DC Field | Value | Language |
---|---|---|
dc.contributor.author | Jun Won Lee | - |
dc.contributor.author | Dae Ook Kang | - |
dc.contributor.author | Bo Yeon Kim | - |
dc.contributor.author | Won Keun Oh | - |
dc.contributor.author | Tae Ick Mheen | - |
dc.contributor.author | Yu Ryang Pyun | - |
dc.contributor.author | Jong Seog Ahn | - |
dc.date.accessioned | 2017-04-19T08:57:24Z | - |
dc.date.available | 2017-04-19T08:57:24Z | - |
dc.date.issued | 2000 | - |
dc.identifier.issn | 0378-1097 | - |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/5243 | - |
dc.description.abstract | To improve the efficiency of the glucoamylase signal peptide (GSP) of Saccharomyces diastaticus for the secretion of foreign proteins, hybrid plasmids containing one of four types of GSP mutant (m1, Pro-18→Leu-18; m2, Tyr-13→Leu-13; m3, Ser-9→Leu-9; m4, Asn-5→Pro-5) were constructed and evaluated in Saccharomyces cerevisiae using Bacillus endo-1,4-β-D-glucanase (CMCase) as a reporter gene. CMCase secretion by m1, m2 and m3 GSP mutants was increased, likely resulting from a higher probability of the modified GSP to assume an α-helical structure. Especially in the case of m3, the substitution of Leu for a polar residue, Ser-9, in the hydrophobic region resulted in approximately a twofold increase in extracellular CMCase activity. In mutant 4, which disrupts the α-helix of GSP, CMCase was less efficiently secreted. | - |
dc.publisher | Oxford Univ Press | - |
dc.title | Mutagenesis of the glucoamylase signal peptide of Saccharomyces diastaticus and functional analysis in Saccharomyces cerevisiae | - |
dc.title.alternative | Mutagenesis of the glucoamylase signal peptide of Saccharomyces diastaticus and functional analysis in Saccharomyces cerevisiae | - |
dc.type | Article | - |
dc.citation.title | FEMS Microbiology Letters | - |
dc.citation.number | 1 | - |
dc.citation.endPage | 11 | - |
dc.citation.startPage | 7 | - |
dc.citation.volume | 193 | - |
dc.contributor.affiliatedAuthor | Jun Won Lee | - |
dc.contributor.affiliatedAuthor | Dae Ook Kang | - |
dc.contributor.affiliatedAuthor | Bo Yeon Kim | - |
dc.contributor.affiliatedAuthor | Won Keun Oh | - |
dc.contributor.affiliatedAuthor | Tae Ick Mheen | - |
dc.contributor.affiliatedAuthor | Jong Seog Ahn | - |
dc.contributor.alternativeName | 이준원 | - |
dc.contributor.alternativeName | 강대욱 | - |
dc.contributor.alternativeName | 김보연 | - |
dc.contributor.alternativeName | 오원근 | - |
dc.contributor.alternativeName | 민태익 | - |
dc.contributor.alternativeName | 변유량 | - |
dc.contributor.alternativeName | 안종석 | - |
dc.identifier.bibliographicCitation | FEMS Microbiology Letters, vol. 193, no. 1, pp. 7-11 | - |
dc.identifier.doi | 10.1111/j.1574-6968.2000.tb09394.x | - |
dc.subject.keyword | glucoamylase signal peptide | - |
dc.subject.keyword | Saccharomyces diastaticus | - |
dc.subject.keyword | Bacillus endo-1,4-β-D-glucanase | - |
dc.subject.keyword | Mutagenesis | - |
dc.subject.keyword | Saccharomyces cerevisiae | - |
dc.subject.keyword | secretion | - |
dc.subject.local | glucoamylase signal peptide | - |
dc.subject.local | Saccharomyces diastaticus | - |
dc.subject.local | Bacillus endo-1,4-β-D-glucanase | - |
dc.subject.local | Mutagenesis | - |
dc.subject.local | mutagenesis | - |
dc.subject.local | Saccharomyces cerevisiae | - |
dc.subject.local | saccharomyces cerevisiae | - |
dc.subject.local | secretion | - |
dc.subject.local | Secretion | - |
dc.description.journalClass | Y | - |
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