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Volumn 26, Issue 3, 2002, Pages 337-342

A dual protein expression system in Bacillus subtilis

Author keywords

Bacillus subtilis; Dual expression; Glucanase; Prophage; Xylanase

Indexed keywords

BACILLUS SUBTILIS; GENE EXPRESSION; GENES, BACTERIAL; GENETIC ENGINEERING; GLYCOSIDE HYDROLASES; MOLECULAR SEQUENCE DATA; PROMOTER REGIONS (GENETICS); RECOMBINANT PROTEINS; TRANSCRIPTION, GENETIC; XYLAN ENDO-1,3-BETA-XYLOSIDASE; XYLOSIDASES;

EID: 0036915133     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(02)00552-1     Document Type: Article
Times cited : (15)

References (18)
  • 1
    • 0024462201 scopus 로고
    • Purification and in vitro DNA-binding specificity of the Bacillus subtilis phage φ105 repressor
    • L.V. Kaer, M.V. Montagus, P. Dhaese, Purification and in vitro DNA-binding specificity of the Bacillus subtilis phage φ105 repressor, J. Biol. Chem. 264 (1989) 14784-14791.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14784-14791
    • Kaer, L.V.1    Montagus, M.V.2    Dhaese, P.3
  • 2
    • 0023971123 scopus 로고
    • Interaction of Bacillus subtilis phage φ105 repressor with operator DNA: A genetic analysis
    • L.V. Kaer, G. Yannick, M.V. Montagus, P. Dhaese, Interaction of Bacillus subtilis phage φ105 repressor with operator DNA: A genetic analysis, EMBO J. 7 (1988) 859-866.
    • (1988) EMBO J. , vol.7 , pp. 859-866
    • Kaer, L.V.1    Yannick, G.2    Montagus, M.V.3    Dhaese, P.4
  • 3
    • 0028893338 scopus 로고
    • Characterization of an insertion in the phage phi 105 genome that blocks host Bacillus subtilis lysis and provides strong expression of heterologous genes
    • Y.C. Leung, J. Errington, Characterization of an insertion in the phage phi 105 genome that blocks host Bacillus subtilis lysis and provides strong expression of heterologous genes, Gene 154 (1995) 1-6.
    • (1995) Gene , vol.154 , pp. 1-6
    • Leung, Y.C.1    Errington, J.2
  • 4
    • 0021014754 scopus 로고
    • Molecular cloning of a B. subtilis xylanase gene in Escherichia coli
    • R. Bernier Jr., H. Driguez, M. Deschrocers, Molecular cloning of a B. subtilis xylanase gene in Escherichia coli, Gene 26 (1983) 59-65.
    • (1983) Gene , vol.26 , pp. 59-65
    • Bernier R., Jr.1    Driguez, H.2    Deschrocers, M.3
  • 5
    • 0026468190 scopus 로고
    • Molecular cloning and expression of Bacillus subtilis bglS gene in Saccharomyces cerevisiae
    • Y. Chen, X. Huang, D. Song, F. Yang, W. Zheng, Molecular cloning and expression of Bacillus subtilis bglS gene in Saccharomyces cerevisiae, Curr. Microbiol. 25 (1992) 279-282.
    • (1992) Curr. Microbiol. , vol.25 , pp. 279-282
    • Chen, Y.1    Huang, X.2    Song, D.3    Yang, F.4    Zheng, W.5
  • 6
    • 0032984477 scopus 로고    scopus 로고
    • Molecular and biotechnological aspects of xylanases
    • N. Kulkarmi, A. Shendye, M. Rao, Molecular and biotechnological aspects of xylanases, FEMS Microbiol. Rev. 23 (1999) 411-456.
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 411-456
    • Kulkarmi, N.1    Shendye, A.2    Rao, M.3
  • 7
    • 0027518228 scopus 로고
    • An efficient expression and secretion system based on Bacillus subtilis phage φ105 and its use for the production of B. cereus β-lactamase I
    • S.J. Thornewell, A.K. East, J. Errington, An efficient expression and secretion system based on Bacillus subtilis phage φ105 and its use for the production of B. cereus β-lactamase I, Gene 133 (1993) 47-53.
    • (1993) Gene , vol.133 , pp. 47-53
    • Thornewell, S.J.1    East, A.K.2    Errington, J.3
  • 8
    • 0021994611 scopus 로고
