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- W2091731888 abstract "Saccharomycescerevisiae harboring linear dsDNA plasmids, pGKL1 and pGKL2, secretes a killer toxin consisting of 97, 31 and 28 kilodalton subunits (Nucleic Acids Res., 15, 1031–1046, 1987). We isolated the DNA encoding the N-terminal pre-sequence of the 28K precursor protein and constructed a new secretion vector in S. cerevisiae. Mouse α-amylase fused to the 28K signal sequence was secreted into the culture medium with a high efficiency similar to those fused to the mating factor α and 97K–31K killer signal sequences. This data clearly indicates that 28K pre-sequence functions as a secretion signal. Glycosylated and non-glycosylated α-amylase molecules were detected in the culture medium. The secretion of α-amylase was blocked by sec18–1 mutation. The secreted α-amylase recovered from the medium was found to migrate faster in SDS-polyacrylamide gel than the precursor form of α-amylase synthesized invitro. These lines of evidence suggest that mouse α-amylase fused to 28K killer signal sequence was processed, glycosylated and secreted through the normal secretion pathway of the yeast." @default.
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- W2091731888 date "1988-01-01" @default.
- W2091731888 modified "2023-09-25" @default.
- W2091731888 title "A novel yeast secretion signal isolated from 28K killer precursor protein encoded on the linear DNA plasmid pGKL1" @default.
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- W2091731888 doi "https://doi.org/10.1093/nar/16.15.7499" @default.
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