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Papers In Press, published online ahead of print June 19, 2000
School of Biological Sciences, University of Manchester, Manchester M13 9PT
Corresponding Author: isrobert{at}fs1.scg.man.ac.uk
The Escherichia coli K5 capsular polysaccharide consists of the repeat structure -4)GlcA-
J. Biol. Chem, 10.1074/jbc.M004426200
Submitted on May 23, 2000
Revised on June 8, 2000
Accepted on June 19, 2000
Identification that KfiA, a Protein Essential for the Biosynthesis of the Escherichia coli K5 Capsular Polysaccharide, is an
-UDP-GlcNAc Glycosyltransferase: The Formation of a Membrane Associated K5 Biosynthetic Complex Requires KfiA, KfiB and KfiC
(1,4)-GlcNAc-
(1- and requires the KfiA, KfiB, KfiC and KfiD proteins for its synthesis. Previously the KfiC protein was shown to be a -UDP-GlcA glycosyltransferase and KfiD to be a UDP-Glc dehydrogenase. Here we demonstrate that KfiA is an -UDP-GlcNAc glycosyltransferase and that biosynthesis of the K5 polysaccharide involves the concerted action of the KfiA and KfiC proteins. By site-directed mutagenesis we identify that the acidic motif of DDD, that is conserved between the C family of glycosyltransferases, is essential for the enzymatic activity of KfiA. In addition, by Western blot analysis we demonstrate that association of KfiA with the cytoplasmic membrane requires KfiC but not KfiB, whilst the interaction of KfiC with the cytoplasmic membrane was dependent on both KfiA and KfiB. Likewise KfiB was only detectable in cytoplasmic membrane fractions when both KfiA and KfiC were present. These data suggest that the interaction between the KfiA, KfiB and KfiC proteins is essential for the stable association of these proteins with the cytoplasmic membrane and the biosynthesis of the K5 polysaccharide.
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