메뉴 건너뛰기




Volumn 84, Issue 6, 1997, Pages 493-501

Molecular cloning, nucleotide sequencing, and regulation of the chiA gene encoding one of Chitinases from Enterobacter sp. G-l

Author keywords

Chitinase; Enterobacter sp; G l; Inverted repeat sequence

Indexed keywords

AMINO ACIDS; BIODEGRADATION; CHITIN; COLIFORM BACTERIA; ENZYMES; GENES; OLIGOMERS;

EID: 0031355633     PISSN: 0922338X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0922-338X(97)81901-0     Document Type: Article
Times cited : (10)

References (30)
  • 1
    • 0000201402 scopus 로고
    • Activation of a bean chitinase promoter in transgenic tobacco plants by phytopathogenic fungi
    • Roby, D., Broglie, K., Cressman, R., Biddle, P., Chet, I., and Broglie, R.: Activation of a bean chitinase promoter in transgenic tobacco plants by phytopathogenic fungi. Plant Cell, 2, 999-1007 (1990).
    • (1990) Plant Cell , vol.2 , pp. 999-1007
    • Roby, D.1    Broglie, K.2    Cressman, R.3    Biddle, P.4    Chet, I.5    Broglie, R.6
  • 2
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbanm, A., Mauch, F., Vogeli, U., and Boiler, T.: Plant chitinases are potent inhibitors of fungal growth. Nature, 3:Z4, 365-367 (1986).
    • (1986) Nature , vol.3 , Issue.Z4 , pp. 365-367
    • Schlumbanm, A.1    Mauch, F.2    Vogeli, U.3    Boiler, T.4
  • 4
    • 0028001451 scopus 로고
    • Enhanced protection against fungal attack by constitutive co-expression of chitinase and glucanase genes in transgenic tobacco
    • Zhu, Q., Mäher, E. A., Masoud, S., Dixon, R. A., and Lamb, C. J.: Enhanced protection against fungal attack by constitutive co-expression of chitinase and glucanase genes in transgenic tobacco. Bio/Technol., 12, 807-812 (1994).
    • (1994) Bio/Technol. , vol.12 , pp. 807-812
    • Zhu, Q.1    Mäher, E.A.2    Masoud, S.3    Dixon, R.A.4    Lamb, C.J.5
  • 5
    • 0026002418 scopus 로고
    • Chitinase is required for cell separation during growth of Saccharomyces cerevisiae
    • Kuranda, M. J. and Robinns, P. W.: Chitinase is required for cell separation during growth of Saccharomyces cerevisiae. J. Biol. Chem., 266, 19758-19767 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 19758-19767
    • Kuranda, M.J.1    Robinns, P.W.2
  • 6
    • 0026709204 scopus 로고
    • What's new in chitinase research?
    • Flach, J., Pilet, P.E., and Jolies, P.: What's new in chitinase research? Experientia., 48, 701-716 (1992).
    • (1992) Experientia. , vol.48 , pp. 701-716
    • Flach, J.1    Pilet, P.E.2    Jolies, P.3
  • 7
    • 0001669533 scopus 로고
    • Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens
    • Jones, J. D. G., Grady, K. L., Snslow, T. V., and Bedbrook, J. R.: Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens. EMBO J., 5, 467-473 (1986).
    • (1986) EMBO J. , vol.5 , pp. 467-473
    • Jones, J.D.G.1    Grady, K.L.2    Snslow, T.V.3    Bedbrook, J.R.4
  • 8
    • 0028815373 scopus 로고
    • Chitinase B from Serratia marcescens BJL200 is exported to the periplasm without processing
    • Brurberg, M. B., Eijsink, V. G. H., Haandrikman, A. J., Venema, G., and Nes, I. F.: Chitinase B from Serratia marcescens BJL200 is exported to the periplasm without processing. Microbiol., 141, 123-131 (1995).
    • (1995) Microbiol. , vol.141 , pp. 123-131
    • Brurberg, M.B.1    Eijsink, V.G.H.2    Haandrikman, A.J.3    Venema, G.4    Nes, I.F.5
  • 9
    • 0024041235 scopus 로고
