depolymerase isoenzymes after electrophoresis or electrofocusing, or in titration curves
    • Bertheau, Y., E. Madgidi-Hervan, A. Kotoujansky, C. Nguyen-The, T. Andro, and A. Coleno. 1984. Detection of depolymerase isoenzymes after electrophoresis or electrofocusing, or in titration curves. Anal. Biochem. 139:383-389.
    • (1984) Anal. Biochem. , vol.139 , pp. 383-389
    • Bertheau, Y.1    Madgidi-Hervan, E.2    Kotoujansky, A.3    Nguyen-The, C.4    Andro, T.5    Coleno, A.6
  • 6
    • 85036442318 scopus 로고    scopus 로고
    • Personal communication
    • 5a.Bertheau, Y. Personal communication.
    • Bertheau, Y.1
  • 7
    • 0002725779 scopus 로고
    • The role of individual pectate lyases of Erwinia chrysanthemi strain 3937 in pathogenicity on Saintpaulia plants
    • Boccara, M., A. Diolez, M. Rouve, and A. Kotoujansky. 1988. The role of individual pectate lyases of Erwinia chrysanthemi strain 3937 in pathogenicity on Saintpaulia plants. Physiol. Mol. Plant Pathol. 33:95-104.
    • (1988) Physiol. Mol. Plant Pathol. , vol.33 , pp. 95-104
    • Boccara, M.1    Diolez, A.2    Rouve, M.3    Kotoujansky, A.4
  • 8
    • 0025605026 scopus 로고
    • Molecular cloning of the structural gene for exopolygalacturonate lyase from Erwinia chrysanthemi EC16 and characterization of the enzyme product
    • Brooks, A. D., S. Y. He, S. Gold, N. T. Keen, A. Collmer, and S. W. Hutcheson. 1990. Molecular cloning of the structural gene for exopolygalacturonate lyase from Erwinia chrysanthemi EC16 and characterization of the enzyme product. J. Bacteriol. 172:6950-6958.
    • (1990) J. Bacteriol. , vol.172 , pp. 6950-6958
    • Brooks, A.D.1    He, S.Y.2    Gold, S.3    Keen, N.T.4    Collmer, A.5    Hutcheson, S.W.6
  • 9
    • 0021966134 scopus 로고
    • Molecular cloning in Escherichia coli of Erwinia chrysanthemi genes encoding multiple forms of pectate lyase
    • Collmer, A., C. Schoedel, D. L. Roeder, J. L. Ried, and J. F. Rissler. 1985. Molecular cloning in Escherichia coli of Erwinia chrysanthemi genes encoding multiple forms of pectate lyase. J. Bacteriol. 161:913-920.
    • (1985) J. Bacteriol. , vol.161 , pp. 913-920
    • Collmer, A.1    Schoedel, C.2    Roeder, D.L.3    Ried, J.L.4    Rissler, J.F.5
  • 11
    • 0026513432 scopus 로고
    • Purification of the acidic pectate lyase of Erwinia chrysanthemi 3937 and sequence analysis of the corresponding gene
    • Favey, S., C. Bourson, Y. Bertheau, A. Kotoujansky, and M. Boccara. 1992. Purification of the acidic pectate lyase of Erwinia chrysanthemi 3937 and sequence analysis of the corresponding gene. J. Gen. Microbiol. 138:499-508.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 499-508
    • Favey, S.1    Bourson, C.2    Bertheau, Y.3    Kotoujansky, A.4    Boccara, M.5
  • 12
    • 0001952007 scopus 로고
    • Pectic enzymes produced by Erwinia chrysanthemi and their effects on plant tissue
    • Garibaldi, A., and D. F. Bateman. 1971. Pectic enzymes produced by Erwinia chrysanthemi and their effects on plant tissue. Physiol. Plant Pathol. 1:25-40.
