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Volumn 146, Issue 1, 2000, Pages 89-95

An unusual pectate lyase from a Bacillus sp. with high activity on pectin: Cloning and characterization

Author keywords

Lyase; Pectate; Pectin

Indexed keywords

BARIUM ION; CALCIUM ION; DNA FRAGMENT; PECTATE LYASE; PECTIN; POLYGALACTURONIC ACID;

EID: 0033972605     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-146-1-89     Document Type: Article
Times cited : (66)

References (40)
  • 1
  • 3
    • 0028156164 scopus 로고
    • Extracellular enzymes and pathogenesis of soft-rot Erwinia
    • Barras, F., van Gijsegem, F. & Chatterjee, A. K. (1994). Extracellular enzymes and pathogenesis of soft-rot Erwinia. Annu Rev Phytopathol 32, 201-234.
    • (1994) Annu Rev Phytopathol , vol.32 , pp. 201-234
    • Barras, F.1    Van Gijsegem, F.2    Chatterjee, A.K.3
  • 4
    • 0027739839 scopus 로고
    • Characterization of cellulase-free xylanases from the newly isolated Bacillus sp. Strain BP-23
    • Blanco, A. & Pastor, F. I. J. (1993). Characterization of cellulase-free xylanases from the newly isolated Bacillus sp. strain BP-23. Can J Microbiol 39, 1162-1166.
    • (1993) Can J Microbiol , vol.39 , pp. 1162-1166
    • Blanco, A.1    Pastor, F.I.J.2
  • 5
    • 0028790376 scopus 로고
    • Purification and properties of xylanase a from alkali-tolerant Bacillus sp. Strain BP-23
    • Blanco, A., Vidal, T., Colom, J. F. & Pastor, F. I. J. (1995). Purification and properties of xylanase A from alkali-tolerant Bacillus sp. strain BP-23. Appl Environ Microbiol 61, 4468-4470.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 4468-4470
    • Blanco, A.1    Vidal, T.2    Colom, J.F.3    Pastor, F.I.J.4
  • 6
    • 0031823404 scopus 로고    scopus 로고
    • Cloning of a new endoglucanase gene from Bacillus sp. BP-23 and characterisation of the enzyme. Performance in paper manufacture from cereal straw
    • Blanco, A., Díaz, P., Martínez, J., Vidal, T., Torres, A. L. & Pastor, F. I. J. (1998). Cloning of a new endoglucanase gene from Bacillus sp. BP-23 and characterisation of the enzyme. Performance in paper manufacture from cereal straw. Appl Microbiol Biotechnol 50, 48-54.
    • (1998) Appl Microbiol Biotechnol , vol.50 , pp. 48-54
    • Blanco, A.1    Díaz, P.2    Martínez, J.3    Vidal, T.4    Torres, A.L.5    Pastor, F.I.J.6
  • 7
    • 0041541782 scopus 로고    scopus 로고
    • A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes
    • Blanco, A., Díaz, P., Zueco, J., Parascandola, P. & Pastor, F. I. J. (1999). A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes. Microbiology 145, 2163-2170.
    • (1999) Microbiology , vol.145 , pp. 2163-2170
    • Blanco, A.1    Díaz, P.2    Zueco, J.3    Parascandola, P.4    Pastor, F.I.J.5
  • 8
    • 0343487562 scopus 로고    scopus 로고
    • Cloning, sequence and expression of the pel gene from an Amycolata sp
    • Brühlmann, F. & Keen, N. T. (1997). Cloning, sequence and expression of the pel gene from an Amycolata sp. Gene 202, 45-51.
    • (1997) Gene , vol.202 , pp. 45-51
    • Brühlmann, F.1    Keen, N.T.2
  • 9
    • 0002806035 scopus 로고
    • The polygalacturonases and lyases
    • Edited by R. H. Walter. San Diego: Academic Press
    • Burns, J. K. (1991). The polygalacturonases and lyases. In The Chemistry and Technology of Pectin, pp. 165-188. Edited by R. H. Walter. San Diego: Academic Press.
    • (1991) The Chemistry and Technology of Pectin , pp. 165-188
    • Burns, J.K.1
  • 10
    • 0031714923 scopus 로고    scopus 로고
    • The Pseudomonas syringae pv. Tomato HrpW protein has domains similar to harpins and pectate lyases and can elicit the plant hypersensitive response and hind to pectate
    • Charkowski, A. O., Alfano, J. R., Preston, G., Yuan, J., He, S. Y. & Collmer, A. (1998). The Pseudomonas syringae pv. tomato HrpW protein has domains similar to harpins and pectate lyases and can elicit the plant hypersensitive response and hind to pectate. J Bacteriol 180, 5211-5217.
