Journal article
Mtrp, a putative methyltransferase in corynebacteria, is required for optimal membrane transport of trehalose mycolates
AK Rainczuk, S Klatt, Y Yamaryo-Botté, R Brammananth, MJ McConville, RL Coppel, PK Crellin
Journal of Biological Chemistry | ELSEVIER | Published : 2020
Abstract
Pathogenic bacteria of the genera Mycobacterium and Corynebacterium cause severe human diseases such as tuberculosis (Mycobacterium tuberculosis) and diphtheria (Corynebacterium diphtheriae). The cells of these species are surrounded by protective cell walls rich in long-chain mycolic acids. These fatty acids are conjugated to the disaccharide trehalose on the cytoplasmic side of the bacterial cell membrane. They are then transported across the membrane to the periplasm where they act as donors for other reactions.Wehave previously shown that transient acetylation of the glycolipid trehalose monohydroxycorynomycolate (hTMCM) enables its efficient transport to the periplasm in Corynebacterium..
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Awarded by Australian Research Council
Funding Acknowledgements
This work was supported by National Health and Medical Research Council of Australia Project Grant 1064466 (to P. K. C., R. L. C., and M. J. M.), Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics Grant COE562063 (to R. L. C.), and Australian Research Council Discovery Grant 180102463 (to R. L. C. and M. J. M.). The authors declare that they have no conflicts of interest with the contents of this article.