Evidence for interactions of acyl carrier protein with glycerol-3-phosphate acyltransferase, an inner membrane protein of Escherichia coli.
We [(1989) FEBS Lett., in press] have previously shown that membrane vesicles from Escherichia coli contain protein-binding sites for the acyl carrier protein (ACP). We report now that membrane vesicles prepared from a strain amplified for glycerol-3-phosphate acyltransferase (GPAT) contain a higher number of ACP-binding sites than the membrane vesicles prepared from a wild type strain. In addition, we show that GPAT is retained specifically on an ACP-Sepharose affinity column and that [3H]ACP binds to the enzyme solubilized by detergent. We conclude that GPAT, an inner membrane protein which catalyses the transesterification of a fatty acyl group from acyl coenzyme A or acyl ACP to glycerol-3-phosphate, possesses a binding site for ACP.
Bayan
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Laboratoire des Biomembranes, UA1116, Université Paris Sud, Orsay, France.
Thérisod
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D000213:Acyl Carrier Protein / Q000378:metabolism*; D000217:Acyltransferases / Q000378:metabolism*; D001665:Binding Sites; D002462:Cell Membrane / Q000201:enzymology; D002846:Chromatography, Affinity; D004926:Escherichia coli / Q000201:enzymology*; D005992:Glycerol-3-Phosphate O-Acyltransferase / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D011485:Protein Binding
D000213:Acyl Carrier Protein; D000217:Acyltransferases; D005992:Glycerol-3-Phosphate O-Acyltransferase