메뉴 건너뛰기




Volumn 65, Issue 2, 2001, Pages 322-329

Molecular cloning, DNA sequence, and expression of the gene encoding for thermostable pectate lyase of thermophilic Bacillus sp. TS 47

Author keywords

Bacillus; Gene cloning; Pectate lyase; Thermophile; Thermostable enzyme

Indexed keywords

BACTERIAL DNA; PECTATE LYASE; POLYSACCHARIDE LYASE; PRIMER DNA;

EID: 0035257585     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.65.322     Document Type: Article
Times cited : (30)

References (34)
  • 2
    • 0027818642 scopus 로고
    • Pectin, pectinase, and protopectinase: Production, properties, and applications
    • Sakai, T., Sakamoto, T., Hallaert, J., and Vandamme, E. J., Pectin, pectinase, and protopectinase: Production, properties, and applications. Adv. Appl. Microbiol., 39, 213-294 (1993).
    • (1993) Adv. Appl. Microbiol. , vol.39 , pp. 213-294
    • Sakai, T.1    Sakamoto, T.2    Hallaert, J.3    Vandamme, E.J.4
  • 3
    • 85008120727 scopus 로고
    • Purification, characterization, and production of two pectic transeliminases with protopectinase activity from Bacillus subtilis
    • Sakamoto, T., Hours, R. A., and Sakai, T., Purification, characterization, and production of two pectic transeliminases with protopectinase activity from Bacillus subtilis. Biosci. Biotechnol. Biochem., 58, 353-358 (1994).
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 353-358
    • Sakamoto, T.1    Hours, R.A.2    Sakai, T.3
  • 4
    • 0015441966 scopus 로고
    • The genus Erwinia: Enterobacteria pathogenic to plants and animals
    • Starr, M. P. and Chatterjee, A. K., The genus Erwinia: enterobacteria pathogenic to plants and animals. Annu. Rev. Microbiol., 26, 389-426 (1972).
    • (1972) Annu. Rev. Microbiol. , vol.26 , pp. 389-426
    • Starr, M.P.1    Chatterjee, A.K.2
  • 5
    • 0014841677 scopus 로고
    • Pectic acid lyases of Bacillus polymyxa
    • Nagel, C. W. and Wilson, T. M., Pectic acid lyases of Bacillus polymyxa. Appl. Microbiol., 20, 374-383 (1970).
    • (1970) Appl. Microbiol. , vol.20 , pp. 374-383
    • Nagel, C.W.1    Wilson, T.M.2
  • 6
    • 0015135189 scopus 로고
    • Purification and properties of a polygalacturonic acid trans-eliminase produced by Bacillus pumilus
    • Davé, B. A. and Vaughn, R. H., Purification and properties of a polygalacturonic acid trans-eliminase produced by Bacillus pumilus. J. Bacteriol., 108, 166-174 (1971).
    • (1971) J. Bacteriol. , vol.108 , pp. 166-174
    • Davé, B.A.1    Vaughn, R.H.2
  • 7
    • 0025005810 scopus 로고
    • Purification and characterization of extracellular pectate lyase from Bacillus subtilis
    • Nasser, W., Chalet, F., and Robert-Baudouy, J., Purification and characterization of extracellular pectate lyase from Bacillus subtilis. Biochimie, 72, 689-695 (1990).
    • (1990) Biochimie , vol.72 , pp. 689-695
    • Nasser, W.1    Chalet, F.2    Robert-Baudouy, J.3
  • 9
    • 33947481151 scopus 로고
    • Purification and properties of polygalacturonic acid transeliminase produced by Clostridium multifermentas
    • Macmillan, J. D. and Vaughan, R. H., Purification and properties of polygalacturonic acid transeliminase produced by Clostridium multifermentas. Biochemistry, 3, 564-572 (1964).
    • (1964) Biochemistry , vol.3 , pp. 564-572
    • Macmillan, J.D.1    Vaughan, R.H.2
  • 10
    • 0014108541 scopus 로고
    • Polygalacturonic acid trans-eliminase of Xanthomonas campestris
    • Nasuno, S. and Starr, M. P., Polygalacturonic acid trans-eliminase of Xanthomonas campestris. Biochem. J., 104, 178-185 (1967).
    • (1967) Biochem. J. , vol.104 , pp. 178-185
    • Nasuno, S.1    Starr, M.P.2
  • 11
    • 0013832551 scopus 로고
    • The trans-eliminative breakdown of Na-polygalacturonate by Pseudomonas fluorecens
