Expression and secretion of Bacillus polymyxa neopullulanase in Saccharomyces cerevisiae
We have isolated the gene encoding the neopullulanase enzyme from Bacillus polymyxa CECT 155. It consists of an open reading frame of 1545 bp that could code for a protein of 515 amino acids. This open reading frame was expressed in Bacillus subtilis and the corresponding transformants produced extr...
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| Autor*in: |
Yebra, Marı́a J [verfasserIn] Blasco, Amalia [verfasserIn] Sanz, Pascual [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1999 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: FEMS microbiology letters - Federation of European Microbiological Societies ; GKD-ID: 114439X, Oxford [u.a.] : Wiley-Blackwell, 1977, 170(1999), 1, Seite 0 |
| Übergeordnetes Werk: |
volume:170 ; year:1999 ; number:1 ; pages:0 |
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| DOI / URN: |
10.1111/j.1574-6968.1999.tb13353.x |
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| 520 | |a We have isolated the gene encoding the neopullulanase enzyme from Bacillus polymyxa CECT 155. It consists of an open reading frame of 1545 bp that could code for a protein of 515 amino acids. This open reading frame was expressed in Bacillus subtilis and the corresponding transformants produced extracellular neopullulanase. The neopullulanase gene was also expressed in Saccharomyces cerevisiae placing it under the control of the yeast actin gene (ACT1) promoter. Clones containing the intact neopullulanase gene, including its own bacterial signal sequence, gave rise to the synthesis of active, but intracellular, enzyme by S. cerevisiae transformants. When sequences specifying the signal sequence and leader region of the yeast mating pheromone α-factor (MFα1) were fused upstream of the gene encoding the neopullulanase enzyme, the enzyme was secreted by S. cerevisiae. The secreted protein presented the same biochemical properties and the same apparent molecular mass as the Bacillus polymyxa original enzyme. The predicted amino acid sequence of the neopullulanase protein contained sequence motifs conserved among amylolytic enzymes. Northern blot analysis indicated that the transcription of the neopullulanase gene in B. polymyxa was induced by the presence of the substrate, pullulan, in the culture, and was repressed by glucose. | ||
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10.1111/j.1574-6968.1999.tb13353.x doi (DE-627)NLEJ242908357 DE-627 ger DE-627 rakwb Yebra, Marı́a J verfasserin aut Expression and secretion of Bacillus polymyxa neopullulanase in Saccharomyces cerevisiae Oxford, UK Blackwell Publishing Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have isolated the gene encoding the neopullulanase enzyme from Bacillus polymyxa CECT 155. It consists of an open reading frame of 1545 bp that could code for a protein of 515 amino acids. This open reading frame was expressed in Bacillus subtilis and the corresponding transformants produced extracellular neopullulanase. The neopullulanase gene was also expressed in Saccharomyces cerevisiae placing it under the control of the yeast actin gene (ACT1) promoter. Clones containing the intact neopullulanase gene, including its own bacterial signal sequence, gave rise to the synthesis of active, but intracellular, enzyme by S. cerevisiae transformants. When sequences specifying the signal sequence and leader region of the yeast mating pheromone α-factor (MFα1) were fused upstream of the gene encoding the neopullulanase enzyme, the enzyme was secreted by S. cerevisiae. The secreted protein presented the same biochemical properties and the same apparent molecular mass as the Bacillus polymyxa original enzyme. The predicted amino acid sequence of the neopullulanase protein contained sequence motifs conserved among amylolytic enzymes. Northern blot analysis indicated that the transcription of the neopullulanase gene in B. polymyxa was induced by the presence of the substrate, pullulan, in the culture, and was repressed by glucose. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Neopullulanase Blasco, Amalia verfasserin aut Sanz, Pascual verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 170(1999), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:170 year:1999 number:1 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1999.tb13353.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 170 1999 1 0 |
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10.1111/j.1574-6968.1999.tb13353.x doi (DE-627)NLEJ242908357 DE-627 ger DE-627 rakwb Yebra, Marı́a J verfasserin aut Expression and secretion of Bacillus polymyxa neopullulanase in Saccharomyces cerevisiae Oxford, UK Blackwell Publishing Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have isolated the gene encoding the neopullulanase enzyme from Bacillus polymyxa CECT 155. It consists of an open reading frame of 1545 bp that could code for a protein of 515 amino acids. This open reading frame was expressed in Bacillus subtilis and the corresponding transformants produced extracellular neopullulanase. The neopullulanase gene was also expressed in Saccharomyces cerevisiae placing it under the control of the yeast actin gene (ACT1) promoter. Clones containing the intact neopullulanase gene, including its own bacterial signal sequence, gave rise to the synthesis of active, but intracellular, enzyme by S. cerevisiae transformants. When sequences specifying the signal sequence and leader region of the yeast mating pheromone α-factor (MFα1) were fused upstream of the gene encoding the neopullulanase enzyme, the enzyme was secreted by S. cerevisiae. The secreted protein presented the same biochemical properties and the same apparent molecular mass as the Bacillus polymyxa original enzyme. The predicted amino acid sequence of the neopullulanase protein contained sequence motifs conserved among amylolytic enzymes. Northern blot analysis indicated that the transcription of the neopullulanase gene in B. polymyxa was induced by the presence of the substrate, pullulan, in the culture, and was repressed by glucose. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Neopullulanase Blasco, Amalia verfasserin aut Sanz, Pascual verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 170(1999), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:170 year:1999 number:1 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1999.tb13353.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 170 1999 1 0 |
