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Journal of Bacteriology, October 2000, p. 5620-5623, Vol. 182, No. 19
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Mutation of the Lipopolysaccharide Core Glycosyltransferase Encoded by waaG Destabilizes the Outer Membrane of Escherichia coli by Interfering with Core Phosphorylation

Jeremy A. Yethon,1 Evgeny Vinogradov,2 Malcolm B. Perry,2 and Chris Whitfield1,*

Canadian Bacterial Diseases Network and Department of Microbiology, University of Guelph, Guelph, Ontario N1G 2W1,1 and Canadian Bacterial Diseases Network and Institute for Biological Sciences, National Research Council, Ottawa, Ontario K1A 0R6,2 Canada

Received 27 March 2000/Accepted 17 July 2000

In Escherichia coli, phosphoryl substituents in the lipopolysaccharide core region are essential for outer membrane stability. Mutation of the core glucosyltransferase encoded by waaG (formerly rfaG) resulted in lipopolysaccharide truncated immediately after the inner core heptose residues, which serve as the sites for phosphorylation. Surprisingly, mutation of waaG also destabilized the outer membrane. Structural analyses of waaG mutant lipopolysaccharide showed that the cause for this phenotype was a decrease in core phosphorylation, an unexpected side effect of the waaG mutation.

* Corresponding author. Mailing address: Department of Microbiology, College of Biological Science, University of Guelph, Guelph, Ontario N1G 2W1, Canada. Phone: (519) 824-4120, ext. 3478. Fax: (519) 837-1802. E-mail: cwhitfie{at}uoguelph.ca.

Journal of Bacteriology, October 2000, p. 5620-5623, Vol. 182, No. 19
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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