    • Cloning of the genes of the chitin utilization regulon of Serratia liquefaciens
    • Joshi, S., Koslowski, M., Selvaraj, G., lyer, V.N., and Davies, R. W.: Cloning of the genes of the chitin utilization regulon of Serratia liquefaciens. J. Bacteriol., 170, 2984-2988 (1988).
    • (1988) J. Bacteriol. , vol.170 , pp. 2984-2988
    • Joshi, S.1    Koslowski, M.2    Selvaraj, G.3    Lyer, V.N.4    Davies, R.W.5
  • 10
    • 0027323001 scopus 로고
    • Characteristics of an exochitinase from Streptomyces olivaceoviridis, its corresponding gene, putative protein domains and relationship to other chitinases
    • Blaak, H., Schnellmann, J., Walter, S., lyer, V.N., and Davies, R. W.: Characteristics of an exochitinase from Streptomyces olivaceoviridis, its corresponding gene, putative protein domains and relationship to other chitinases. Eur. J. Biochem., 241, 659-669 (1993).
    • (1993) Eur. J. Biochem. , vol.241 , pp. 659-669
    • Blaak, H.1    Schnellmann, J.2    Walter, S.3    Lyer, V.N.4    Davies, R.W.5
  • 11
    • 0027534187 scopus 로고
    • Cloning, sequencing, and expression of a chitinase gene from a marine bacterium, Alteromonas sp. strain O-7
    • Tsujibo, H., Orikoshi, H., Tanno, H., Fujimoto, K., Miyamoto, K., Imada, C., Okami, V., and Inamori, Y.: Cloning, sequencing, and expression of a chitinase gene from a marine bacterium, Alteromonas sp. strain O-7. J. Bacteriol., 175, 176-181 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 176-181
    • Tsujibo, H.1    Orikoshi, H.2    Tanno, H.3    Fujimoto, K.4    Miyamoto, K.5    Imada, C.6    Okami, V.7    Inamori, Y.8
  • 12
    • 0025171327 scopus 로고
    • Gene cloning of chitinase Al from Bacillus circulons WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin
    • Watanabe, T., Suzuki, K., Oyanagi, W., Ohnishi, K., and Tanaka, H.: Gene cloning of chitinase Al from Bacillus circulons WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin. J. Biol. Chem., 265, 15659-15665 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 15659-15665
    • Watanabe, T.1    Suzuki, K.2    Oyanagi, W.3    Ohnishi, K.4    Tanaka, H.5
  • 13
    • 0029619176 scopus 로고
    • Cloning and sequencing of chiC gene of Bacillus circulons WL12 and relationship of its product to some other chitinases and chitinase-like proteins
    • Alam, MD. M., Nikaidou, N., Tanaka, H., and Watanabe, T.: Cloning and sequencing of chiC gene of Bacillus circulons WL12 and relationship of its product to some other chitinases and chitinase-like proteins. J. Ferment. Bioengin., 80, 454-461 (1995).
    • (1995) J. Ferment. Bioengin. , vol.80 , pp. 454-461
    • Alam, M.D.M.1    Nikaidou, N.2    Tanaka, H.3    Watanabe, T.4
  • 14
    • 85004678184 scopus 로고
    • Necleotide sequence and analysis of a gene (chiA) for a chitinase from Streptomyces lividans 66
    • Miyashita, K. and Fujii, T.: Necleotide sequence and analysis of a gene (chiA) for a chitinase from Streptomyces lividans 66. Biosci. Biotech. Biochem., 57, 1691-1698 (1993).
    • (1993) Biosci. Biotech. Biochem. , vol.57 , pp. 1691-1698
    • Miyashita, K.1    Fujii, T.2
  • 15
    • 0029055875 scopus 로고
    • Cloning and primary structure of the chiA gene from Aeromonas caviae
    • Sitrit, Y., Vorgias, C. E., and Oppenheim, A.B.: Cloning and primary structure of the chiA gene from Aeromonas caviae. J. Bacteriol., 177, 4187-4189 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 4187-4189