    • (1971) Physiol. Plant Pathol. , vol.1 , pp. 25-40
    • Garibaldi, A.1    Bateman, D.F.2
  • 14
    • 0029257437 scopus 로고
    • Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase superfamily
    • Henrissat, B., S. E. Heffron, M. D. Yoder, S. E. Lietzke, and F. Jurnak. 1995. Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase superfamily. Plant Physiol. 107:963-976.
    • (1995) Plant Physiol. , vol.107 , pp. 963-976
    • Henrissat, B.1    Heffron, S.E.2    Yoder, M.D.3    Lietzke, S.E.4    Jurnak, F.5
  • 15
    • 0024853451 scopus 로고
    • Extracellular and periplasmic isoenzymes of pectate lyase from Erwinia carotovora subspecies carotovora belong to different gene families
    • Hinton, J. C. D., J. M. Sidebotham, D. R. Gill, and G. P. C. Salmond. 1989. Extracellular and periplasmic isoenzymes of pectate lyase from Erwinia carotovora subspecies carotovora belong to different gene families. Mol. Microbiol. 3:1785-1795.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1785-1795
    • Hinton, J.C.D.1    Sidebotham, J.M.2    Gill, D.R.3    Salmond, G.P.C.4
  • 17
    • 0026470914 scopus 로고
    • Environmental conditions affect the transcription of the pectinase genes of Erwinia chrysanthemi 3937
    • Hugouvieux-Cotte-Pattat, N., H. Dominguez, and J. Robert-Baudouy. 1992. Environmental conditions affect the transcription of the pectinase genes of Erwinia chrysanthemi 3937. J. Bacteriol. 174:7807-7818.
    • (1992) J. Bacteriol. , vol.174 , pp. 7807-7818
    • Hugouvieux-Cotte-Pattat, N.1    Dominguez, H.2    Robert-Baudouy, J.3
  • 18
    • 0026667574 scopus 로고
    • Analysis of the regulation of pelBC genes in Erwinia chrysanthemi 3937
    • Hugouvieux-Cotte-Pattat, N., and J. Robert-Baudouy. 1992. Analysis of the regulation of pelBC genes in Erwinia chrysanthemi 3937. Mol. Microbiol 6:2363-2376.
    • (1992) Mol. Microbiol , vol.6 , pp. 2363-2376
    • Hugouvieux-Cotte-Pattat, N.1    Robert-Baudouy, J.2
  • 19
    • 0021127426 scopus 로고
    • Molecular cloning of pectate lyase genes from Erwinia chrysanthemi and their expression in Escherichia coli
    • Keen, N. T., D. Dahlbeck, B. Staskawicz, and W. Belser. 1984. Molecular cloning of pectate lyase genes from Erwinia chrysanthemi and their expression in Escherichia coli. J. Bacteriol. 159:825-831.
    • (1984) J. Bacteriol. , vol.159 , pp. 825-831
    • Keen, N.T.1    Dahlbeck, D.2    Staskawicz, B.3    Belser, W.4
  • 20
    • 0023036933 scopus 로고
    • Structure of two pectate lyase genes from Erwinia chrysanthemi EC16 and their expression in Escherichia coli
    • Keen, N. T., and S. Tamaki. 1986. Structure of two pectate lyase genes from Erwinia chrysanthemi EC16 and their expression in Escherichia coli, J. Bacteriol. 168:595-606.
    • (1986) J. Bacteriol. , vol.168 , pp. 595-606
    • Keen, N.T.1    Tamaki, S.2
  • 21
    • 0027258413 scopus 로고
    • Erwinia chrysanthemi EC16 produces a second set of plant-inducible pectate lyase isoenzymes
    • Kelemu, S., and A. Collmer. 1993. Erwinia chrysanthemi EC16 produces a second set of plant-inducible pectate lyase isoenzymes. Appl. Environ. Microbiol. 59:1756-1761.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1756-1761
    • Kelemu, S.1    Collmer, A.2
  • 22
    • 0028191528 scopus 로고
    • The three dimensional structure of pectate lyase E, a plant virulence factor from Erwinia chrysanthemi
    • Lietzke, S. E., M. D. Yoder, N. T. Keen, and F. Jurnak. 1994. The three dimensional structure of pectate lyase E, a plant virulence factor from Erwinia chrysanthemi. Plant Physiol. 106:849-862.
