메뉴 건너뛰기




Volumn 64, Issue 8, 1998, Pages 2794-2799

Expression and secretion of defined cutinase variants by Aspergillus awamori

Author keywords

[No Author keywords available]

Indexed keywords

CUTINASE;

EID: 0031879271     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.8.2794-2799.1998     Document Type: Article
Times cited : (31)

References (37)
  • 1
    • 0026683946 scopus 로고
    • Proteolytic degradation of heterologous proteins expressed in Aspergillus niger
    • Archer, D. B., D. A. Mackenzie, D. J. Jeenes, and I. N. Roberts. 1992. Proteolytic degradation of heterologous proteins expressed in Aspergillus niger. Biotechnol. Lett. 14:357-362.
    • (1992) Biotechnol. Lett. , vol.14 , pp. 357-362
    • Archer, D.B.1    Mackenzie, D.A.2    Jeenes, D.J.3    Roberts, I.N.4
  • 2
    • 0028021549 scopus 로고
    • Effect of amino acid deletions in the O-glycosylated region of Aspergillus awamori glucoamylase
    • Baker Libby, C., C. A. G. Cornett, P. J. Reilly, and C. Ford. 1994. Effect of amino acid deletions in the O-glycosylated region of Aspergillus awamori glucoamylase. Protein Eng. 7:1109-1114.
    • (1994) Protein Eng. , vol.7 , pp. 1109-1114
    • Baker Libby, C.1    Cornett, C.A.G.2    Reilly, P.J.3    Ford, C.4
  • 4
    • 0027508505 scopus 로고
    • Secretion of heterologous proteins by Aspergillus niger: Production of active human interleukin-6 in a protease deficient mutant by KEX2-like processing of a glucoamylase-HIL6 fusion protein
    • Broekhuijsen, M. P., I. E. Mattern, R. Contreras, J. R. Kinghorn, and C. A. M. J. J. Van den Hondel. 1993. Secretion of heterologous proteins by Aspergillus niger: production of active human interleukin-6 in a protease deficient mutant by KEX2-like processing of a glucoamylase-HIL6 fusion protein. J. Biotechnol. 31:135-145.
    • (1993) J. Biotechnol. , vol.31 , pp. 135-145
    • Broekhuijsen, M.P.1    Mattern, I.E.2    Contreras, R.3    Kinghorn, J.R.4    Van Den Hondel, C.A.M.J.J.5
  • 7
    • 0000056184 scopus 로고
    • Structure of cutinase gene, cDNA, and the derived amino acid sequence from phytopathogenic fungi
    • Ettinger, W. F., S. K. Thukral, and P. E. Kolattukudy. 1987. Structure of cutinase gene, cDNA, and the derived amino acid sequence from phytopathogenic fungi. Biochemistry 26:7883-7892.
    • (1987) Biochemistry , vol.26 , pp. 7883-7892
    • Ettinger, W.F.1    Thukral, S.K.2    Kolattukudy, P.E.3
  • 9
    • 0029028453 scopus 로고
    • A novel strategy for the isolation of defined pyrG mutants and the development of a site-specific integration system for Aspergillus awamori
    • Gouka, R. J., J. G. M. Hessing, H. Stam, W. Musters, and C. A. M. J. J. Van den Hondel. 1995. A novel strategy for the isolation of defined pyrG mutants and the development of a site-specific integration system for Aspergillus awamori. Curr. Genet. 27:536-540.
    • (1995) Curr. Genet. , vol.27 , pp. 536-540
    • Gouka, R.J.1    Hessing, J.G.M.2    Stam, H.3    Musters, W.4    Van Den Hondel, C.A.M.J.J.5
  • 11
    • 0029952011 scopus 로고    scopus 로고
    • Analysis of heterologous protein production in defined recombinant Aspergillus awamori strains
    • Gouka, R. J., P. J. Punt, J. G. M. Hessing, and C. A. M. J. J. Van den Hondel. 1996. Analysis of heterologous protein production in defined recombinant Aspergillus awamori strains. Appl. Environ. Microbiol. 62:1951-1957.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1951-1957
    • Gouka, R.J.1    Punt, P.J.2    Hessing, J.G.M.3    Van Den Hondel, C.A.M.J.J.4
  • 12
    • 0029826047 scopus 로고    scopus 로고
    • Overexpression of binding protein and disruption of the PMR1 gene synergistically stimulate secretion of bovine prochymosine but not plant thaumatin in yeast
    • Harmsen, M. M., M. I. Bruyne, H. A. Raué, and J. Maat. 1996. Overexpression of binding protein and disruption of the PMR1 gene synergistically stimulate secretion of bovine prochymosine but not plant thaumatin in yeast. Appl. Microbiol. Biotechnol. 46:365-370.
    • (1996) Appl. Microbiol. Biotechnol. , vol.46 , pp. 365-370
    • Harmsen, M.M.1    Bruyne, M.I.2    Raué, H.A.3    Maat, J.4
  • 14
    • 0019877072 scopus 로고