    • Sitrit, Y.1    Vorgias, C.E.2    Oppenheim, A.B.3
  • 18
    • 0039948526 scopus 로고
    • Isolation, identification, and effect of oxygen supply on cultivation of chitin and chitosan degrading bacterium
    • Yamasaki, Y., Ohta, Y., Morita, K., Nakagawa, T., Kawamukai, M., and Malsuda, H.: Isolation, identification, and effect of oxygen supply on cultivation of chitin and chitosan degrading bacterium. Biosci. Biotech. Biochem., 56, 1325-1326 (1992).
    • (1992) Biosci. Biotech. Biochem. , vol.56 , pp. 1325-1326
    • Yamasaki, Y.1    Ohta, Y.2    Morita, K.3    Nakagawa, T.4    Kawamukai, M.5    Malsuda, H.6
  • 20
    • 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 (London), 227, 680-685 (1970).
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto, T. and Yagishita, K.: A simple activity measurement of lysozyme. Agric. Biol. Chem., 35, 1154-1156 (1971).
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 22
    • 0023901367 scopus 로고
    • Cloning and expression of a Streptomyces plicatus chitinase (chitinase-63) in Escherichia coli
    • Robbins, P.W., Albright, C., and Benfield, B.: Cloning and expression of a Streptomyces plicatus chitinase (chitinase-63) in Escherichia coli. J. Biol. Chem., 263, 443-447 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 443-447
    • Robbins, P.W.1    Albright, C.2    Benfield, B.3
  • 25
    • 0342444416 scopus 로고
    • GUS fusions: /S-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson, R. A., Kavanagh, T. A., and Bevan, M. W.: GUS fusions: /S-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J., 6, 3901-3907 (1987).
    • (1987) EMBO J. , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0022422726 scopus 로고
    • Structure and transcription of the tRNA Prol gene from Escherichia coli
    • Kuchino, Y., Mori, F., and Nishimnra, S.: Structure and transcription of the tRNA Prol gene from Escherichia coli. Nucl. Acids Res., 13, 3213-3220 (1985).
    • (1985) Nucl. Acids Res. , vol.13 , pp. 3213-3220
    • Kuchino, Y.1    Mori, F.2    Nishimnra, S.3
  • 28
    • 0003802645 scopus 로고
    • Genetic improvement of chitinase production by Serratia marcescens
    • John, P. Z. (ed.), Academic Press, New York
    • Horwitz, M., Reid, J., and Ogrydziak, D.: Genetic improvement of chitinase production by Serratia marcescens, p. 191-208. In John, P. Z. (ed.), Chitin, chitosan and related enzymes. Academic Press, New York (1984).
    • (1984) Chitin, Chitosan and Related Enzymes , pp. 191-208
    • Horwitz, M.1    Reid, J.2    Ogrydziak, D.3
  • 29
    • 0025834867 scopus 로고
    • Molecular cloning and characterization of chitinase genes from Streptomyces lividans 66
    • Miyashita, K., Fujii, T., and Sawada, Y.: Molecular cloning and characterization of chitinase genes from Streptomyces lividans 66. J. Gen. Microbiol., 137, 2065-2072 (1991).
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2065-2072
    • Miyashita, K.1    Fujii, T.2    Sawada, Y.3
  • 30
    • 0029040621 scopus 로고
    • The glucose kinase gene of Streptomyces coelicoior is not required for glucose repression of the chi63 promoter
    • Ingram, C. and Westpheling, J.: The glucose kinase gene of Streptomyces coelicoior is not required for glucose repression of the chi63 promoter. J. Bacteriol., 177, 3587-3588 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 3587-3588
    • Ingram, C.1    Westpheling, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.