Cloning, sequencing and characterization of a fatty acid synthase-encoding gene from Mycobacterium tuberculosis var. bovis BCG.
Mycobacterial cell walls contain unique lipids such as mycolic acids, very long chain fatty acids and multimethyl-branched fatty acids. A multifunctional fatty acid synthase ( Fas) with the unique capability of catalyzing both de novo synthesis and chain elongation of fatty acids has been purified and characterized from Mycobacterium tuberculosis var. bovis BCG (Bacillus Calmette-Geurin) [Kikuchi et al., Arch. Biochem. Biophys. 295 (1992) 318-326]. To understand how the various domains that catalyze the reactions involved in both de novo synthesis and elongation are organized in the mycobacteria, a fas gene was cloned from a cosmid library of genomic DNA from M. bovis BCG. Sequencing of the cosmid clone revealed a contiguous sequence of 11 577 bp of mycobacterial genome containing a 8389-bp open reading frame that could code for a protein of 2797 amino acids (301 kDa). By comparing the Fas aa sequence with the sequences in the active site regions of known fas and polyketide synthase-encoding genes, the functional catalytic domains in Fas were identified. This analysis revealed that the domains are organized in the following order: acyltransferase, enoyl reductase, dehydratase, malonyl/palmitoyl transferase, acyl carrier protein, beta-keto reductase, beta-ketoacyl synthase. This domain organization is like a head to tail fusion of the two yeast fas gene subunits. The results obtained constitute the first report of the cloning, sequencing and structural elucidation of a fas from the Mycobacteria.[1]References
- Cloning, sequencing and characterization of a fatty acid synthase-encoding gene from Mycobacterium tuberculosis var. bovis BCG. Fernandes, N.D., Kolattukudy, P.E. Gene (1996) [Pubmed]
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