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10.1111/j.1574-6968.1999.tb13353.x doi (DE-627)NLEJ242908357 DE-627 ger DE-627 rakwb Yebra, Marı́a J verfasserin aut Expression and secretion of Bacillus polymyxa neopullulanase in Saccharomyces cerevisiae Oxford, UK Blackwell Publishing Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have isolated the gene encoding the neopullulanase enzyme from Bacillus polymyxa CECT 155. It consists of an open reading frame of 1545 bp that could code for a protein of 515 amino acids. This open reading frame was expressed in Bacillus subtilis and the corresponding transformants produced extracellular neopullulanase. The neopullulanase gene was also expressed in Saccharomyces cerevisiae placing it under the control of the yeast actin gene (ACT1) promoter. Clones containing the intact neopullulanase gene, including its own bacterial signal sequence, gave rise to the synthesis of active, but intracellular, enzyme by S. cerevisiae transformants. When sequences specifying the signal sequence and leader region of the yeast mating pheromone α-factor (MFα1) were fused upstream of the gene encoding the neopullulanase enzyme, the enzyme was secreted by S. cerevisiae. The secreted protein presented the same biochemical properties and the same apparent molecular mass as the Bacillus polymyxa original enzyme. The predicted amino acid sequence of the neopullulanase protein contained sequence motifs conserved among amylolytic enzymes. Northern blot analysis indicated that the transcription of the neopullulanase gene in B. polymyxa was induced by the presence of the substrate, pullulan, in the culture, and was repressed by glucose. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Neopullulanase Blasco, Amalia verfasserin aut Sanz, Pascual verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 170(1999), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:170 year:1999 number:1 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1999.tb13353.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 170 1999 1 0 |
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10.1111/j.1574-6968.1999.tb13353.x doi (DE-627)NLEJ242908357 DE-627 ger DE-627 rakwb Yebra, Marı́a J verfasserin aut Expression and secretion of Bacillus polymyxa neopullulanase in Saccharomyces cerevisiae Oxford, UK Blackwell Publishing Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have isolated the gene encoding the neopullulanase enzyme from Bacillus polymyxa CECT 155. It consists of an open reading frame of 1545 bp that could code for a protein of 515 amino acids. This open reading frame was expressed in Bacillus subtilis and the corresponding transformants produced extracellular neopullulanase. The neopullulanase gene was also expressed in Saccharomyces cerevisiae placing it under the control of the yeast actin gene (ACT1) promoter. Clones containing the intact neopullulanase gene, including its own bacterial signal sequence, gave rise to the synthesis of active, but intracellular, enzyme by S. cerevisiae transformants. When sequences specifying the signal sequence and leader region of the yeast mating pheromone α-factor (MFα1) were fused upstream of the gene encoding the neopullulanase enzyme, the enzyme was secreted by S. cerevisiae. The secreted protein presented the same biochemical properties and the same apparent molecular mass as the Bacillus polymyxa original enzyme. The predicted amino acid sequence of the neopullulanase protein contained sequence motifs conserved among amylolytic enzymes. Northern blot analysis indicated that the transcription of the neopullulanase gene in B. polymyxa was induced by the presence of the substrate, pullulan, in the culture, and was repressed by glucose. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Neopullulanase Blasco, Amalia verfasserin aut Sanz, Pascual verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 170(1999), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:170 year:1999 number:1 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1999.tb13353.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 170 1999 1 0 |
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10.1111/j.1574-6968.1999.tb13353.x doi (DE-627)NLEJ242908357 DE-627 ger DE-627 rakwb Yebra, Marı́a J verfasserin aut Expression and secretion of Bacillus polymyxa neopullulanase in Saccharomyces cerevisiae Oxford, UK Blackwell Publishing Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have isolated the gene encoding the neopullulanase enzyme from Bacillus polymyxa CECT 155. It consists of an open reading frame of 1545 bp that could code for a protein of 515 amino acids. This open reading frame was expressed in Bacillus subtilis and the corresponding transformants produced extracellular neopullulanase. The neopullulanase gene was also expressed in Saccharomyces cerevisiae placing it under the control of the yeast actin gene (ACT1) promoter. Clones containing the intact neopullulanase gene, including its own bacterial signal sequence, gave rise to the synthesis of active, but intracellular, enzyme by S. cerevisiae transformants. When sequences specifying the signal sequence and leader region of the yeast mating pheromone α-factor (MFα1) were fused upstream of the gene encoding the neopullulanase enzyme, the enzyme was secreted by S. cerevisiae. The secreted protein presented the same biochemical properties and the same apparent molecular mass as the Bacillus polymyxa original enzyme. The predicted amino acid sequence of the neopullulanase protein contained sequence motifs conserved among amylolytic enzymes. Northern blot analysis indicated that the transcription of the neopullulanase gene in B. polymyxa was induced by the presence of the substrate, pullulan, in the culture, and was repressed by glucose. