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Identification of a terminal rhamnopyranosyltransferase (RptA) involved in Corynebacterium glutamicum cell wall biosynthesis.

Journal of bacteriology (2009-06-02)
Helen L Birch, Luke J Alderwick, Doris Rittmann, Karin Krumbach, Helga Etterich, Anna Grzegorzewicz, Michael R McNeil, Lothar Eggeling, Gurdyal S Besra
ABSTRACT

A bioinformatics approach identified a putative integral membrane protein, NCgl0543, in Corynebacterium glutamicum, with 13 predicted transmembrane domains and a glycosyltransferase motif (RXXDE), features that are common to the glycosyltransferase C superfamily of glycosyltransferases. The deletion of C. glutamicum NCgl0543 resulted in a viable mutant. Further glycosyl linkage analyses of the mycolyl-arabinogalactan-peptidoglycan complex revealed a reduction of terminal rhamnopyranosyl-linked residues and, as a result, a corresponding loss of branched 2,5-linked arabinofuranosyl residues, which was fully restored upon the complementation of the deletion mutant by NCgl0543. As a result, we have now termed this previously uncharacterized open reading frame, rhamnopyranosyltransferase A (rptA). Furthermore, an analysis of base-stable extractable lipids from C. glutamicum revealed the presence of decaprenyl-monophosphorylrhamnose, a putative substrate for the cognate cell wall transferase.

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Sigma-Aldrich
IGEPAL® CA-630, viscous liquid
Sigma-Aldrich
IGEPAL® CA-630, for molecular biology
Supelco
IGEPAL® CA-630