1. Identification of a Terminal Rhamnopyranosyltransferase (RptA) Involved in Corynebacterium glutamicum Cell Wall Biosynthesis
- Author
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Doris Rittmann, Michael R. McNeil, Gurdyal S. Besra, Karin Krumbach, Lothar Eggeling, Helga Etterich, Helen L. Birch, Anna E. Grzegorzewicz, and Luke J. Alderwick
- Subjects
Chromatography, Gas ,Molecular Sequence Data ,Mutant ,Genetics and Molecular Biology ,Biology ,Models, Biological ,Microbiology ,Gas Chromatography-Mass Spectrometry ,Corynebacterium glutamicum ,Bacterial Proteins ,Cell Wall ,Glycosyltransferase ,Transferase ,Amino Acid Sequence ,Molecular Biology ,Integral membrane protein ,Sequence Homology, Amino Acid ,Glycosyltransferases ,Complementation ,Open reading frame ,Transmembrane domain ,Biochemistry ,biology.protein ,bacteria ,Glycolipids ,Genome, Bacterial - 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, r hamno p yranosyl t ransferase 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.
- Published
- 2009
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