    • Fuchs, A., The trans-eliminative breakdown of Na-polygalacturonate by Pseudomonas fluorecens. Antonie van Leeuwenhoek, 31, 323-340 (1965).
    • (1965) Antonie van Leeuwenhoek , vol.31 , pp. 323-340
    • Fuchs, A.1
  • 12
    • 0018885098 scopus 로고
    • Purification and properties of polygalacturonic acid trans-eliminase from Bacillus stearothermophilus
    • Karbassi, A. and Vaughn, R. H., Purification and properties of polygalacturonic acid trans-eliminase from Bacillus stearothermophilus. Can. J. Microbiol., 26, 377-384 (1980).
    • (1980) Can. J. Microbiol. , vol.26 , pp. 377-384
    • Karbassi, A.1    Vaughn, R.H.2
  • 13
    • 0034328744 scopus 로고    scopus 로고
    • Purification and characterization of thermostable pectate lyase with protopectinase activity from thermophilic Bacillus sp. TS 47
    • Takao, M., Nakaniwa, T., Yoshikawa, K., Terashita, T., and Sakai, T., Purification and characterization of thermostable pectate lyase with protopectinase activity from thermophilic Bacillus sp. TS 47. Biosci. Biotechnol. Biochem., 64, 2360-2367 (2000).
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 2360-2367
    • Takao, M.1    Nakaniwa, T.2    Yoshikawa, K.3    Terashita, T.4    Sakai, T.5
  • 14
    • 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., and Robert-Baudouy, J., Pectate lyase from Bacillus subtilis: molecular characterization of the gene, and properties of the cloned enzyme. FEBS Lett., 335, 319-326 (1993).
    • (1993) FEBS Lett. , vol.335 , pp. 319-326
    • Nasser, W.1    Awadé, A.C.2    Reverchon, S.3    Robert-Baudouy, J.4
  • 16
    • 0027329090 scopus 로고
    • New domain motif: The structure of pectate lyase C, a secreted plant virulence factor
    • Yoder, M. D., Keen, N. T., and Jurnak, F., New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science, 260, 1503-1507 (1993).
    • (1993) Science , vol.260 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3
  • 17
    • 0000033553 scopus 로고
    • Replication and expression of plasmids from Staphylococcus aureus in Bacillus subtilis
    • Ehrlich, S. D., Replication and expression of plasmids from Staphylococcus aureus in Bacillus subtilis. Proc. Natl. Acad. Sci. USA, 74, 1680-1682 (1977).
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 1680-1682
    • Ehrlich, S.D.1
  • 18
    • 0017847690 scopus 로고
    • Characterization of Staphylococcus aureus plasmids introduced by transformation into Bacillus subtilis
    • Gryczan, T. J., Contente, S., and Dubnau, D., Characterization of Staphylococcus aureus plasmids introduced by transformation into Bacillus subtilis. J. Bacteriol., 134, 318-329 (1978).
    • (1978) J. Bacteriol. , vol.134 , pp. 318-329
    • Gryczan, T.J.1    Contente, S.2    Dubnau, D.3
  • 19
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • Saito, H. and Miura, K., Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochim. Biophys. Acta, 72, 619-629 (1963).
    • (1963) Biochim. Biophys. Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.2
  • 20
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D., Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol., 166, 557-580 (1983).
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 21
    • 0018287541 scopus 로고
    • High frequency transformation of Bacillus subtilis
    • Chang, S. and Cohen, S. N., High frequency transformation of Bacillus subtilis. Mol. Gen. Genet., 168, 111-115 (1979).
    • (1979) Mol. Gen. Genet. , vol.168 , pp. 111-115
    • Chang, S.1    Cohen, S.N.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0013683706 scopus 로고
    • Secrition of proteins by bacilli
    • eds. Dubnau, D. A., Academic Press, Orlando
    • Mézes, P. S. F. and Lampen, J. O., Secrition of proteins by bacilli. In "The Molecular Biology of the Bacilli", vol. 2, eds. Dubnau, D. A., Academic Press, Orlando, pp. 151-183 (1985).
