The Mycobacterium Tuberculosis FAS-II Dehydratases and Methyltransferases Define the Specificity of the Mycolic Acid Elongation Complexes

Sylvain Cantaloube (1) , Romain Veyron-Churlet (1) , Nabila Haddache (1) , Mamadou Daffe (1) , Didier Zerbib (1)

1 IPBS - Institut de pharmacologie et de biologie structurale

Background: The human pathogen Mycobacterium tuberculosis (Mtb) has the originality of possessing a multifunctional mega-enzyme FAS-I (Fatty Acid Synthase-I), together with a multi-protein FAS-II system, to carry out the biosynthesis of common and of specific long chain fatty acids: the mycolic acids (MA). MA are the main constituents of the external mycomembrane that represents a tight permeability barrier involved in the pathogenicity of Mtb. The MA biosynthesis pathway is essential and contains targets for efficient antibiotics. We have demonstrated previously that proteins of FAS-II interact specifically to form specialized and interconnected complexes. This finding suggested that the organization of FAS-II resemble to the architecture of multifunctional mega-enzyme like the mammalian mFAS-I, which is devoted to the fatty acid biosynthesis.

Domaines: Sciences du Vivant [q-bio]

Sylvain Cantaloube, Romain Veyron-Churlet, Nabila Haddache, Mamadou Daffe, Didier Zerbib. The Mycobacterium Tuberculosis FAS-II Dehydratases and Methyltransferases Define the Specificity of the Mycolic Acid Elongation Complexes. PLoS ONE, 2011, 6 (12), ⟨10.1371/journal.pone.0029564⟩. ⟨hal-01883511⟩