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J. Biol. Chem., Vol. 261, Issue 20, 9144-9149, Jul, 1986
TS Tillman and RM Bell
Fourteen independent mutants of Saccharomyces cerevisiae defective in
sn-glycerol-3-phosphate acyltransferase activity were isolated using a
colony autoradiographic screening technique. All 14 mutants were similarly
defective in dihydroxyacetone phosphate acyltransferase activity. The
mutations were recessive and fell into a single complementation group.
Tetrad analysis gave results consistent with mutations in a single nuclear
gene affecting both activities. sn- Glycerol-3-phosphate acyltransferase
activity from different mutant strains exhibited different substrate
dependencies and differing responses to temperature, detergent, and pH. In
each case, the response of the dihydroxyacetone phosphate acyltransferase
activity was similar to that of the sn-glycerol-3-phosphate
acyltransferase. These results are consistent with the mutations occurring
in the structural gene. The data also establish that the predominant
dihydroxyacetone phosphate acyltransferase activity in yeast is a second
activity of the sn- glycerol-3-phosphate acyltransferase.
Mutants of Saccharomyces cerevisiae defective in sn-glycerol-3- phosphate acyltransferase. Simultaneous loss of dihydroxyacetone phosphate acyltransferase indicates a common gene
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