    • Rapid and efficient cosmid cloning
    • Ish-Horowicz, D., and J. F. Burke. 1981. Rapid and efficient cosmid cloning. Nucleic Acids Res. 9:2989-2998.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 2989-2998
    • Ish-Horowicz, D.1    Burke, J.F.2
  • 15
    • 0029809321 scopus 로고    scopus 로고
    • Effect of mutagenesis of GPIIb amino acid 273 on the expression and conformation of the platelet integrin GPIIb-IIIa
    • Kahn, M. J., T. Kieber-Emmons, G. Vilaire, R. Murali, M. Poncz, and J. S. Bennett. 1996. Effect of mutagenesis of GPIIb amino acid 273 on the expression and conformation of the platelet integrin GPIIb-IIIa. Biochemistry 35:14304-14311.
    • (1996) Biochemistry , vol.35 , pp. 14304-14311
    • Kahn, M.J.1    Kieber-Emmons, T.2    Vilaire, G.3    Murali, R.4    Poncz, M.5    Bennett, J.S.6
  • 16
    • 0006347676 scopus 로고
    • A simple colony blot procedure for Neurospora
    • Kinsey, J. A. 1989. A simple colony blot procedure for Neurospora. Fungal Genet. Newsl. 36:45-46.
    • (1989) Fungal Genet. Newsl. , vol.36 , pp. 45-46
    • Kinsey, J.A.1
  • 17
    • 0023930331 scopus 로고
    • Transformation of Penicillium chrysochenum using dominant selection markers and expression of an Escherichia coli lacZ fusion gene
    • Kolar, M., P. J. Punt, C. A. M. J. J. Van den Hondel, and H. Schwab. 1988. Transformation of Penicillium chrysochenum using dominant selection markers and expression of an Escherichia coli lacZ fusion gene. Gene 62:127-134.
    • (1988) Gene , vol.62 , pp. 127-134
    • Kolar, M.1    Punt, P.J.2    Van Den Hondel, C.A.M.J.J.3    Schwab, H.4
  • 18
    • 0001961791 scopus 로고
    • Cutinases from fungi and pollen
    • B. Borgström and H. Brockman (ed.), Elsevier, Amsterdam, The Netherlands
    • Kolattukudy, P. E. 1984. Cutinases from fungi and pollen, p. 471-504. In B. Borgström and H. Brockman (ed.), Lipases. Elsevier, Amsterdam, The Netherlands.
    • (1984) Lipases , pp. 471-504
    • Kolattukudy, P.E.1
  • 19
    • 0026726710 scopus 로고
    • Effect of overproduction of heat shock chaperones GroESL and DnaK on human procollagenase production by Escherichia coli
    • Lee, S. C., and P. O. Olins. 1992. Effect of overproduction of heat shock chaperones GroESL and DnaK on human procollagenase production by Escherichia coli. J. Biol. Chem. 267:2849-2852.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2849-2852
    • Lee, S.C.1    Olins, P.O.2
  • 20
    • 0026066885 scopus 로고
    • Codon usage in Aspergillus nidulans
    • Lloyd, A. T., and P. M. Sharp. 1991. Codon usage in Aspergillus nidulans. Mol. Gen. Genet. 230:288-294.
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 288-294
    • Lloyd, A.T.1    Sharp, P.M.2
  • 21
    • 0026583770 scopus 로고
    • Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent
    • Martinez, C., P. de Geus, M. Lauwereys, G. Matthysens, and C. Cambillau. 1992. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature 356:615-618.
    • (1992) Nature , vol.356 , pp. 615-618
    • Martinez, C.1    De Geus, P.2    Lauwereys, M.3    Matthysens, G.4    Cambillau, C.5
  • 22
    • 0023777869 scopus 로고
    • Isolation and characterisation of the glyceraldehyde-3-phosphate dehydrogenase gene of Aspergillus nidulans
    • Punt, P. J., M. A. Dingemanse, B. J. M. Jacobs-Meijsing, P. H. Pouwels, and C. A. M. J. J. Van den Hondel. 1988. Isolation and characterisation of the glyceraldehyde-3-phosphate dehydrogenase gene of Aspergillus nidulans. Gene 69:49-57.
    • (1988) Gene , vol.69 , pp. 49-57
    • Punt, P.J.1    Dingemanse, M.A.2    Jacobs-Meijsing, B.J.M.3    Pouwels, P.H.4    Van Den Hondel, C.A.M.J.J.5
  • 23
    • 0027016529 scopus 로고
    • Transformation of filamentous fungi based on hygromycin B and phleomycin resistance markers
    • Punt, P. J., and C. A. M. J. J. Van den Hondel. 1992. Transformation of filamentous fungi based on hygromycin B and phleomycin resistance markers. Methods Enzymol. 216:447-457.
    • (1992) Methods Enzymol. , vol.216 , pp. 447-457
    • Punt, P.J.1    Van Den Hondel, C.A.M.J.J.2
  • 24
    • 0027275896 scopus 로고
    • Retention of a co-translational translocated mutant protein of carboxypeptidase Y of Saccharomyces cerevisiae in endoplasmic reticulum
