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Journal of Bacteriology, June 1999, p. 3626-3631, Vol. 181, No. 12
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The mdoC Gene of Escherichia coli Encodes a Membrane Protein That Is Required for Succinylation of Osmoregulated Periplasmic Glucans

Jean-Marie Lacroix, Eric Lanfroy, Virginie Cogez, Yannick Lequette, Anne Bohin, and Jean-Pierre Bohin*

Laboratoire de Chimie Biologique, UMR111 du CNRS, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq, Cedex, France

Received 24 February 1999/Accepted 19 April 1999

Osmoregulated periplasmic glucans (OPGs) of Escherichia coli are anionic oligosaccharides that accumulate in the periplasmic space in response to low osmolarity of the medium. Their anionic character is provided by the substitution of the glucosidic backbone by phosphoglycerol originating from the membrane phospholipids and by succinyl residues from unknown origin. A phosphoglycerol-transferase-deficient mdoB mutant was subjected to Tn5 transposon mutagenesis, and putative mutant clones were screened for changes in the anionic character of OPGs by thin-layer chromatography. One mutant deficient in succinylation of OPGs was obtained, and the gene inactivated in this mutant was characterized and named mdoC. mdoC, which encodes a membrane-bound protein, is closely linked to the mdoGH operon necessary for the synthesis of the OPG backbone.

* Corresponding author. Mailing address: U.S.T.L., Bât. C9, 59655 Villeneuve d'Ascq Cedex, France. Phone: 33 (0)3 20 43 65 92. Fax: 33 (0)3 20 43 65 55. E-mail: Jean-Pierre.Bohin{at}univ-lille1.fr.

Journal of Bacteriology, June 1999, p. 3626-3631, Vol. 181, No. 12
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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