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J. Biol. Chem., Vol. 280, Issue 10, 9236-9242, March 11, 2005

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Two Proteins Homologous to the N- and C-terminal Domains of the Bacterial Glycosyltransferase Murg Are Required for the Second Step of Dolichyl-linked Oligosaccharide Synthesis in Saccharomyces cerevisiae^*

Isabelle Chantret, Julia Dancourt, Alain Barbat, and Stuart E. H. Moore

From the Institut National de la Santé et de la Recherche Médicale, U504, Bâtiment INSERM, 16 avenue Paul Vaillant-Couturier, 94807 Villejuif, France

Two highly conserved eukaryotic gene products of unknown function showing homology to glycosyltransferases involved in the second steps of bacterial peptidoglycan (Murg) and capsular polysaccharide (Cps14f/Cps14g) biosynthesis have been identified in silico. The amino acid sequence of the eukaryotic protein that is homologous to the lipid acceptor- and membrane-associating N-terminal domain of Murg and the Cps14f 4-galactosyltransferase enhancer protein is predicted to possess a cleavable signal peptide and transmembrane helices. The other eukaryotic protein is predicted to possess neither transmembrane regions nor a signal peptide but is homologous to the UDP-sugar binding C-terminal domain of Murg and the Cps14g 4-galactosyltransferase. Both the eukaryotic proteins are encoded by essential genes in Saccharomyces cerevisiae, and down-regulation of either causes growth retardation, reduced N-glycosylation of carboxypeptidase Y, and accumulation of dolichyl-PP-GlcNAc. In vitro studies demonstrate that these proteins are required for transfer of [³H]GlcNAc from UDP-[³H]GlcNAc onto dolichyl-PP-GlcNAc. To conclude, two gene products showing homology to bacterial glycosyltransferases are required for the second step in dolichyl-PP-oligosaccharide biosynthesis.

Received for publication, December 10, 2004

Note Added in Proof—On the basis of the results presented in this article we suggest that the S. cerevisiae genes, YGL047w and YBR070c, be called ALG13 and ALG14, respectively.

^* This work was supported by the Mizutani Foundation, the GIS-Institut des maladies rares/INSERM funded French Congenital Disorders of Glycosylation Research Network, and by institutional funding from INSERM. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

These authors contributed equally to this work.

To whom correspondence should be addressed: INSERM U504, 16 avenue Paul Vaillant-Couturier, 94807 Villejuif CEDEX, France. Tel.: 33-1-45-59-50-47; Fax: 33-1-46-77-02-33; E-mail: moore{at}vjf.inserm.fr.

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