Disease relevance of aroF

• Repression of the aroF promoter by the TyrR repressor in Escherichia coli K-12: role of the 'upstream' operator site [1].
• Regulation of the Salmonella typhimurium aroF gene in Escherichia coli [2].

High impact information on aroF

• A similar accumulation of tyrosine and phenylalanine is seen in cells carrying a multiple-copy plasmid that carries a wild-type aroF allele in addition to pheA and tyrA, the structural genes for controlling enzymes of the terminal pathways to phenylalanine and tyrosine biosynthesis [3].
• Two of these operator sites lie adjacent to each other and overlap the -35 region of the aroF promoter while the third lies about 70 base pairs upstream of the promoter [1].
• Three other TyrR mutant proteins, lacking up to 143 amino acid residues from the N-terminal end of the protein, retained the ability to repress the aroF promoter, to different extents, in a tyrosine-dependent manner [4].
• The S. typhimurium aroF regulatory region contains three imperfect palindromes, two upstream of the promoter and one overlapping the promoter, that are nearly identical to operators aroFo1, aroFo2, and TyrR box 1 of E. coli [2].
• The nucleotide sequence of S. typhimurium aroF was determined and compared with its E. coli homolog [2].

Chemical compound and disease context of aroF

• The Salmonella typhimurium aroF gene, encoding the tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase, was localized to a chromosomal PstI fragment by Southern blotting with an Escherichia coli aroF probe [2].

Biological context of aroF

• In the present study, gene expression patterns of the shikimate producing strain W3110.shik1 (W3110 with aroL deletion and plasmid-overexpressed aroF) and the wild type strain W3110 grown under carbon- and phosphate-limited (carbon-rich) chemostat conditions (D=0.23h(-1)) were analyzed [5].
• The existence of a functional promoter divergently transcribing from the aroF regulatory region was also demonstrated by using the cat fusion vector [6].
• It is proposed that in the proximal region of the aroF-tyrA operon there is an attenuator site controlled by the level of charged tryptophanyl-transfer RNA [7].
• In the aroF gene this bend has been localized to a region containing two TyrR protein-binding sites [8].

References