PMID:1649829

Citation	Hsu, L, Jackowski, S and Rock, CO (1991) Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity.J. Biol. Chem. 266:13783-8
Abstract	2-Acyl-glycerophosphoethanolamine (2-acyl-GPE) acyltransferase and acyl-acyl carrier protein (acyl-ACP) synthetase are thought to be dual catalytic activities of a single inner membrane enzyme. A filter disc replica print method for the detection of acyl-ACP synthetase activity by colony fluorography was used to screen a mutagenized population of cells for acyl-ACP synthetase mutants (aas). All aas mutants lacked both acyl-ACP synthetase and 2-acyl-GPE acyltransferase activities in vitro. There was no detectable acyl-CoA-independent incorporation of exogenous fatty acids into phosphatidylethanolamine or the major outer membrane lipoprotein in aas mutants. Exogenous lysophospholipid uptake and acylation was also lacking in aas mutants. Lipoprotein acylation by phospholipids synthesized by the de novo biosynthetic pathway was not affected in aas mutants showing that this gene product was not directly involved in lipoprotein biogenesis. The aas mutants had an altered membrane phospholipid composition and accumulated both 2-acyl-GPE and acylphosphatidylglycerol. Acylphosphatidylglycerol accumulation was due to the transacylase activity of lysophospholipase L2 (the pldB gene product) since aas pldB double mutants accumulated 2-acyl-GPE, but not acylphosphatidylglycerol. The aas allele was mapped to 61 min of the Escherichia coli chromosome, and the deduced gene order in this region was thyA-aas-lysA. The biochemical, physiological, and genetic analyses of aas mutants support the conclusion that 2-acyl-GPE acyltransferase and acyl-ACP synthetase are two activities of the same protein and confirm that this enzyme system participates in membrane phospholipid turnover and governs the acyl-CoA independent incorporation of exogenous fatty acids and lysophospholipids into the membrane.
Links	PubMed
Keywords	Acylation; Acyltransferases; Chromosome Mapping; Coenzyme A Ligases; Escherichia coli; Fatty Acids; Genes, Bacterial; Lysophospholipids; Membrane Lipids; Multienzyme Complexes; Mutation; Phosphatidylethanolamines; Phosphotransferases; Proteins; Transferases (Other Substituted Phosphate Groups)
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Materials and Methods Used

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Phenotype Annotations

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Species	Taxon ID	Strain	Gene (if known)	OMP	Phenotype	Details	Evidence	Notes
Escherichia coli		LCH1	aas-1	abolished acyl-ACP synthetase activity
Escherichia coli		LCH2	aas-2	abolished acyl-ACP synthetase activity
Escherichia coli		LCH1	aas-1	abolished acyltransferase activity	Metabolic Activity		Biochemical Assay	Table 2
Escherichia coli		LCH1	aas-1	altered composition of phospholipid membrane increased lysophosphatidylethanolamine content in membrane	Metabolic Activity		Biochemical Assay
Escherichia coli		LCH1	aas-1	altered composition of phospholipid membrane increased accumulation of Acyl-PtdGro			Biochemical Assay
Escherichia coli		LK29	pld12	altered membrane composition absent acyl-PtdGro in membranes			Biochemical Assay
Escherichia coli			fadD	absent acyl-CoA synthetase activity			Biochemical Assay
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References

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