    • (1994) Plant Physiol. , vol.106 , pp. 849-862
    • Lietzke, S.E.1    Yoder, M.D.2    Keen, N.T.3    Jurnak, F.4
  • 25
    • 0030045010 scopus 로고    scopus 로고
    • Iron is a triggering factor for differential expression of Erwinia chrysanthemi strain 3937 pectate lyases in pathogenesis of African violets
    • Masclaux, C., N. Hugouvieux-Cotte-Pattat, and D. Expert. 1996. Iron is a triggering factor for differential expression of Erwinia chrysanthemi strain 3937 pectate lyases in pathogenesis of African violets. Mol. Plant-Microbe Interact. 9:198-205.
    • (1996) Mol. Plant-Microbe Interact. , vol.9 , pp. 198-205
    • Masclaux, C.1    Hugouvieux-Cotte-Pattat, N.2    Expert, D.3
  • 26
    • 0141881090 scopus 로고
    • Activation of pectate-lyase from Erwinia carotovora subsp. atroseptica by potato tuber tissue extract
    • McMillan, G. P., D. Hedley, and M. C. M. Perombelon. 1993. Activation of pectate-lyase from Erwinia carotovora subsp. atroseptica by potato tuber tissue extract. Physiol. Mol. Plant Pathol. 42:1-18.
    • (1993) Physiol. Mol. Plant Pathol. , vol.42 , pp. 1-18
    • McMillan, G.P.1    Hedley, D.2    Perombelon, M.C.M.3
  • 27
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Miller, J. H. 1972. Experiment in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1972) Experiment in Molecular Genetics
    • Miller, J.H.1
  • 28
    • 0014252221 scopus 로고
    • Extracellular and intracellular polygalacturonic acid trans eliminase of Erwinia carotovora
    • Moran, F., S. Nasuno, and M. P. Starr. 1968. Extracellular and intracellular polygalacturonic acid trans eliminase of Erwinia carotovora. Arch. Biochem. Biophys. 123:298-306.
    • (1968) Arch. Biochem. Biophys. , vol.123 , pp. 298-306
    • Moran, F.1    Nasuno, S.2    Starr, M.P.3
  • 29
    • 0030466275 scopus 로고    scopus 로고
    • Regulation of pelZ, a gene of the pelB-pelC cluster encoding a new pectate lyase of Erwinia chrysanthemi 3937
    • 27a.Pissavin, C., J. Robert-Baudouy, and N. Hugouvieux-Cotte-Pattat. 1996. Regulation of pelZ, a gene of the pelB-pelC cluster encoding a new pectate lyase of Erwinia chrysanthemi 3937. J. Bacteriol. 178:7187-7196.
    • (1996) J. Bacteriol. , vol.178 , pp. 7187-7196
    • Pissavin, C.1    Robert-Baudouy, J.2    Hugouvieux-Cotte-Pattat, N.3
  • 30
    • 0026599991 scopus 로고
    • Differential depolymerization mechanisms of pectate lyase secreted by Erwinia chrysanthemi EC16
    • Preston, J., J. Rice, L. Ingram, and N. T. Keen. 1992. Differential depolymerization mechanisms of pectate lyase secreted by Erwinia chrysanthemi EC16. J. Bacteriol. 174:2039-2042.
    • (1992) J. Bacteriol. , vol.174 , pp. 2039-2042
    • Preston, J.1    Rice, J.2    Ingram, L.3    Keen, N.T.4
  • 31
    • 0000723913 scopus 로고
    • Purification and characterization of an endopolygalacturonase produced by Colletotrichum gloeosporioides
    • Prusky, D., S. Gold, and N. T. Keen. 1989. Purification and characterization of an endopolygalacturonase produced by Colletotrichum gloeosporioides. Physiol. Mol. Plant Pathol. 35:121-133.
