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Identification of mdoD, an mdoG Paralog Which Encodes a Twin-Arginine-Dependent Periplasmic Protein That Controls Osmoregulated Periplasmic Glucan Backbone Structures

Yannick Lequette, Carmen Ödberg-Ferragut, Jean-Pierre Bohin,^* and Jean-Marie Lacroix

Unité de Glycobiologie Structurale et Fonctionnelle, UMR USTL-CNRS 8576, IFR118, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq Cedex, France

Received 23 February 2004/ Accepted 16 March 2004

Osmoregulated periplasmic glucans (OPGs) of Escherichia coli are anionic and highly branched oligosaccharides that accumulate in the periplasmic space in response to low osmolarity of the medium. The glucan length, ranging from 5 to 12 glucose residues, is under strict control. Two genes that form an operon, mdoGH, govern glucose backbone synthesis. The new gene mdoD, which appears to be a paralog of mdoG, was characterized in this study. Cassette inactivation of mdoD resulted in production of OPGs with a higher degree of polymerization, indicating that OpgD, the mdoD product (according to the new nomenclature), controls the glucose backbone structures. OpgD secretion depends on the Tat secretory pathway. Orthologs of the mdoG and mdoD genes are found in various proteobacteria. Most of the OpgD orthologs exhibit a Tat-dependent secretion signal, while most of the OpgG orthologs are Sec dependent.

Y.L. and C.Ö.-F. contributed equally to this work.

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