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Volumn 99, Issue 4, 2005, Pages 945-953

Molecular characterization of a novel chitinase from Bacillus thuringiensis subsp. kurstaki

Author keywords

Bacillus thuringiensis; Chitibiosidase; Cloning; Expression; Sequencing

Indexed keywords

AMINO ACIDS; BACTERIOLOGY; ESCHERICHIA COLI; GENE ENCODING;

EID: 25844465801     PISSN: 13645072     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2672.2005.02639.x     Document Type: Article
Times cited : (75)

References (31)
  • 1
    • 0028820391 scopus 로고
    • How does Bacillus thuringiensis produce so much insecticidal crystal proteins?
    • Agaisse, H. and Lereclus, D. (1995) How does Bacillus thuringiensis produce so much insecticidal crystal proteins?. J Bacteriol 177, 6027-6032.
    • (1995) J Bacteriol , vol.177 , pp. 6027-6032
    • Agaisse, H.1    Lereclus, D.2
  • 3
    • 0042171469 scopus 로고    scopus 로고
    • A constitutively expressed 36 kDa exochitinase from Bacillus thuringiensis HD-1
    • Arora, N., Ahmad, T., Rojagopal, R. and Bhatnagar, R.K. (2003) A constitutively expressed 36 kDa exochitinase from Bacillus thuringiensis HD-1. Biochem Biophys Res Commun 307, 620-625.
    • (2003) Biochem Biophys Res Commun , vol.307 , pp. 620-625
    • Arora, N.1    Ahmad, T.2    Rojagopal, R.3    Bhatnagar, R.K.4
  • 6
    • 0344734005 scopus 로고
    • Characterization and prospective view of Bacillus thuringiensis israelensis
    • ed. de Barjac, H. & Sutherland, D.J. Rutgers: Rutgers University Press
    • de Barjac, H. (1990) Characterization and prospective view of Bacillus thuringiensis israelensis. In Bacterial Control of Mosquitoes and Blackflies ed. de Barjac, H. & Sutherland, D.J. pp. 10-15. Rutgers: Rutgers University Press.
    • (1990) Bacterial Control of Mosquitoes and Blackflies , pp. 10-15
    • De Barjac, H.1
  • 7
    • 0032052151 scopus 로고    scopus 로고
    • Substrate specificities of tobacco chitinases
    • Brunner, F., Stintzi, A., Fritig, B. and Legrand, M. (1998) Substrate specificities of tobacco chitinases. Plant J 14, 225-234.
    • (1998) Plant J , vol.14 , pp. 225-234
    • Brunner, F.1    Stintzi, A.2    Fritig, B.3    Legrand, M.4
  • 8
    • 0025345822 scopus 로고
    • Biochemical and genetic analysis of a maltopentose-producing amylase from an alkaliphilic Gram-positive bacterium
    • Candussio, A., Schmid, G. and Bock, A. (1990) Biochemical and genetic analysis of a maltopentose-producing amylase from an alkaliphilic Gram-positive bacterium. Eur J Biochem 191, 177-185.
    • (1990) Eur J Biochem , vol.191 , pp. 177-185
    • Candussio, A.1    Schmid, G.2    Bock, A.3
  • 9
    • 0003133857 scopus 로고
    • The ecology of chitin decomposition
    • Gooday, G.W. (1990) The ecology of chitin decomposition. Adv Microb Ecol 11, 378-430.
    • (1990) Adv Microb Ecol , vol.11 , pp. 378-430
    • Gooday, G.W.1
  • 10
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. and Bairoch, A. (1993) New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 293, 781-788.
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 11
    • 0024337104 scopus 로고
    • Insecticidal proteins of Bacillus thuringiensis
    • Höfte, H. and Whiteley, H.R. (1989) Insecticidal proteins of Bacillus thuringiensis. Microbiol Rev 53, 242-255.
    • (1989) Microbiol Rev , vol.53 , pp. 242-255
    • Höfte, H.1    Whiteley, H.R.2
  • 12
    • 0016719994 scopus 로고
    • Metalloprotease from Bacillus thuringiensis
    • Li, E. and Yousten, A.A. (1975) Metalloprotease from Bacillus thuringiensis. Appl Microbiol 30, 354-361.
