Disease relevance of argR

• In Escherichia coli, the arginine repressor, the product of the argR gene, in conjunction with L-arginine controls the synthesis of the enzymes of arginine biosynthesis [1].
• The argR gene of Bacillus subtilis complements an E.coli argR deficiency for cer-mediated recombination despite the two proteins having only 27% amino acid identity [2].
• We report here the cloning of the arginine repressor gene argR of Bacillus stearothermophilus and the characterization and purification to homogeneity of its product [3].
• However, here we demonstrate that the arginine repressor from the hyperthermophilic bacterium Thermotoga neapolitana (ArgR(Tn)) exhibits characteristics that clearly distinguish this regulator from the well-studied homologues from Escherichia coli, Bacillus subtilis and B.stearothermophilus [4].
• Control of arg gene expression in Salmonella typhimurium by the arginine repressor from Escherichia coli K-12 [5].

High impact information on argR

• This plasmid stabilizing recombination system requires the presence in cis of the ColE1 cer region, plus at least two trans-acting factors encoded by the xerA and xerB genes of Escherichia coli [6].
• The argR protein binds to cer DNA both in vivo and in vitro in the presence of arginine [2].
• Sequences within DsrA complementary to three additional genes, argR, ilvIH, and rbsD, suggest that DsrA is a riboregulator of gene expression that acts coordinately via RNA:RNA interactions at multiple loci [7].
• We describe the nucleotide sequence of the argR gene, including its control region, and show that formation of the repressor is autoregulated [1].
• The argR control region contains two promoters, one of which overlaps the operator site and, as with other arg genes, consists of two adjacent palindromic sequences ("ARG boxes") [1].

Chemical compound and disease context of argR

• Ornithine transcarbamoylase was purified by affinity chromatography from Escherichia coli W argR- by using N-delta-(phosphonoacetyl)ornithine as the ligand [8].
• A single free Cys sidechain in the N-terminal domain of the E. coli arginine repressor was covalently derivatized with S-cysteaminyl-EDTA for site-specific attachment of paramagnetic metal ions [9].
• The filter element is demonstrated with a (1)H NOESY spectrum of a 28.5-kDa 2:1 complex between the uniformly (13)C-labeled N-terminal domain of Escherichia coli arginine repressor and operator DNA [10].
• A plasmid carrying the arginine repressor gene (argR) of Escherichia coli was obtained out of the Clarke and Carbon colony bank which contains clones of individual ColE1 plasmids carrying fragments of the E. coli chromosome [11].

Biological context of argR

• In the operator sites for the structural genes of the regulon the two ARG boxes are separated by three base-pairs, in the regulatory gene argR they are separated by two base-pairs [12].
• By hydroxylamine mutagenesis two types of argR mutants were isolated and mapped [13].
• Furthermore, the arginine catabolic arcABD1C1C2TD2 operon was activated by the product of ahrC but not by that of argR [14].
• Arginine operator sequences (Arg boxes) from argI were also cloned into the same plasmids for titration of the arginine repressor [15].
• The relative positions of argR (encoding arginine repressor) and mdh on the chromosome of S. typhimurium were determined from analysis of the nt sequence [16].

Associations of argR with chemical compounds

• These effects appear to depend on the concurrent expression of the regulatory-gene and streptomycin resistance mutations, as indicated by analogous experiments with canavanine-resistant mutants of 250-10 that have partial argR- character [17].
• This observation, together with our previous report that argR mutations impair the cumulative repression of CPSase, suggests that this control is mediated through the concerted effects of regulatory elements specific for the arginine and pyrimidine pathways [18].
• Other mutants harbored wild-type argR genes, and 20 mutants have lost their ability to grow in normal air without carbon dioxide enrichment; this revealed a link between arginine biosynthesis and a still-unknown CO2-dependent metabolic pathway [19].
• We demonstrate that this unusual behaviour for an ArgR protein can, to a large extent, be ascribed to the presence of a serine residue at position 107 of ArgR(Tn), instead of the highly conserved glutamine that is involved in arginine binding in the E.coli repressor [4].
• Dissecting the molecular details of prokaryotic transcriptional control by surface plasmon resonance: the methionine and arginine repressor proteins [20].

Other interactions of argR

• The three arginine biosynthetic operons argCJDBF, argGH, and gltS-argE were shown to be repressed by the products of argR and ahrC [14].
• Using strains carrying defined argR, and rpoS mutations, we evaluated the relative contributions of these two regulators to the expression of argH using operon-lacZ fusions [21].

Analytical, diagnostic and therapeutic context of argR

• Moreover, sequence analysis of 85 strains shows no evidence of selection at the arginine repressor locus [22].

References