Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8940004 | The Cell Surface | 2018 | 41 Pages |
Abstract
Arabinogalactan (AG) is an essential structural macromolecule present in the cell wall of Mycobacterium tuberculosis, serving to connect peptidoglycan with the outer mycolic acid layer. The D-arabinan segment is a highly branched component of AG and is assembled in a step-wise fashion by a variety of arabinofuranosyltransferases (AraT). We have previously used Corynebacterium glutamicum as a model organism to study these complex processes which are otherwise essential in mycobacteria. In order to further our understanding of the molecular basis of AG assembly, we investigated the role of a fourth AraT, now termed AftD by generating single (ÎaftD) and double deletion (ÎaftB ÎaftD) mutants of C. glutamicum. We demonstrate that AftD functions as an α(1â¯ââ¯5) AraT and reveal the point at which it exerts its activity in the AG biosynthetic pathway.
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Applied Microbiology and Biotechnology
Authors
Luke J. Alderwick, Helen L. Birch, Karin Krumbach, Michael Bott, Lothar Eggeling, Gurdyal S. Besra,