    • (1998) J Bacteriol , vol.180 , pp. 5211-5217
    • Charkowski, A.O.1    Alfano, J.R.2    Preston, G.3    Yuan, J.4    He, S.Y.5    Collmer, A.6
  • 11
  • 12
    • 0015222721 scopus 로고
    • Fate of transforming DNA following uptake by competent Bacillus subtilis. I. Formation and properties of the donor-recipient complex
    • Dubnau, D. & Davidoff-Abelson, R. (1971). Fate of transforming DNA following uptake by competent Bacillus subtilis. I. Formation and properties of the donor-recipient complex. J Mol Biol 56, 209-221.
    • (1971) J Mol Biol , vol.56 , pp. 209-221
    • Dubnau, D.1    Davidoff-Abelson, R.2
  • 13
    • 0023811628 scopus 로고
    • Chromosomal mutations that increase the production of a plasmid-encoded haemolysin in Escherichia coli
    • Godessart, N., Muñoa, F. J., Regue, M. & Juárez, A. (1988). Chromosomal mutations that increase the production of a plasmid-encoded haemolysin in Escherichia coli. J Gen Microbiol 134, 2779-2787.
    • (1988) J Gen Microbiol , vol.134 , pp. 2779-2787
    • Godessart, N.1    Muñoa, F.J.2    Regue, M.3    Juárez, A.4
  • 14
    • 0026702554 scopus 로고
    • Isolation and analysis of a novel inducible pectate lyase gene from the phytopathogenic fungus fusarium solani f. sp. pisi (Nectria haematococca, mating population VI)
    • González-Candelas, L. & Kolattukudy, P. E. (1992). Isolation and analysis of a novel inducible pectate lyase gene from the phytopathogenic fungus Fusarium solani f. sp. pisi (Nectria haematococca, mating population VI). J Bacteriol 174, 6343-6349.
    • (1992) J Bacteriol , vol.174 , pp. 6343-6349
    • González-Candelas, L.1    Kolattukudy, P.E.2
  • 15
    • 0028832570 scopus 로고
    • Cloning of a new pectate lyase gene pelC from Fusarium solani f. sp. pisi (Nectria haematococca, mating type VI) and characterization of the gene product expressed in Pichia pastoris
    • Guo, W., González-Candelas, L. & Kolattukudy, P. E. (1995a). Cloning of a new pectate lyase gene pelC from Fusarium solani f. sp. pisi (Nectria haematococca, mating type VI) and characterization of the gene product expressed in Pichia pastoris. Arch Biochem Biophys 323, 352-360.
    • (1995) Arch Biochem Biophys , vol.323 , pp. 352-360
    • Guo, W.1    González-Candelas, L.2    Kolattukudy, P.E.3
  • 16
    • 0028894866 scopus 로고
    • Cloning of a novel constitutively expressed pectate lyase gene pelB from Fusarium solani f. sp. pisi (Nectria haematococca, mating type VI) and characterization of the gene product expressed in Pichia pastoris
    • Guo, W., González-Candelas, L. & Kolattukudy, P. E. (1995b). Cloning of a novel constitutively expressed pectate lyase gene pelB from Fusarium solani f. sp. pisi (Nectria haematococca, mating type VI) and characterization of the gene product expressed in Pichia pastoris. J Bacteriol 177, 7070-7077.
    • (1995) J Bacteriol , vol.177 , pp. 7070-7077
    • Guo, W.1    González-Candelas, L.2    Kolattukudy, P.E.3
  • 17
    • 0030586717 scopus 로고    scopus 로고
    • Identification of a novel pelD gene expressed uniquely in planta by Fusarium solani f. sp. pisi (Nectria haematococca, mating type VI) and characterization of its protein product as an endo-pectate lyase
    • Guo, W., González-Candelas, L. & Kolattukudy, P. E. (1996). Identification of a novel pelD gene expressed uniquely in planta by Fusarium solani f. sp. pisi (Nectria haematococca, mating type VI) and characterization of its protein product as an endo-pectate lyase. Arch Biochem Biophys 332, 305-312.
    • (1996) Arch Biochem Biophys , vol.332 , pp. 305-312
    • Guo, W.1    González-Candelas, L.2    Kolattukudy, P.E.3
  • 18
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. (1983). Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166, 557-580.
