Disease relevance of argA

• Escherichia coli mutant containing a large deletion from relA to argA [1].
• Characterization of the argA gene required for arginine biosynthesis and syringomycin production by Pseudomonas syringae pv. syringae [2].
• Involvement of LuxR, a quorum sensing regulator in Vibrio harveyi, in the promotion of metabolic genes: argA, purM, lysE and rluA [3].

High impact information on argA

• Regions suggesting ancestral relationships to N-acetylglutamate synthase and aspartate beta-semialdehyde dehydrogenase have been identified [4].
• The ts mutation was mapped to 60.6 min of the S. typhimurium chromosome and was linked to argA and cysH [5].
• Although the signal peptide encoded by the new plasmid differs from the wild type (pBR322) by 2 amino acid residues (Ser 2 to Arg 2 and Ala 23 to Gly 23), the synthesis, transport, and processing of the beta-lactamase remain unchanged in Escherichia coli [6].
• Complete nucleotide sequence of the Escherichia coli argA gene [7].
• The cDNA sequence complements an argA (NAGS)-deficient Escherichia coli strain, reversing its arginine auxotrophy [8].

Chemical compound and disease context of argA

• Gel-filtration of a heat-treated extract of the complemented double mutant E. coli host showed that N-acetylglutamate synthase and ornithine acetyltransferase activities co-elute in a single peak corresponding to M(r) 110,000 [9].
• The Escherichia coli argB and argC gene products are functionally analogous to kinases and dehydrogenases of other pathways, which by their successive action also achieve the conversion of a carboxylate into an aldehyde function [10].
• Nucleotide sequence of Escherichia coli argB and argC genes: comparison of N-acetylglutamate kinase and N-acetylglutamate-gamma-semialdehyde dehydrogenase with homologous and analogous enzymes [10].

Biological context of argA

• Both N-acetylglutamate synthase and ornithine acetyltransferase are encoded by the same 1290 bp open reading frame [9].
• The inferred amino acid sequence of the T. cutaneum argA-encoded protein contains 1,168 residues showing 62% identity with the sequence of the S. cerevisiae CPA2 protein, and the comparison of the two sequences uncovered a putative intron sequence of 81 nucleotides close to the 5' end of the coding region of the T. cutaneum argA gene [11].
• Based on analysis of luxR-dependent promoters, particularly that of argA, we describe a LuxR binding site, and implicate the coordination of LuxR with ArgR [3].
• Integration of the fusion at the argB locus results in a situation in which the only 5'-flanking sequences of the IPNS gene upstream from the chimeric fused gene are those included in the transforming plasmid [12].
• One of the structures analyzed displays two inversely repeated argE genes rearranged into an artificial divergent operon [13].

Associations of argA with chemical compounds

• N-acetylglutamate synthase extracted from the three mutants was approximately one hundred times less sensitive to L-arginine than the enzyme from the feedback sensitive parent strain [14].
• We have therefore undertaken the nucleotide sequence analysis of the argB and argC genes and compared the derived amino acid sequences with the known sequences of analogous enzymes active in the proline and homoserine biosynthetic pathways and in glycolysis [10].

Other interactions of argA

• Mutants with a feedback resistant N-acetylglutamate synthase have been isolated from a proA/B, argD, argR strain by screening for proline excretion on minimal medium with arginine [14].
• We have constructed a series of deletion plasmids which contain the Aspergillus nidulans argB gene for ornithine carbamoyltransferase (OTC) [15].
• Residues Arg-2 and Leu-3 were shown to be critical for the activation of the mtr promoter [16].

References