    • (1985) The Molecular Biology of the Bacilli , vol.2 , pp. 151-183
    • Mézes, P.S.F.1    Lampen, J.O.2
  • 27
    • 0023880326 scopus 로고
    • Characterization of the Erwinia carotovora pelA gene and its product pectate lyase A
    • Lei, S. P., Lin, H. C., Wang, S. S., and Wilcox, G., Characterization of the Erwinia carotovora pelA gene and its product pectate lyase A. Gene, 62, 159-164 (1988).
    • (1988) Gene , vol.62 , pp. 159-164
    • Lei, S.P.1    Lin, H.C.2    Wang, S.S.3    Wilcox, G.4
  • 28
    • 0024060080 scopus 로고
    • Structure and organization of the pel genes from Erwinia chrysanthemi EC16
    • Tamaki, S. J., Gold, S., Robeson, M., Manulis, S., and Keen, N. T., Structure and organization of the pel genes from Erwinia chrysanthemi EC16. J. Bacteriol., 170, 3468-3478 (1988).
    • (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
  • 29
    • 0023036933 scopus 로고
    • Structure of two pectate lyase genes from Erwinia chrysanthemi EC16 and their high-level expression in Escherichia coli
    • Keen, N. T. and Tamaki, S., Structure of two pectate lyase genes from Erwinia chrysanthemi EC16 and their high-level expression in Escherichia coli. J. Bacteriol., 168, 595-606 (1986).
    • (1986) J. Bacteriol. , vol.168 , pp. 595-606
    • Keen, N.T.1    Tamaki, S.2
  • 30
    • 0030019268 scopus 로고    scopus 로고
    • Cloning of a pectate lyase gene from Xanthomonas campestris pv. malvacearum and comparison of its sequence relationship with pel genes of soft-rot Erwinia and Pseudomonas
    • Liao, C. H., Gaffney, T. D., Bradley, S. P., and Wang, L. C., Cloning of a pectate lyase gene from Xanthomonas campestris pv. malvacearum and comparison of its sequence relationship with pel genes of soft-rot Erwinia and Pseudomonas. Mol. Plant-Microbe Interact., 9, 14-20 (1996).
    • (1996) Mol. Plant-microbe Interact. , vol.9 , pp. 14-20
    • Liao, C.H.1    Gaffney, T.D.2    Bradley, S.P.3    Wang, L.C.4
  • 31
    • 0028898476 scopus 로고
    • Sequence analysis of the Aspergillus nidulans pectate lyase pelA gene and evidence for binding of promoter regions to CREA, a regulator of carbon catabolite repression
    • Ho, M. C., Whitehead, M. P., Cleveland, T. E., and Dean, R. A., Sequence analysis of the Aspergillus nidulans pectate lyase pelA gene and evidence for binding of promoter regions to CREA, a regulator of carbon catabolite repression. Curr. Genet., 27, 142-149 (1995).
    • (1995) Curr. Genet. , vol.27 , pp. 142-149
    • Ho, M.C.1    Whitehead, M.P.2    Cleveland, T.E.3    Dean, R.A.4
  • 32
    • 0029257437 scopus 로고
    • Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase superfamily
    • Henrissat, B., Heffron, S. E., Yoder, M. D., Lietzke, S. E., and Jurnak, F., Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase superfamily. Plant Physiol., 107, 963-976 (1995).
    • (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
  • 33
    • 0026513432 scopus 로고
    • Purification of the acidic pectate lyase and nucleotide sequence of the corresponding gene (pelA) of Erwinia chrysanthemi strain 3937
    • Favey, S., Bourson, C., Bertheau, Y., Kotoujansky, A., and Boccara, M., Purification of the acidic pectate lyase and nucleotide sequence of the corresponding gene (pelA) of Erwinia chrysanthemi strain 3937. J. Gen. Microbiol., 138, 499-508 (1992).
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 499-508
    • Favey, S.1    Bourson, C.2    Bertheau, Y.3    Kotoujansky, A.4    Boccara, M.5
  • 34
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R. F., A simple method for displaying the hydropathic character of a protein. J. Mol. Biol., 157, 105-132 (1982).
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.