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 19
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. (1986). A new method for predicting signal sequence cleavage sites. Nucleic Acids Res 14, 4683-4690.
    • (1986) Nucleic Acids Res , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 21
    • 0032995005 scopus 로고    scopus 로고
    • Production of highly efficient enzymes for flax retting by Rhizomucor pusillus
    • Henriksson, G., Akin, D. E., Slomczynski, D. & Eriksson, K.-E. L. (1999). Production of highly efficient enzymes for flax retting by Rhizomucor pusillus. J Biotechnol 68, 115-123.
    • (1999) J Biotechnol , vol.68 , pp. 115-123
    • Henriksson, G.1    Akin, D.E.2    Slomczynski, D.3    Eriksson, K.-E.L.4
  • 22
    • 0029257437 scopus 로고
    • Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase super-family
    • Henrissat, B., Heffron, S. E., Yoder, M. D., Lietzke, S. E. & Jurnak, F. (1995). Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase super-family. 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
  • 23
    • 0024853451 scopus 로고
    • Extracellular and periplasmic isoenzymes of pectate lyase from Erwinia carotovora subspecies carotovora belong to different gene families
    • Hinton, J. C. D., Sidebotham, J. M., Gill, D. R. & Salmond, G. P. C. (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
  • 25
    • 0021127426 scopus 로고
    • Molecular cloning of pectate lyase genes from Erwinia chrysanthemi and their expression in Escherichia coli
    • Keen, N. T., Dahlbeck, D., Staskawicz, B. & Belser, W. (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
  • 26
    • 0031684457 scopus 로고    scopus 로고
    • HrpW of Erwinia amylovora, a new harpin that contains a domain homologous to pectate lyases of a distinct class
    • Kim, J. F. & Beer, S. V. (1998). HrpW of Erwinia amylovora, a new harpin that contains a domain homologous to pectate lyases of a distinct class. J Bacteriol 180, 5203-5210.
    • (1998) J Bacteriol , vol.180 , pp. 5203-5210
    • Kim, J.F.1    Beer, S.V.2
  • 27
    • 0032608734 scopus 로고    scopus 로고
    • Purification and properties of a low-molecular-weight, high-alkaline pectate lyase from an alkaliphilic strain of Bacillus
    • Kobayashi, T., Koike, K., Yoshimatsu, T., Higaki, N., Suzumatsu, A., Ozawa, T., Hatada, Y. & Ito, S. (1999). Purification and properties of a low-molecular-weight, high-alkaline pectate lyase from an alkaliphilic strain of Bacillus. Biosci Biotechnol Biochem 63, 65-72.
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 65-72
    • Kobayashi, T.1    Koike, K.2    Yoshimatsu, T.3    Higaki, N.4    Suzumatsu, A.5    Ozawa, T.6    Hatada, Y.7    Ito, S.8
  • 28
    • 0031267241 scopus 로고    scopus 로고
    • Purification and characterization of thermostable pectate-lyases from a newly isolated thermophilic bacterium, Thermoanaerobacter italicus sp. nov
    • Kozianowski, G., Canganella, F., Rainey, F. A., Hippe, H. & Antranikian, G. (1997). Purification and characterization of thermostable pectate-lyases from a newly isolated thermophilic bacterium, Thermoanaerobacter italicus sp. nov. Extremophiles 1, 171-182.
    • (1997) Extremophiles , vol.1 , pp. 171-182
    • Kozianowski, G.1    Canganella, F.2    Rainey, F.A.3    Hippe, H.4    Antranikian, G.5
  • 29
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the gram-positive bacterium Bacillus subtilis
    • Kunst, F., Ogasawara, N., Moszer, I. & 148 other authors (1997). The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature 390, 249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 221, 680-685.
    • (1970) Nature , vol.221 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0028277691 scopus 로고
    • Nucleotide sequence and expression of a novel pectate lyase gene (pel-3) and a closely linked endopolygalacturonase gene (peh-1) of Erwinia carotovora subsp. carotovora 71