    • Thermoinducible transcription system for Bacillus subtilis that utilize control elements from temperate phage phi-105
    • M.S. Osbume, R.J. Craig, D.M. Rothstein, Thermoinducible transcription system for Bacillus subtilis that utilize control elements from temperate phage phi-105, J. Bacteriol. 163 (1985) 1101-1108.
    • (1985) J. Bacteriol. , vol.163 , pp. 1101-1108
    • Osbume, M.S.1    Craig, R.J.2    Rothstein, D.M.3
  • 9
    • 0013833244 scopus 로고
    • Determination of reducing sugar with improved precision
    • S. Dygert, L.H. Li, D. Florida, J.A. Thoma, Determination of reducing sugar with improved precision, Anal. Biochem. 13 (1965) 367-374.
    • (1965) Anal. Biochem. , vol.13 , pp. 367-374
    • Dygert, S.1    Li, L.H.2    Florida, D.3    Thoma, J.A.4
  • 10
    • 0032947597 scopus 로고    scopus 로고
    • Temporal expression of the Bacillus subtilis secA gene, encoding a central component of the preprotein translocase
    • M. Herbort, M. Klein, H. Manting, A.J.M. Driessen, R. Freudl, Temporal expression of the Bacillus subtilis secA gene, encoding a central component of the preprotein translocase, J. Bacteriol. 181 (1999) 493-500.
    • (1999) J. Bacteriol. , vol.181 , pp. 493-500
    • Herbort, M.1    Klein, M.2    Manting, H.3    Driessen, A.J.M.4    Freudl, R.5
  • 11
    • 0024064875 scopus 로고
    • Mutants of Bacillus subtilis defective in protein export
    • V.P. Kontinen, M. Sarvas, Mutants of Bacillus subtilis defective in protein export, J. Gen. Microbiol. 134 (1988) 2333-2344.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 2333-2344
    • Kontinen, V.P.1    Sarvas, M.2
  • 13
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • D. Missiakas, S. Raina, Protein folding in the bacterial periplasm, J. Bacteriol. 179 (1997) 2465-2471.
    • (1997) J. Bacteriol. , vol.179 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 14
    • 0027476802 scopus 로고
    • Characterization of a Bacillus subtilis Sec A mutant protein deficient in translocation ATPase and release from the membrane
    • J. Van der Wolk, M. Klose, R.A. Breukink, B. Demel, B. de Kruijff, R. Freudi, A.J.M. Driessen, Characterization of a Bacillus subtilis Sec A mutant protein deficient in translocation ATPase and release from the membrane, Mol. Microbiol. 8 (1993) 31-42.
    • (1993) Mol. Microbiol. , vol.8 , pp. 31-42
    • Van der Wolk, J.1    Klose, M.2    Breukink, R.A.3    Demel, B.4    De Kruijff, B.5    Freudi, R.6    Driessen, A.J.M.7
  • 15
    • 0035108399 scopus 로고    scopus 로고
    • Quantitation and capacity of the secretion apparatus and requirement for PrsA in growth and secretion of α-amylase in Bacillus sutilis
    • M. Vitikainen, T. Pummi, U. Airaksinen, E. Wahlstrom, H. Wu, M. Sarvas, V.P. Kontinen, Quantitation and capacity of the secretion apparatus and requirement for PrsA in growth and secretion of α-amylase in Bacillus sutilis, J. Biotech. 183 (2001) 1881-1890.
    • (2001) J. Biotech. , vol.183 , pp. 1881-1890
    • Vitikainen, M.1    Pummi, T.2    Airaksinen, U.3    Wahlstrom, E.4    Wu, H.5    Sarvas, M.6    Kontinen, V.P.7
  • 18
    • 0030868265 scopus 로고    scopus 로고
    • Bacillus subtilis contains four closely related type I signal peptidases with overlapping substrate specificities
    • H. Tjalsma, M.A. Noback, S. Bron, G. Venema, K. Yamane, J.M. van Diji, Bacillus subtilis contains four closely related type I signal peptidases with overlapping substrate specificities, J. Biol. Chem. 272 (1997) 25983-25992.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25983-25992
    • Tjalsma, H.1    Noback, M.A.2    Bron, S.3    Venema, G.4    Yamane, K.5    Van Diji, J.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.