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(Received for publication, January 21, 1997)
From the Department of Biochemistry, Duke University Medical
Center, Durham, North Carolina 27710
Overexpression of the Escherichia coli
msbB gene on high copy plasmids suppresses the
temperature-sensitive growth associated with mutations in the
htrB gene. htrB encodes the lauroyl transferase of lipid A biosynthesis that acylates the intermediate
(Kdo)2-lipid IVA (Brozek, K. A., and Raetz, C. R. H. (1990) J. Biol. Chem. 265, 15410-15417). Since
msbB displays 27.5% identity and 42.2% similarity to
htrB, we explored the possibility that msbB
encodes a related acyltransferase. In contrast to htrB,
extracts of strains with insertion mutations in msbB are
not defective in transferring laurate from lauroyl acyl carrier protein
to (Kdo)2-lipid IVA. However, extracts of
msbB mutants do not efficiently acylate the product formed
by HtrB, designated (Kdo)2-(lauroyl)-lipid IVA. Extracts of strains harboring msbB+ bearing
plasmids acylate (Kdo)2-(lauroyl)-lipid IVA
very rapidly compared with wild type. We solubilized and partially
purified MsbB from an overproducing strain, lacking HtrB. MsbB
transfers myristate or laurate, activated on ACP, to
(Kdo)2-(lauroyl)-lipid IVA. Decanoyl,
palmitoyl, palmitoleoyl, and (R)-3-hydroxymyristoyl-ACP are
poor acyl donors. MsbB acylates (Kdo)2-(lauroyl)-lipid
IVA about 100 times faster than (Kdo)2-lipid
IVA. The slow, but measurable, rate whereby MsbB acts on
(Kdo)2-lipid IVA may explain why overexpression of MsbB suppresses the temperature-sensitive phenotype of
htrB mutations. Presumably, the acyloxyacyl group generated
by excess MsbB substitutes for the one normally formed by HtrB.
Volume 272, Number 16,
Issue of April 18, 1997
pp. 10353-10360
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
ACYLATION BY MsbB FOLLOWS LAURATE INCORPORATION BY
HtrB
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