This title appears in the Scientific Report :
2009
Please use the identifier:
http://dx.doi.org/10.1128/JB.00296-09 in citations.
Identification of a terminal rhamnopyranosyltransferase (RptA) involved in Corynebacterium glutamicum cell wall biosynthesis
Identification of a terminal rhamnopyranosyltransferase (RptA) involved in Corynebacterium glutamicum cell wall biosynthesis
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...
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Personal Name(s): | Birch, H. L. |
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Alderwick, L. J. / Rittmann, D. / Krumbach, K. / Etterich, H. / Grzegorzewicz, A. / McNeil, M. R. / Eggeling, L. / Besra, G. S. | |
Contributing Institute: |
Biotechnologie 1; IBT-1 |
Published in: | Journal of bacteriology, 191 (2009) S. 4879 - 4887 |
Imprint: |
Washington, DC
Soc.
2009
|
Physical Description: |
4879 - 4887 |
PubMed ID: |
19482925 |
DOI: |
10.1128/JB.00296-09 |
Document Type: |
Journal Article |
Research Program: |
Biotechnologie |
Series Title: |
Journal of Bacteriology
191 |
Subject (ZB): | |
Publikationsportal JuSER |
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. |