    • (1975) Appl Microbiol , vol.30 , pp. 354-361
    • Li, E.1    Yousten, A.A.2
  • 13
    • 0036902507 scopus 로고    scopus 로고
    • Chitinolytic activities in Bacillus thuringiensis and their synergistic effects on larvicidal activity
    • Liu, M., Cai, Q.X. Liu, H.Z., Zhang, B.H., Yan, J.P. and Yuan, Z.M. (2002) Chitinolytic activities in Bacillus thuringiensis and their synergistic effects on larvicidal activity. J Appl Microbiol 93, 374-379.
    • (2002) J Appl Microbiol , vol.93 , pp. 374-379
    • Liu, M.1    Cai, Q.X.2    Liu, H.Z.3    Zhang, B.H.4    Yan, J.P.5    Yuan, Z.M.6
  • 14
    • 0025965558 scopus 로고
    • Unusual sequence organization in CenB. An inverting endoglucanase from Cellulomonas fimi
    • Meink, A., Braam, C., Gilkes, N.R., Kiburn, D.G., Miller, R.C. and Warren, E.A.J. (1991) Unusual sequence organization in CenB. An inverting endoglucanase from Cellulomonas fimi. J Bacteriol 173, 308-314.
    • (1991) J Bacteriol , vol.173 , pp. 308-314
    • Meink, A.1    Braam, C.2    Gilkes, N.R.3    Kiburn, D.G.4    Miller, R.C.5    Warren, E.A.J.6
  • 15
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugars
    • Miller, G.L. (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugars. Anal Chem 31, 426-428.
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 16
    • 0030726362 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the function of novel cadherin-like domains and a chitin-binding domain
    • Morimoto, K., Karita, S., Kimura, T., Sakka, K. and Ohmya, K. (1997) Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the function of novel cadherin-like domains and a chitin-binding domain. J Bacteriol 179, 7306-7314.
    • (1997) J Bacteriol , vol.179 , pp. 7306-7314
    • Morimoto, K.1    Karita, S.2    Kimura, T.3    Sakka, K.4    Ohmya, K.5
  • 17
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielson, 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
    • Nielson, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 19
    • 10144263280 scopus 로고    scopus 로고
    • Synergistic activity of a Bacillus thuringiensis δ-endotoxin and a bacterial endochitinase against Spodoptera littoralis larvae
    • Regev, A., Keller, M., Strizhov, N., Sheh, B., Prudovsky, E., Chet, I., Ginzberg, I., Koncz-Kalman, Z. et al. (1996) Synergistic activity of a Bacillus thuringiensis δ-endotoxin and a bacterial endochitinase against Spodoptera littoralis larvae. Appl Environ Microbiol 62, 3581-3586.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3581-3586
    • Regev, A.1    Keller, M.2    Strizhov, N.3    Sheh, B.4    Prudovsky, E.5    Chet, I.6    Ginzberg, I.7    Koncz-Kalman, Z.8
  • 20
    • 0023901367 scopus 로고
    • Cloning and expression of a Streptomyces plicatus chitinase (chitinase- 63) in Escherichia coli
    • Robbins, P.W., Albright, C. and Benfield, B. (1988) Cloning and expression of a Streptomyces plicatus chitinase (chitinase- 63) in Escherichia coli. J Biol Chem 263, 443-447.
    • (1988) J Biol Chem , vol.263 , pp. 443-447
    • Robbins, P.W.1    Albright, C.2    Benfield, B.3
  • 22
    • 0031666818 scopus 로고    scopus 로고
    • Involvement of chitinases of Bacillus thuringiensis during pathogenesis in insects
    • Sampson, M.N. and Gooday, G.W. (1998) Involvement of chitinases of Bacillus thuringiensis during pathogenesis in insects. Microbiology 144, 2189-2194.
    • (1998) Microbiology , vol.144 , pp. 2189-2194
    • Sampson, M.N.1    Gooday, G.W.2
  • 23
