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Title 

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

Authors 

Jun Won LeeDae Ook KangBo Yeon KimWon Keun OhTae Ick MheenYu Ryang PyunJong Seog Ahn

Publisher 

Wiley-Blackwell

Issue Date 

2000

Citation 

FEMS Microbiology Letters, vol. 193, no. 1, pp. 7-11

Keywords 

glucoamylase signal peptideSaccharomyces diastaticusBacillus endo-1,4-β-D-glucanaseMutagenesisSaccharomyces cerevisiaesecretion

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.

ISSN 

0378-1097

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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