A Dominant Mutation Which Suppresses Deletion Mutations in the Secretory Signal Sequences of Glucoamylase from the Yeast Saccharomyces diastaticus(Biological Chemistry)

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The Saccharomyces diastaticus glucoamylase encoded by STA1 contains two signal sequences for potent secretion of the enzyme, a hydrophobic leader peptide (HL), and a tract consisting of threonine- and serine-rich sequences (TS) ; hybrid proteins of Escherichia colt β-galactosidase carrying both HL and TS are secreted through the cytoplasmic membrane to the cell-surface fraction of yeast cells, but those carrying either HL or TS are not. To investigate the molecular mechanisms for these signal sequences, we have isolated a dominant mutation, SSD1, which suppresses a secretory defect caused by deletion of these sequences. Yeast cells harboring the mutation secreted hybrid β-galactosidase proteins carrying either HL or TS into the cell-surface fraction. Even β-galactosidase itself was secreted to the cell surface in the mutant. These results suggest that HL and TS interact with a wild-type ssd1^+ gene product to promote protein secretion.
社団法人日本農芸化学会の論文
1989-12-23