Laval, F and Haites, R and Movahedzadeh, F and Lemassu, A and Wong, C Y and Stoker, N G and Billman-Jacobe, H and Daffe, M (2008) Investigating the function of the putative mycolic acid methyltransferase UmaA - Divergence between the Mycobacterium smegmatis and Mycobacterium tuberculosis proteins. JOURNAL OF BIOLOGICAL CHEMISTRY, 283 (3). pp. 1419-1427.
Full text not available from this repository.Abstract
Mycolic acids are major and specific lipid components of the cell envelope of mycobacteria that include the causative agents of tuberculosis and leprosy, Mycobacterium tuberculosis and Mycobacterium leprae, respectively. Subtle structural variations that are known to be crucial for both their virulence and the permeability of their cell envelope occur in mycolic acids. Among these are the introduction of cyclopropyl groups and methyl branches by mycolic acid S-adenosylmethionine-dependent methyltransferases (MA-MTs). While the functions of seven of the M. tuberculosis MA-MTs have been either established or strongly presumed nothing is known of the roles of the remaining umaA gene product and those of M. smegmatis MA-MTs. Mutants of the M. tuberculosis umaA gene and its putative M. smegmatis orthologue, MSMEG0913, were created. The lipid extracts of the resulting mutants were analyzed in detail using a combination of analytical techniques such as matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and proton nuclear magnetic resonance spectroscopy, and chemical degradation methods. The M. smegmatis mutants no longer synthesized subtypes of mycolates containing a methyl branch adjacent to either trans cyclopropyl group or trans double bond at the "proximal" position of both alpha- and epoxy-mycolates. Complementation with MSMEG0913, but not with umaA, fully restored the wild-type phenotype in M. smegmatis.
Item Type: | Article |
---|---|
RVC Publication Type: | Research (full) paper |
WoS ID: | 000252282700025 |
DOI: | https://doi.org/10.1074/jbc.M708859200 |
Research Programmes: | Livestock Production and Health > Infection and Immunity |
Depositing User: | RVC Auto-import |
Last Modified: | 21 Nov 2020 15:51 |
URI: | https://researchonline.rvc.ac.uk/id/eprint/1544 |
Actions (Repository Editors)
![]() |
View Item |