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The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes.

1992; Elsevier BV; Volume: 267; Issue: 9 Linguagem: Inglês

10.1016/s0021-9258(18)42616-6

1083-351X

Merriann Rawlings, John E. Cronan,

Microbial Metabolic Engineering and Bioproduction

The gene encoding Escherichia coli acyl carrier protein (ACP) has been isolated and sequenced.The ACP gene (called acpP) was located on the genetic map between fabF and fabD which encode two fatty acid biosynthetic enzymes, 3-ketoacyl-ACP synthase I1 and malonyl CoA-ACP transacylase, respectively.An open reading frame between acpP and fabD encodes a 26.5-kDa protein that has significant sequence identity (>40%) with two acetoacetyl-CoA reductases and thus is believed to encode a 3-ketoacyl-ACP reductase.This gene (called fa") is cotranscribed with acpP.Thus, the gene encoding ACP, the key carrier protein of fatty acid synthesis, is located within a cluster of fatty acid biosynthetic genes.Acyl carrier protein (ACP)' plays a key role in lipid biosynthesis in bacteria (1) and plants (2).ACP carries the nascent fatty acid chain esterified to the thiol group of the 4"phosphopantetheine prosthetic group and delivers the finished acyl chain to the acyltransferases catalyzing complex lipid synthesis (phospholipids and lipid A) (1, 2).Acyl-ACP has also been reported as an acyl donor in protein acylation (3).Escherichia coli ACP and its acyl forms thus interact with at least 12 different E. coli enzymes.The ACPs of other bacteria and plants are very similar to that of E. coli; all are small ((90 residues) acidic proteins modified with 4-phosphopantetheine with strong similarities of the sequences neighboring the modification site (1, 2).Indeed, several of these proteins are known to function with various of the ACP-dependent enzymes of E. coli in vitro (2) and in vivo (2, 4) suggesting similar solution structures.The large polyfunctional proteins that catalyze fatty acid synthesis in mammals (5) and fungi (6) contain 4'-phosphopantetheine-modified domains with strong sequence similarity to E. coli ACP.ACP-like proteins also function as acyl group carriers in the biosynthesis of polyketide (7) and polyamino acid antibiotics (8).