Dmochowska A, et al. (1987) (original) (raw)
Reference: Dmochowska A, et al. (1987)
Abstract
The yeast KEX1 gene product has homology to yeast carboxypeptidase Y. A mutant replacing serine at the putative active site of the KEX1 protein abolished activity in vivo. A probable site of processing by the KEX1 product is the C-terminus of the alpha-subunit of killer toxin, where toxin is followed in the precursor by 2 basic residues. Processing involves endoproteolysis following these basic residues and trimming of their C-terminal by a carboxypeptidase. Consistent with the KEX1 product being this carboxypeptidase is its role in alpha-factor pheromone production. In wild-type yeast, KEX1 is not essential for alpha-factor production, as the final pheromone repeat needs no C-terminal processing. However, in a mutant in which alpha-factor production requires a carboxypeptidase, pheromone production is KEX1-dependent.
PMID: 3301004
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Reference Type
Comparative Study | Journal Article | Research Support, Non-U.S. Gov't
Authors
Dmochowska A, Dignard D, Henning D, Thomas DY, Bussey H
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