Disease relevance of argE

• An E. coli defective in the acetylornithine deacetylase gene (argE) was complemented by the ornithine acetyltransferase gene (argJ) from N. gonorrhoeae [1].
• The analysis of a large number of Arg mutants obtained by inserting phage Mu in the argECBH cluster of genes confirmed the "facing" arrangement proposed earlier for the promoters of argE (argEp) and argCBH (argCBHp) and clarified remaining ambiguities regarding the localization of argEp [2].
• The rearrangements were obtained as reactivations of argE in a strain harboring an argEp deletion on a lambda darg prophage [3].
• Identification and characterization of the Myxococcus xanthus argE gene [4].
• Nucleotide sequence analysis of a gene cloned from Leptospira biflexa serovar patoc which complements an argE defect in Escherichia coli [5].

High impact information on argE

• Since substitution of the rat Arg-4 codon with synonymous codons showed strong effects upon the expression level, we propose that the arg codon at the N-terminal coding region plays a role in modulating expression [6].
• Mutations causing semi-constitutive expression of argE improve putative promoter sequences within argC [7].
• Overlapping of the argCBH promoter and the region involved in ribosome mobilization for argE translation explains the dual effect of some mutations [7].
• In order to construct inducible male-sterile plants, the argE coding region was fused to a DNA fragment carrying sequences homologous to the tobacco TA29 promoter, known to function exclusively in the tapetum [8].
• The argE gene product of Escherichia coli, representing a N-acetyl-L-ornithine deacetylase was identified to remove the acetyl-group from N-ac-Pt giving the cytotoxic compound L-phosphinothricin (Pt, glufosinate) [8].

Chemical compound and disease context of argE

• The chromosomal acetylornithine deacetylase (argE) gene of Myxococcus xanthus was identified via homology to acetylornithine deacetylases from other bacterial species [4].
• Archaeal argJ only complements an Escherichia coli argE mutant (deficient in acetylornithinase, which catalyzes the fifth step in the linear biosynthetic pathway), whereas bacterial genes additionally complement an argA mutant (deficient in N-acetylglutamate synthetase, the first enzyme of the pathway) [9].
• Transformants expressing aminoacylase activity were selected by their ability to complement E. coli mutants defective in acetylornithine deacetylase activity, the enzyme that converts N-acetylornithine to ornithine in the arginine biosynthetic pathway [10].
• The argG gene of Streptomyces clavuligerus has low homology to unstable argG from other actinomycetes: effect of amplification on clavulanic acid biosynthesis [11].
• In contrast to results obtained with Escherichia coli mutants, there was no linkage between mutations affecting glutamate synthase activity and the argG gene [12].

Biological context of argE

• In vitro transcription of the Escherichia coli K-12 argA, argE, and argCBH operons [13].
• Co-suppression of each argE mutation with known strongly polar lacZ amber, ochre and UGA mutations was looked for to distinguish missfense from nonsense argE's, Arg+ revertants being screened for Lac+ and Mel+ phenotypes [14].
• The DNA sequence of a 2,100-bp region containing the argE gene from Escherichia coli has been determined [15].
• Nucleotide sequence analysis indicated a single open reading frame within the region containing argE complementing activity [5].
• A gene which complements an argE mutation in Escherichia coli was isolated from a plasmid-based genomic library composed of Leptospira biflexa serovar patoc DNA [5].

Anatomical context of argE

• Added ppGpp had no important effect upon (i) measurable argE or argH enzyme activity, (ii) total protein synthesis in the cell-free system, or (iii) the rate of decay of hybridizable argECBH mRNA [16].

Associations of argE with chemical compounds

• Mechanistic analysis of the argE-encoded N-acetylornithine deacetylase [17].
• Citrulline utilizers are argG bradytrophs or strains in which the synthesis of ornithine carbamoyltransferase (either of the F or I type) is specifically depressed by unstable chromosomal rearrangements or stable mutations that presumably affect the operators of those genes [18].
• A mutant carrying a disruption in argE was unable to grow on minimal media lacking supplemental arginine and formed fruiting bodies and spores in response to arginine starvation at high cell density [4].
• The argECBH mRNA made under conditions of restricted protein synthesis had reduced ability to function in the formation of the argE and argH enzymes and was found to be predominantly 6 to 8S in sucrose density gradients [19].
• The accurate determination of argE and argCBH m-RNA levels in different steady states of expression of the arg regulon supports the following conclusions: 1 [20].

Other interactions of argE

• The nucleotide sequence of the ppc-argE intergenic region was also solved and shown to contain six tandemly repeated REP sequences [15].
• The E. coli argA and argF enzymes, which are controlled by repression in their native host, were synthesized constitutively in P. aeruginosa at 5% of the levels measured in E. coli under derepressed conditions [21].

Analytical, diagnostic and therapeutic context of argE

• However, sequence analysis of the gene complementing ArgA function in two separate E. coli argA mutants determined that the C. jejuni gene was not a canonical argA gene [22].

References