Abstract
A mutant of yeast sensitive to growth inhibition by 2,6-diaminopurine (2,6-DAP) was analyzed genetically and found to be a double mutant. One gene, dap, conferred approximately 30% sensitivity to the analogue. The other, slw, potentiated the inhibition such that the double mutant dap slw was inhibited 90%. The mutation dap conferred concomitant sensitivity to a number of other purine analogues. The activity of a purine phosphoribosyltransferase with 2,6-DAP in a strain carrying dap was found to be three times higher than in the wild type. It is inferred that the mutation alters the properties of a purine phosphoribosyltransferase. A possible mechanism for the effect of slw is also discussed.
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Selected References
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