Evidence for interactions of acyl carrier protein with glycerol‐3‐phosphate acyltransferase, an inner membrane protein of Escherichia coli

FEBS Letters

Thérisod, Hélène¹  Bayan, Nicolas¹ 

[1] Laboratoire des Biomembranes, UA1116, Université Paris Sud, Bât 433, 91405 Orsay Cedex, France

关键词: Acyl carrier protein;    Plasma membrane;    Glycerol-3-phosphate acyltransferase;    (E. coli);   

DOI  :  10.1016/0014-5793(89)81115-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown