This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Belánová, M.
Right arrow Articles by Mikusová, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Belánová, M.
Right arrow Articles by Mikusová, K.

 Previous Article  |  Next Article 

Journal of Bacteriology, February 2008, p. 1141-1145, Vol. 190, No. 3
0021-9193/08/$08.00+0     doi:10.1128/JB.01326-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Galactosyl Transferases in Mycobacterial Cell Wall Synthesis{triangledown}

Martina Belánová,1 Petronela Dianisková,1 Patrick J. Brennan,2* Gladys C. Completo,3 Natisha L. Rose,3 Todd L. Lowary,3 and Katarína Mikusová1*

Department of Biochemistry, Comenius University, Faculty of Natural Sciences, Bratislava, Slovakia SK-842 15,1 Mycobacterial Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, Colorado 80523,2 Alberta Ingenuity Centre for Carbohydrate Science and Department of Chemistry, The University of Alberta, Edmonton, Alberta, Canada T6G 2G23

Received 15 August 2007/ Accepted 17 November 2007

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 (Galf) 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) Galf transferase activities and that the product of the enzyme, decaprenyl-P-P-GlcNAc-Rha-Galf-Galf, serves as a direct substrate for full polymerization catalyzed by another bifunctional Galf transferase, GlfT2, the Rv3808c enzyme.


* Corresponding author. Mailing address for K. Mikusová: Department of Biochemistry, Comenius University, Faculty of Natural Sciences, Bratislava, Slovakia SK-842 15. Phone: 00421 (2) 60296 547. Fax: 00421 (2) 60296 452. E-mail: mikusova{at}fns.uniba.sk. Mailing address for P. J. Brennan: Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523. Phone: (970) 491 6700. Fax: (970) 491 1815. E-mail: patrick.brennan{at}colostate.edu

{triangledown} Published ahead of print on 30 November 2007.


Journal of Bacteriology, February 2008, p. 1141-1145, Vol. 190, No. 3
0021-9193/08/$08.00+0     doi:10.1128/JB.01326-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.