    • Rad, M. R., and H. Katz. 1993. Retention of a co-translational translocated mutant protein of carboxypeptidase Y of Saccharomyces cerevisiae in endoplasmic reticulum. FEMS Microbiol. Lett. 111:165-170.
    • (1993) FEMS Microbiol. Lett. , vol.111 , pp. 165-170
    • Rad, M.R.1    Katz, H.2
  • 25
    • 0028219869 scopus 로고
    • Protein disulphide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae
    • Robinson, A. S., V. Hines, and K. D. Wittrup. 1994. Protein disulphide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae. Bio/Technology 12:381-384.
    • (1994) Bio/Technology , vol.12 , pp. 381-384
    • Robinson, A.S.1    Hines, V.2    Wittrup, K.D.3
  • 26
    • 0344474668 scopus 로고    scopus 로고
    • Impaired secretion of a hydrophobic cutinase by Saccharomyces cerevisiae correlates with an increased association with BiP
    • Sagt, C. M. J., W. H. Müller, J. Boonstra, A. J. Verkleij, and C. T. Verrips. 1998. Impaired secretion of a hydrophobic cutinase by Saccharomyces cerevisiae correlates with an increased association with BiP. Appl. Environ. Microbiol. 64:316-324.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 316-324
    • Sagt, C.M.J.1    Müller, W.H.2    Boonstra, J.3    Verkleij, A.J.4    Verrips, C.T.5
  • 28
    • 0021878793 scopus 로고
    • Heterologous protein secretion from yeast
    • Smith, R. A., M. J. Duncan, and D. T. Moir. 1985. Heterologous protein secretion from yeast. Science 229:1219-1224.
    • (1985) Science , vol.229 , pp. 1219-1224
    • Smith, R.A.1    Duncan, M.J.2    Moir, D.T.3
  • 29
    • 0000730153 scopus 로고
    • Cloning and structure determination of cDNA for cutinase, an enzyme involved in fungal penetration of plants
    • Soliday, C. L., W. H. Flurkey, T. W. Okita, and P. E. Kolattukudy. 1984. Cloning and structure determination of cDNA for cutinase, an enzyme involved in fungal penetration of plants. Proc. Natl. Acad. Sci. USA 82:3939-3943.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3939-3943
    • Soliday, C.L.1    Flurkey, W.H.2    Okita, T.W.3    Kolattukudy, P.E.4
  • 30
    • 0026533312 scopus 로고
    • Cloning and analysis of CUT1, a cutinase gene from Magnaporta grisea
    • Sweigard, J. A., F. G. Chumley, and B. Valent. 1992. Cloning and analysis of CUT1, a cutinase gene from Magnaporta grisea. Mol. Gen. Genet. 232:174-182.
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 174-182
    • Sweigard, J.A.1    Chumley, F.G.2    Valent, B.3
  • 32
    • 0029056506 scopus 로고
    • Construction and heterologous expression of a synthetic copy of the cutinase cDNa from Fusarium solani pisi
    • Van Gemeren, I. A., W. Musters, C. A. M. J. J. Van den Hondel, and C. T. Verrips. 1995. Construction and heterologous expression of a synthetic copy of the cutinase cDNA from Fusarium solani pisi. J. Biotechnol. 40:155-162.
    • (1995) J. Biotechnol. , vol.40 , pp. 155-162
    • Van Gemeren, I.A.1    Musters, W.2    Van Den Hondel, C.A.M.J.J.3    Verrips, C.T.4
  • 33
    • 0029762302 scopus 로고    scopus 로고
    • The effect of pre- and pro-sequences and multi-copy integration on heterologous expression of the Fusarium solani pisi cutinase gene in Aspergillus awamori
    • Van Gemeren, I. A., A. Beijersbergen, W. Musters, R. J. Gouka, C. A. M. J. J. Van den Hondel, and C. T. Verrips. 1996. The effect of pre- and pro-sequences and multi-copy integration on heterologous expression of the Fusarium solani pisi cutinase gene in Aspergillus awamori. Appl. Microbiol. Biotechnol. 45:755-763.
    • (1996) Appl. Microbiol. Biotechnol. , vol.45 , pp. 755-763
    • Van Gemeren, I.A.1    Beijersbergen, A.2    Musters, W.3    Gouka, R.J.4    Van Den Hondel, C.A.M.J.J.5    Verrips, C.T.6
  • 36
    • 0028298127 scopus 로고
    • Mutations and off-pathway aggregation of proteins
    • Wetzel, R. 1994. Mutations and off-pathway aggregation of proteins. TIBTECH 12:193-198.
    • (1994) TIBTECH , vol.12 , pp. 193-198
    • Wetzel, R.1
  • 37
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanish-Perron, C. J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanish-Perron1    Vieira, C.J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.