Physiological Function of Mycobacterial mtFabD, an Essential Malonyl-CoA : AcpM Transacylase of Type 2 Fatty Acid Synthase FASII, in Yeast mct1Δ Cells

Abstract EN

Mycobacterium tuberculosis mtFabD is an essential malonyl-CoA:AcpM transacylase and is important for vital protein-protein interactions within type 2 fatty acid synthase FASII.

mtFabD contacts KasA, KasB, FabH, InhA, and possibly also HadAB, HadBC, and FabG1/MabA.

Disruption of mtFabD's interactions during FASII has been proposed for drug development.

Here, the gene for a mitochondrially targeted mtFabD was ectopically expressed in Saccharomyces cerevisiae mct1Δ mutant cells lacking the corresponding mitochondrial malonyl-CoA transferase Mct1p, allowing the mutants to recover their abilities to respire on glycerol and synthesize lipoic acid.

Hence, mtFabD could physiologically function in an environment lacking holo-AcpM or other native interaction partners.