    • Liu, Y., Chatterjee, A. & Chatterjee, A. K. (1994). Nucleotide sequence and expression of a novel pectate lyase gene (pel-3) and a closely linked endopolygalacturonase gene (peh-1) of Erwinia carotovora subsp. carotovora 71. Appl Environ Microbiol 60, 2545-2552.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 2545-2552
    • Liu, Y.1    Chatterjee, A.2    Chatterjee, A.K.3
  • 33
    • 0025005810 scopus 로고
    • Purification and characterization of extracellular pectate lyase from Bacillus subtilis
    • Nasser, W., Chalet, F. & Robert-Baudouy, J. (1990). Purification and characterization of extracellular pectate lyase from Bacillus subtilis. Biochimie 72, 689-695.
    • (1990) Biochimie , vol.72 , pp. 689-695
    • Nasser, W.1    Chalet, F.2    Robert-Baudouy, J.3
  • 34
    • 0027360579 scopus 로고
    • Pectate lyase from Bacillus subtilis: Molecular characterization of the gene, and properties of the cloned enzyme
    • Nasser, W., Awadé, A. C., Reverchon, S. & Robert-Baudouy, J. (1993). Pectate lyase from Bacillus subtilis: molecular characterization of the gene, and properties of the cloned enzyme. FEBS Lett 335, 319-326.
    • (1993) FEBS Lett , vol.335 , pp. 319-326
    • Nasser, W.1    Awadé, A.C.2    Reverchon, S.3    Robert-Baudouy, J.4
  • 35
    • 85008120727 scopus 로고
    • Purification, characterization, and production of two pectic transeliminases with proropectinase activity from Bacillus subtilis
    • Sakamoto, T., Hours, R. A. & Sakai, T. (1994). Purification, characterization, and production of two pectic transeliminases with proropectinase activity from Bacillus subtilis. Biosci Biotechnol Biochem 58, 353-358.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 353-358
    • Sakamoto, T.1    Hours, R.A.2    Sakai, T.3
  • 36
    • 0030566873 scopus 로고    scopus 로고
    • Molecular cloning and nucleotide sequence of the gene encoding phosphate-inducible pectin lyase of Bacillus subtilis
    • Sakamoto, T., Kawasaki, H. & Sakai, T. (1996). Molecular cloning and nucleotide sequence of the gene encoding phosphate-inducible pectin lyase of Bacillus subtilis. FEBS Lett 398, 269-273.
    • (1996) FEBS Lett , vol.398 , pp. 269-273
    • Sakamoto, T.1    Kawasaki, H.2    Sakai, T.3
  • 38
    • 0030670938 scopus 로고    scopus 로고
    • Pectate lyase Peli of Erwinia chrysanthemi 3937 belongs to a new family
    • Shevchik, V. E., Robert-Baudouy, J. & Hugouvieux-Cotte-Pattat, N. (1997). Pectate lyase PelI of Erwinia chrysanthemi 3937 belongs to a new family. J Bacteriol 179, 7321-7330.
    • (1997) J Bacteriol , vol.179 , pp. 7321-7330
    • Shevchik, V.E.1    Robert-Baudouy, J.2    Hugouvieux-Cotte-Pattat, N.3
  • 39
    • 0031692695 scopus 로고    scopus 로고
    • Processing of the pectate lyase Peli by extracellular proteases of Erwinia chrysanthemi 3937
    • Shevchik, V. E., Boccara, M., Vedel, R. & Hugouvieux-Cotte-Pattat, N. (1998). Processing of the pectate lyase PelI by extracellular proteases of Erwinia chrysanthemi 3937. Mol Microbiol 29, 1459-1469.
    • (1998) Mol Microbiol , vol.29 , pp. 1459-1469
    • Shevchik, V.E.1    Boccara, M.2    Vedel, R.3    Hugouvieux-Cotte-Pattat, N.4
  • 40
    • 0030944441 scopus 로고    scopus 로고
    • Comparative analysis of the five major Erwinia chrysanthemi pectate lyases: Enzyme characteristics and potential inhibitors
    • Tardy, F., Nasser, W., Robert-Baudouy, J. & Hugouvieux-Cotte-Pattat, N. (1997). Comparative analysis of the five major Erwinia chrysanthemi pectate lyases: enzyme characteristics and potential inhibitors. J Bacteriol 179, 2503-2511.
    • (1997) J Bacteriol , vol.179 , pp. 2503-2511
    • Tardy, F.1    Nasser, W.2    Robert-Baudouy, J.3    Hugouvieux-Cotte-Pattat, N.4


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