Disease relevance of fadR

• Fatty acid biosynthesis and fatty acid degradation in Escherichia coli are co-ordinately regulated at the level of transcription by the product of the fadR gene, FadR [1].
• Recombinant Escherichia coli fadR atoC(Con) mutants containing the polyhydroxyalkanoate (PHA) biosynthesis genes from Alcaligenes eutrophus are able to incorporate significant levels of 3-hydroxyvalerate (3HV) into the copolymer poly(3-hydroxybutyrate-co-3-hydroxyvalerate) [P(3HB-co-3HV)] [2].
• An 8.1-kb fragment of chromosomal DNA from Clostridium acetobutylicum NCIMB 8052 (formerly NCIB 8052) has been cloned into plasmid pAT153 and shown to allow the growth of Escherichia coli LJ32 (F+ atoC2c atoD32 fadR) on butyrate as the sole source of carbon and energy [3].

High impact information on fadR

• Nucleotide sequence of the fadR gene, a multifunctional regulator of fatty acid metabolism in Escherichia coli [4].
• Primer extension experiments demonstrated that the transcription of the fadR gene initiates with an adenine nucleotide 33 nucleotides upstream from the predicted start of translation [4].
• The coding sequence of the fadR gene is 714 nucleotides long and is preceded by a typical E. coli ribosome binding site and is followed by a sequence predicted to be sufficient for factor-independent chain termination [4].
• Thus, uspA is a member of the fadR regulon [5].
• The growth phase-dependent increased and decreased transcription of fad genes and fabA, respectively, is dependent on the status of the fadR gene [5].

Biological context of fadR

• We located the rap site at 26 min in the E. coli genetic map and determined the gene order fadR-rap-supF-trp from our transduction experiments [6].

Associations of fadR with chemical compounds

• Transcription of uspA is derepressed during exponential growth in fadR null mutants or by including the fatty acid oleate in the growth medium of FadR+ cells [5].

Other interactions of fadR

• Microarray data indicated that the expression levels of several important genes of acetate metabolism such as acs, aceAB, cysDEK, fadR, etc. were significantly altered in the absence of rpoS gene [7].
• Similarly, E. coli fadR mutants were used alone and in conjunction with fadA, fadB, and fadL mutants to show that the effect of the fadR mutation is dependent on fadB+ and fadA+ gene products [2].

Analytical, diagnostic and therapeutic context of fadR

• Dominant negative mutations in fadR were generated by random and site-directed mutagenesis [8].

References