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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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.
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PMID: 33610760 PMC: 7613133. DOI: 10.1016/j.bbalip.2021.158907.
A review of phosphatidate phosphatase assays.
Dey P, Han G, Carman G J Lipid Res. 2020; 61(12):1556-1564.
PMID: 32963036 PMC: 7707177. DOI: 10.1194/jlr.R120001092.
Hirasawa T, Ida Y, Furuasawa C, Shimizu H Bioengineered. 2013; 5(2):123-8.
PMID: 24247205 PMC: 4049903. DOI: 10.4161/bioe.26569.
Moon H, Chowrira G, Rowland O, Blacklock B, Smith M, Kunst L Plant Mol Biol. 2005; 56(6):917-27.
PMID: 15821990 DOI: 10.1007/s11103-004-6235-z.
Athenstaedt K, Weys S, Paltauf F, Daum G J Bacteriol. 1999; 181(5):1458-63.
PMID: 10049376 PMC: 93534. DOI: 10.1128/JB.181.5.1458-1463.1999.