Identification of a Terminal Rhamnopyranosyltransferase (RptA) Involved in Corynebacterium glutamicum Cell Wall Biosynthesis

Author:

Birch Helen L.1,Alderwick Luke J.1,Rittmann Doris2,Krumbach Karin2,Etterich Helga2,Grzegorzewicz Anna3,McNeil Michael R.3,Eggeling Lothar2,Besra Gurdyal S.1

Affiliation:

1. School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom

2. Institute for Biotechnology 1, Research Centre Juelich, D-52425 Juelich, Germany

3. Department of Microbiology, Colorado State University, Fort Collins, Colorado 80523

Abstract

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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference43 articles.

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