Mutagenesis of the glucoamylase signal peptide of Saccharomyces diastaticus and functional analysis in Saccharomyces cerevisiae

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dc.contributor.authorJun Won Lee-
dc.contributor.authorDae Ook Kang-
dc.contributor.authorBo Yeon Kim-
dc.contributor.authorWon Keun Oh-
dc.contributor.authorTae Ick Mheen-
dc.contributor.authorYu Ryang Pyun-
dc.contributor.authorJong Seog Ahn-
dc.date.accessioned2017-04-19T08:57:24Z-
dc.date.available2017-04-19T08:57:24Z-
dc.date.issued2000-
dc.identifier.issn0378-1097-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/5243-
dc.description.abstractTo 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.publisherOxford Univ Press-
dc.titleMutagenesis of the glucoamylase signal peptide of Saccharomyces diastaticus and functional analysis in Saccharomyces cerevisiae-
dc.title.alternativeMutagenesis of the glucoamylase signal peptide of Saccharomyces diastaticus and functional analysis in Saccharomyces cerevisiae-
dc.typeArticle-
dc.citation.titleFEMS Microbiology Letters-
dc.citation.number1-
dc.citation.endPage11-
dc.citation.startPage7-
dc.citation.volume193-
dc.contributor.affiliatedAuthorJun Won Lee-
dc.contributor.affiliatedAuthorDae Ook Kang-
dc.contributor.affiliatedAuthorBo Yeon Kim-
dc.contributor.affiliatedAuthorWon Keun Oh-
dc.contributor.affiliatedAuthorTae Ick Mheen-
dc.contributor.affiliatedAuthorJong Seog Ahn-
dc.contributor.alternativeName이준원-
dc.contributor.alternativeName강대욱-
dc.contributor.alternativeName김보연-
dc.contributor.alternativeName오원근-
dc.contributor.alternativeName민태익-
dc.contributor.alternativeName변유량-
dc.contributor.alternativeName안종석-
dc.identifier.bibliographicCitationFEMS Microbiology Letters, vol. 193, no. 1, pp. 7-11-
dc.identifier.doi10.1111/j.1574-6968.2000.tb09394.x-
dc.subject.keywordglucoamylase signal peptide-
dc.subject.keywordSaccharomyces diastaticus-
dc.subject.keywordBacillus endo-1,4-β-D-glucanase-
dc.subject.keywordMutagenesis-
dc.subject.keywordSaccharomyces cerevisiae-
dc.subject.keywordsecretion-
dc.subject.localglucoamylase signal peptide-
dc.subject.localSaccharomyces diastaticus-
dc.subject.localBacillus endo-1,4-β-D-glucanase-
dc.subject.localMutagenesis-
dc.subject.localmutagenesis-
dc.subject.localSaccharomyces cerevisiae-
dc.subject.localsaccharomyces cerevisiae-
dc.subject.localsecretion-
dc.subject.localSecretion-
dc.description.journalClassY-
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Ochang Branch Institute > Chemical Biology Research Center > 1. Journal Articles
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