    • (1989) Physiol. Mol. Plant Pathol. , vol.35 , pp. 121-133
    • Prusky, D.1    Gold, S.2    Keen, N.T.3
  • 32
    • 0021795611 scopus 로고
    • Cloning of genes encoding pectolytic enzyme from a genomic library of the phytopathogenic bacteria Erwinia chrysanthemi
    • Reverchon, S., N. Hugouvieux-Cotte-Pattat, and J. Robert-Baudouy. 1985. Cloning of genes encoding pectolytic enzyme from a genomic library of the phytopathogenic bacteria Erwinia chrysanthemi. Gene 35:121-130.
    • (1985) Gene , vol.35 , pp. 121-130
    • Reverchon, S.1    Hugouvieux-Cotte-Pattat, N.2    Robert-Baudouy, J.3
  • 34
    • 0022539268 scopus 로고
    • Comparison of pectic enzymes produced by Erwinia chrysanthemi, Erwinia carotovora subsp. carotovora, and Erwinia carotovora subsp. atroseptica
    • Ried, J. L., and A. Collmer. 1986. Comparison of pectic enzymes produced by Erwinia chrysanthemi, Erwinia carotovora subsp. carotovora, and Erwinia carotovora subsp. atroseptica. Appl. Environ. Microbiol. 52:305-310.
    • (1986) Appl. Environ. Microbiol. , vol.52 , pp. 305-310
    • Ried, J.L.1    Collmer, A.2
  • 35
    • 0028154704 scopus 로고
    • Secretion of extracellular virulence factors by plant pathogenic bacteria
    • Salmond, G. P. C. 1994. Secretion of extracellular virulence factors by plant pathogenic bacteria. Annu. Rev. Phytopathol. 32:181-200.
    • (1994) Annu. Rev. Phytopathol. , vol.32 , pp. 181-200
    • Salmond, G.P.C.1
  • 37
    • 0023761294 scopus 로고
    • Isoenzymes of extracellular pectate lyases of bacteria of the genus Erwinia
    • Shevchik, V. E., A. N. Evtushenkov, and Y. K. Fomichev. 1988. Isoenzymes of extracellular pectate lyases of bacteria of the genus Erwinia. Biokhimiya 53:1628-1638.
    • (1988) Biokhimiya , vol.53 , pp. 1628-1638
    • Shevchik, V.E.1    Evtushenkov, A.N.2    Fomichev, Y.K.3
  • 38
    • 85036449078 scopus 로고    scopus 로고
    • Unpublished data
    • 35a.Shevchik, V. E., et al. Unpublished data.
    • Shevchik, V.E.1
  • 39
    • 0001035316 scopus 로고
    • Pectic enzyme complex from Erwinia carotovora: A model for degradation and assimilation of host pectic fractions
    • Stack, J. P., M. S. Mount, P. M. Berman, and J. P. Hubbard. 1980. Pectic enzyme complex from Erwinia carotovora: a model for degradation and assimilation of host pectic fractions. Phytopathology 70:267-272.
    • (1980) Phytopathology , vol.70 , pp. 267-272
    • Stack, J.P.1    Mount, M.S.2    Berman, P.M.3    Hubbard, J.P.4
  • 40
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, W. F., and B. A. Moffat. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, W.F.1    Moffat, B.A.2
  • 41
    • 0021749061 scopus 로고
    • Purification and properties of two pectate lyases produced by Erwinia carotovora
    • Sugiura, J., M. Yasuda, S. Kamimiya, K. Izaki, and H. Takahashi. 1984. Purification and properties of two pectate lyases produced by Erwinia carotovora. J. Gen. Microbiol. 30:167-175.
