Skip Navigation



Glycobiology Advance Access published online on August 4, 2006
Glycobiology, doi:10.1093/glycob/cwl030
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow All Versions of this Article:
16/11/1073    most recent
cwl030v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Alderwick, L. J.
Right arrow Articles by Besra, G. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Alderwick, L. J.
Right arrow Articles by Besra, G. S.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received June 8, 2006
Revised July 26, 2006
Accepted July 26, 2006

Article

Arabinan deficient mutants of Corynebacterium glutamicum and the consequent flux in decaprenylmonophosphoryl-D-arabinose metabolism

Luke J. Alderwick 1, Lynn G. Dover 1, Mathias Seidel 2, Roland Gande 2, Hermann Sahm 2, Lothar Eggeling 2, and Gurdyal S. Besra 1 *

1 School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK
2 Institute for Biotechnologie 1, Research Centre Juelich, D-52425 Juelich, Germany

* To whom correspondence should be addressed.
Gurdyal S. Besra, E-mail: g.besra{at}bham.ac.uk


  Abstract

The arabinogalactan (AG) of Corynebacterianeae is a critical macromolecule that tethers mycolic acids to peptidoglycan, thus forming a highly impermeable cell wall matrix termed the mycolyl-arabinogalactan peptidoglycan complex (mAGP). The front line anti-tuberculosis drug, ethambutol, targets the Mycobacterium tuberculosis and Corynebacterium glutamicum arabinofuranosyltransferase Mt-EmbA, Mt-EmbB and Cg-Emb enzymes respectively, which are responsible for the biosynthesis of the arabinan domain of AG. The substrate utilised by these important glycosyltransferases, decaprenylmonophosphoryl-D-arabinose (DPA), is synthesised via a decaprenylphosphoryl-5-phosphoribose (DPPR) synthase (UbiA), which catalyses the transfer of phosphoribiose diphosphate (pRpp) to decaprenol phosphate to form DPPR. Glycosyl compositional analysis of cell walls extracted from a Corynebacterium glutamicum::ubiA mutant revealed a galactan core consisting of alternating {beta}(1->5)-Galf and {beta}(1->6)-Galf residues, completely devoid of arabinan and a concomitant loss of cell wall bound mycolic acids. In addition, in vitro assays demonstrated a complete loss of arabinofuranosyltransferase activity and DPA biosynthesis in the C. glutamicum::ubiA mutant when supplemented with p[14C]Rpp, the precursor of DPA. Interestingly, in vitro arabinofuranosyltransferase activity was restored in the C. glutamicum::ubiA mutant when supplemented with exogenous DP[1414]A substrate and C. glutamicum strains deficient in ubiA, emb and aftA all exhibited different levels of DPA biosynthesis.

Keywords: decaprenylmonophosphoryl-D-arabinose/Mycobacterium tuberculosis/Corynebacterium glutamicum/mutants/arabinogalactan.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Bacteriol.Home page
H. L. Birch, L. J. Alderwick, D. Rittmann, K. Krumbach, H. Etterich, A. Grzegorzewicz, M. R. McNeil, L. Eggeling, and G. S. Besra
Identification of a Terminal Rhamnopyranosyltransferase (RptA) Involved in Corynebacterium glutamicum Cell Wall Biosynthesis
J. Bacteriol., August 1, 2009; 191(15): 4879 - 4887.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
X. Meniche, C. de Sousa-d'Auria, B. Van-der-Rest, S. Bhamidi, E. Huc, H. Huang, D. De Paepe, M. Tropis, M. McNeil, M. Daffe, et al.
Partial redundancy in the synthesis of the D-arabinose incorporated in the cell wall arabinan of Corynebacterineae
Microbiology, August 1, 2008; 154(8): 2315 - 2326.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
R. V. V. Tatituri, L. J. Alderwick, A. K. Mishra, J. Nigou, M. Gilleron, K. Krumbach, P. Hitchen, A. Giordano, H. R. Morris, A. Dell, et al.
Structural characterization of a partially arabinosylated lipoarabinomannan variant isolated from a Corynebacterium glutamicum ubiA mutant
Microbiology, August 1, 2007; 153(8): 2621 - 2629.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Seidel, L. J. Alderwick, H. L. Birch, H. Sahm, L. Eggeling, and G. S. Besra
Identification of a Novel Arabinofuranosyltransferase AftB Involved in a Terminal Step of Cell Wall Arabinan Biosynthesis in Corynebacterianeae, such as Corynebacterium glutamicum and Mycobacterium tuberculosis
J. Biol. Chem., May 18, 2007; 282(20): 14729 - 14740.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
M. Seidel, L. J. Alderwick, H. Sahm, G. S. Besra, and L. Eggeling
Topology and mutational analysis of the single Emb arabinofuranosyltransferase of Corynebacterium glutamicum as a model of Emb proteins of Mycobacterium tuberculosis
Glycobiology, February 1, 2007; 17(2): 210 - 219.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.