Galactosyl Transferases in Mycobacterial Cell Wall Synthesis

Author:

Beláňová Martina1,Dianišková Petronela1,Brennan Patrick J.2,Completo Gladys C.3,Rose Natisha L.3,Lowary Todd L.3,Mikušová Katarína1

Affiliation:

1. Department of Biochemistry, Comenius University, Faculty of Natural Sciences, Bratislava, Slovakia SK-842 15

2. Mycobacterial Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, Colorado 80523

3. Alberta Ingenuity Centre for Carbohydrate Science and Department of Chemistry, The University of Alberta, Edmonton, Alberta, Canada T6G 2G2

Abstract

ABSTRACT Two galactosyl transferases can apparently account for the full biosynthesis of the cell wall galactan of mycobacteria. Evidence is presented based on enzymatic incubations with purified natural and synthetic galactofuranose (Gal f ) acceptors that the recombinant galactofuranosyl transferase, GlfT1, from Mycobacterium smegmatis , the Mycobacterium tuberculosis Rv3782 ortholog known to be involved in the initial steps of galactan formation, harbors dual β-(1→4) and β-(1→5) Gal f transferase activities and that the product of the enzyme, decaprenyl-P-P-GlcNAc-Rha-Gal f -Gal f , serves as a direct substrate for full polymerization catalyzed by another bifunctional Gal f transferase, GlfT2, the Rv3808c enzyme.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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