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Neopullulanase Blasco, Amalia verfasserin aut Sanz, Pascual verfasserin aut In Federation of European Microbiological Societies ; GKD-ID: 114439X FEMS microbiology letters Oxford [u.a.] : Wiley-Blackwell, 1977 170(1999), 1, Seite 0 Online-Ressource (DE-627)NLEJ243927053 (DE-600)1501716-3 1574-6968 nnns volume:170 year:1999 number:1 pages:0 http://dx.doi.org/10.1111/j.1574-6968.1999.tb13353.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 170 1999 1 0 |
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Expression and secretion of Bacillus polymyxa neopullulanase in Saccharomyces cerevisiae |
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We have isolated the gene encoding the neopullulanase enzyme from Bacillus polymyxa CECT 155. It consists of an open reading frame of 1545 bp that could code for a protein of 515 amino acids. This open reading frame was expressed in Bacillus subtilis and the corresponding transformants produced extracellular neopullulanase. The neopullulanase gene was also expressed in Saccharomyces cerevisiae placing it under the control of the yeast actin gene (ACT1) promoter. Clones containing the intact neopullulanase gene, including its own bacterial signal sequence, gave rise to the synthesis of active, but intracellular, enzyme by S. cerevisiae transformants. When sequences specifying the signal sequence and leader region of the yeast mating pheromone α-factor (MFα1) were fused upstream of the gene encoding the neopullulanase enzyme, the enzyme was secreted by S. cerevisiae. The secreted protein presented the same biochemical properties and the same apparent molecular mass as the Bacillus polymyxa original enzyme. The predicted amino acid sequence of the neopullulanase protein contained sequence motifs conserved among amylolytic enzymes. Northern blot analysis indicated that the transcription of the neopullulanase gene in B. polymyxa was induced by the presence of the substrate, pullulan, in the culture, and was repressed by glucose. |
| abstractGer |
We have isolated the gene encoding the neopullulanase enzyme from Bacillus polymyxa CECT 155. It consists of an open reading frame of 1545 bp that could code for a protein of 515 amino acids. This open reading frame was expressed in Bacillus subtilis and the corresponding transformants produced extracellular neopullulanase. The neopullulanase gene was also expressed in Saccharomyces cerevisiae placing it under the control of the yeast actin gene (ACT1) promoter. Clones containing the intact neopullulanase gene, including its own bacterial signal sequence, gave rise to the synthesis of active, but intracellular, enzyme by S. cerevisiae transformants. When sequences specifying the signal sequence and leader region of the yeast mating pheromone α-factor (MFα1) were fused upstream of the gene encoding the neopullulanase enzyme, the enzyme was secreted by S. cerevisiae. The secreted protein presented the same biochemical properties and the same apparent molecular mass as the Bacillus polymyxa original enzyme. The predicted amino acid sequence of the neopullulanase protein contained sequence motifs conserved among amylolytic enzymes. Northern blot analysis indicated that the transcription of the neopullulanase gene in B. polymyxa was induced by the presence of the substrate, pullulan, in the culture, and was repressed by glucose. |
| abstract_unstemmed |
We have isolated the gene encoding the neopullulanase enzyme from Bacillus polymyxa CECT 155. It consists of an open reading frame of 1545 bp that could code for a protein of 515 amino acids. This open reading frame was expressed in Bacillus subtilis and the corresponding transformants produced extracellular neopullulanase. The neopullulanase gene was also expressed in Saccharomyces cerevisiae placing it under the control of the yeast actin gene (ACT1) promoter. Clones containing the intact neopullulanase gene, including its own bacterial signal sequence, gave rise to the synthesis of active, but intracellular, enzyme by S. cerevisiae transformants. When sequences specifying the signal sequence and leader region of the yeast mating pheromone α-factor (MFα1) were fused upstream of the gene encoding the neopullulanase enzyme, the enzyme was secreted by S. cerevisiae. The secreted protein presented the same biochemical properties and the same apparent molecular mass as the Bacillus polymyxa original enzyme. The predicted amino acid sequence of the neopullulanase protein contained sequence motifs conserved among amylolytic enzymes. Northern blot analysis indicated that the transcription of the neopullulanase gene in B. polymyxa was induced by the presence of the substrate, pullulan, in the culture, and was repressed by glucose. |
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Expression and secretion of Bacillus polymyxa neopullulanase in Saccharomyces cerevisiae |
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Blasco, Amalia Sanz, Pascual |
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10.1111/j.1574-6968.1999.tb13353.x |
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