| Literature DB >> 19482925 |
Helen L Birch1, 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.Entities:
Mesh:
Substances:
Year: 2009 PMID: 19482925 PMCID: PMC2715713 DOI: 10.1128/JB.00296-09
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490