Comparative and Functional Genomics
Volume 2009 (2009), Article ID 836172, 4 pages
doi:10.1155/2009/836172
Research Article

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

Aner Gurvitz

Section of Physiology of Lipid Metabolism, Center for Physiology, Pathophysiology and Immunology, Institute of Physiology, Medical University of Vienna, Schwarzspanierstrasse 17, 1090 Vienna, Austria

Received 16 March 2009; Accepted 31 July 2009

Academic Editor: Eivind Hovig

Copyright © 2009 Aner Gurvitz. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

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.