    • (1984) J. Gen. Microbiol. , vol.30 , pp. 167-175
    • Sugiura, J.1    Yasuda, M.2    Kamimiya, S.3    Izaki, K.4    Takahashi, H.5
  • 42
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor, S., and C. Richardson. 1985. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA 82:1074-1078.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.2
  • 43
    • 0024060080 scopus 로고
    • Structure and organisation of the pel genes from Erwinia chrysanthemi EC16
    • Tamaki, S. J., S. Gold, M. Robeson, S. Manulis, and N. T. Keen. 1988. Structure and organisation of the pel genes from Erwinia chrysanthemi EC16. J. Bacteriol. 170:3468-3478.
    • (1988) J. Bacteriol. , vol.170 , pp. 3468-3478
    • Tamaki, S.J.1    Gold, S.2    Robeson, M.3    Manulis, S.4    Keen, N.T.5
  • 44
    • 0025864519 scopus 로고
    • Pectate lyase fixation and pectate disorganization visualized by immunochemistry in Saintpaulia ionan- Tha infected by Erwinia chrysanthemi
    • Temsah, M., Y. Bertheau, and B. Vian. 1991. Pectate lyase fixation and pectate disorganization visualized by immunochemistry in Saintpaulia ionan- tha infected by Erwinia chrysanthemi. Cell Biol. Int. Rep. 15:611-620.
    • (1991) Cell Biol. Int. Rep. , vol.15 , pp. 611-620
    • Temsah, M.1    Bertheau, Y.2    Vian, B.3
  • 45
    • 0343219416 scopus 로고
    • Production and potential uses of monoclonal antibodies to pectate lyases of Erwinia chrysanthemi
    • Vergnet-Ballas, C., Y. Bertheau, and J. Grosclaude. 1986. Production and potential uses of monoclonal antibodies to pectate lyases of Erwinia chrysanthemi. Symbiosis 2:367-372.
    • (1986) Symbiosis , vol.2 , pp. 367-372
    • Vergnet-Ballas, C.1    Bertheau, Y.2    Grosclaude, J.3
  • 46
    • 0028385026 scopus 로고
    • Purification of pectate lyase produced by Colletotrichum gloeosporioides and its inhibition by epicatechin: A possible factor involved in the resistance of unripe avocado fruits to anthraenose
    • Wattad, C., A. Dinoor, and D. Prusky. 1994. Purification of pectate lyase produced by Colletotrichum gloeosporioides and its inhibition by epicatechin: a possible factor involved in the resistance of unripe avocado fruits to anthraenose. Mol. Plant-Microbe Interact. 7:293-297.
    • (1994) Mol. Plant-Microbe Interact. , vol.7 , pp. 293-297
    • Wattad, C.1    Dinoor, A.2    Prusky, D.3
  • 47
    • 84886622040 scopus 로고
    • An efficient and reproducible procedure for the formation of spheroplasts from variously grown Escherichia coli
    • Witholt, B., M. Boekhout, M. Brock, J. Kingma, H. van Heerikhuizen, and L. deLeij. 1976. An efficient and reproducible procedure for the formation of spheroplasts from variously grown Escherichia coli. Anal. Biochem. 74:160-170.
    • (1976) Anal. Biochem. , vol.74 , pp. 160-170
    • Witholt, B.1    Boekhout, M.2    Brock, M.3    Kingma, J.4    Van Heerikhuizen, H.5    Deleij, L.6
  • 48
    • 0027329090 scopus 로고
    • New domain motif: The structure of pectate lyase C, a secreted plant virulence factor
    • Yoder, M. D., N. T. Keen, and F. Jurnak. 1993. New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science 260:1503-1507.
    • (1993) Science , vol.260 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3
  • 49
    • 0027918655 scopus 로고
    • Unusual structural features in the parallel β-helix in pectate lyases
    • Yoder, M. D., S. E. Lietzke, and F. Jurnak. 1993. Unusual structural features in the parallel β-helix in pectate lyases. Structure 1:241-251.
    • (1993) Structure , vol.1 , pp. 241-251
    • Yoder, M.D.1    Lietzke, S.E.2    Jurnak, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.