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Journal of Bacteriology, August 2009, p. 4879-4887, Vol. 191, No. 15
0021-9193/09/$08.00+0 doi:10.1128/JB.00296-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Luke J. Alderwick,1,
Doris Rittmann,2
Karin Krumbach,2
Helga Etterich,2
Anna Grzegorzewicz,3
Michael R. McNeil,3
Lothar Eggeling,2 and
Gurdyal S. Besra1*
School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom,1 Institute for Biotechnology 1, Research Centre Juelich, D-52425 Juelich, Germany,2 Department of Microbiology, Colorado State University, Fort Collins, Colorado 805233
Received 5 March 2009/ Accepted 21 May 2009
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.
Published ahead of print on 29 May 2009.
These authors contributed equally to the work.
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