    • 0002577185 scopus 로고
    • Improvement of the insecticidal activity of Bacillus thuringiensis var. entomocidus on larvae of Spodoptera littoralis (Lepidoptera-Noctuidae) by addition of chitinolytic bacteria, a phagostimulant and a UV-protectant
    • Sneh, B., Schuster, S. and Gross, S. (1983) Improvement of the insecticidal activity of Bacillus thuringiensis var. entomocidus on larvae of Spodoptera littoralis (Lepidoptera-Noctuidae) by addition of chitinolytic bacteria, a phagostimulant and a UV-protectant. Z Angew Entomol 96, 77-83.
    • (1983) Z Angew Entomol , vol.96 , pp. 77-83
    • Sneh, B.1    Schuster, S.2    Gross, S.3
  • 24
    • 0027401020 scopus 로고
    • Protein secretion in Bacillus species
    • Simomen, M. and Palva, I. (1993) Protein secretion in Bacillus species. Microbiol Rev 57, 109-137.
    • (1993) Microbiol Rev , vol.57 , pp. 109-137
    • Simomen, M.1    Palva, I.2
  • 25
    • 0031412589 scopus 로고    scopus 로고
    • Cloning of a chitinase gene into Bacillus thuringiensis subsp. aizawai for enhanced insecticidal activity
    • Tantimavanich, S., Pantowatana, S., Bhumiratana, A. and Panbangred, W. (1997) Cloning of a chitinase gene into Bacillus thuringiensis subsp. aizawai for enhanced insecticidal activity. J Gen Appl Microbiol 43, 31-37.
    • (1997) J Gen Appl Microbiol , vol.43 , pp. 31-37
    • Tantimavanich, S.1    Pantowatana, S.2    Bhumiratana, A.3    Panbangred, W.4
  • 27
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22, 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 28
    • 0027401151 scopus 로고
    • Detection and quantification of N-Acetyl-B-D-glucosaminidase, chitobiosidase, and endochitinase in solution and on gels
    • Tronsmo, A. and Harman, G.E. (1993) Detection and quantification of N-Acetyl-B-D-glucosaminidase, chitobiosidase, and endochitinase in solution and on gels. Anal Biochem 208, 74-79.
    • (1993) Anal Biochem , vol.208 , pp. 74-79
    • Tronsmo, A.1    Harman, G.E.2
  • 29
    • 0027216435 scopus 로고
    • Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity
    • Watanabe, T., Kobori, K., Miyachita, K., Fujii, T., Sakai, M., Uchida, M. and Tanaka, H. (1993) Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. J Biol Chem 268, 18567-18572.
    • (1993) J Biol Chem , vol.268 , pp. 18567-18572
    • Watanabe, T.1    Kobori, K.2    Miyachita, K.3    Fujii, T.4    Sakai, M.5    Uchida, M.6    Tanaka, H.7
  • 30
    • 0034521608 scopus 로고    scopus 로고
    • Toxicity of chitinase-producing Bacillus thuringiensis sp. kurstaki HD-1 toward Plutella xylostella
    • Wiwat, C., Thaithanun, S., Pantuwatana, S. and Bhumiratana, A. (2000) Toxicity of chitinase-producing Bacillus thuringiensis sp. kurstaki HD-1 toward Plutella xylostella. J Invertebr Pathol 79, 270-277.
    • (2000) J Invertebr Pathol , vol.79 , pp. 270-277
    • Wiwat, C.1    Thaithanun, S.2    Pantuwatana, S.3    Bhumiratana, A.4
  • 31
    • 0033180054 scopus 로고    scopus 로고
    • Production and characterization of metalloproteases synthesized concomitantly with delta-endotoxin by Bacillus thuringiensis subsp. Kurstaki strain grown on gruel-based media
    • Zouari, N. and Jaoua, S. (1999) Production and characterization of metalloproteases synthesized concomitantly with delta-endotoxin by Bacillus thuringiensis subsp. Kurstaki strain grown on gruel-based media. Enzyme Microb Technol 25, 364-371.
    • (1999) Enzyme Microb Technol , vol.25 , pp. 364-371
    • Zouari, N.1    Jaoua, S.2


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