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J Biol Chem, Vol. 274, Issue 14, 9677-9685, April 2, 1999

Effect of Cold Shock on Lipid A Biosynthesis in Escherichia coli
INDUCTION AT 12 °C OF AN ACYLTRANSFERASE SPECIFIC FOR PALMITOLEOYL-ACYL CARRIER PROTEIN

Sherry M. Carty, Kodangattil R. Sreekumar^¶, and Christian R. H. Raetz

From the  Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710 and the ^¶ Department of Molecular Biology and Microbiology, Tufts University Health Sciences Campus, Boston, Massachusetts 02111

Palmitoleate is not present in lipid A isolated from Escherichia coli grown at 30 °C or higher, but it comprises ~11% of the fatty acyl chains of lipid A in cells grown at 12 °C. The appearance of palmitoleate at 12 °C is accompanied by a decline in laurate from ~18% to ~5.5%. We now report that wild-type E. coli shifted from 30 °C to 12 °C acquire a novel palmitoleoyl-acyl carrier protein (ACP)-dependent acyltransferase that acts on the key lipid A precursor Kdo₂-lipid IV_A. The palmitoleoyl transferase is induced more than 30-fold upon cold shock, as judged by assaying extracts of cells shifted to 12 °C. The induced activity is maximal after 2 h of cold shock, and then gradually declines but does not disappear. Strains harboring an insertion mutation in the lpxL(htrB) gene, which encodes the enzyme that normally transfers laurate from lauroyl-ACP to Kdo₂-lipid IV_A (Clementz, T., Bednarski, J. J., and Raetz, C. R. H. (1996) J. Biol. Chem. 271, 12095-12102) are not defective in the cold-induced palmitoleoyl transferase. Recently, a gene displaying 54% identity and 73% similarity at the protein level to lpxL was found in the genome of E. coli. This lpxL homologue, designated lpxP, encodes the cold shock-induced palmitoleoyl transferase. Extracts of cells containing lpxP on the multicopy plasmid pSK57 exhibit a 10-fold increase in the specific activity of the cold-induced palmitoleoyl transferase compared with cells lacking the plasmid. The elevated specific activity of the palmitoleoyl transferase under conditions of cold shock is attributed to greatly increased levels of lpxP mRNA. The replacement of laurate with palmitoleate in lipid A may reflect the desirability of maintaining the optimal outer membrane fluidity at 12 °C.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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