Moreover, we found that FdmR suppresses degradation of long-chain acyl-CoAs endogenously synthesized through the type I fatty acid synthase. We demonstrated that FdmR functions as a valve to direct the flux of exogenously derived fatty acids away from β-oxidation toward lipid biosynthesis, thereby avoiding the overactive catabolism and accumulation of biologically toxic intermediates. FdmR was identified as a long-chain acyl-coenzyme A (acyl-CoA)–responsive repressor of genes involved in fatty acid degradation and modification. The mutant showed defective growth but high substrate consumption on fatty acids. marinum mutant deficient in FdmR was severely attenuated in zebrafish larvae and adult zebrafish. Here, we identified a TetR-family transcriptional factor, FdmR, as the key regulator of fatty acid catabolism in the pathogen Mycobacterium marinum by combining use of transcriptomics, chromatin immunoprecipitation followed by sequencing, dynamic 13C-based flux analysis, metabolomics, and lipidomics. How mycobacterial cells regulate the catabolism of fatty acids to serve the pathogenicity, however, remains unknown. Host-derived fatty acids are an important carbon source for pathogenic mycobacteria during infection.
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The developer pre-release version was a snapshot of AmigaOS 4.0 for AmigaOne. Support for file sizes larger than 2 GBĭeveloper pre-releases AmigaOS 4.0 (Developer Pre-release).
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