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Gene Review

argE  -  acetylornithine deacetylase

Escherichia coli str. K-12 substr. MG1655

Synonyms: Arg4, ECK3948, JW3929, argA
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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


Biological context of argE


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].


  1. Cloning and organization of seven arginine biosynthesis genes from Neisseria gonorrhoeae. Picard, F.J., Dillon, J.R. J. Bacteriol. (1989) [Pubmed]
  2. Promoter mapping and selection of operator mutants by using insertion of bacteriophage Mu in the argECBH divergent operon of Escherichia coli K-12. Beny, G., Boyen, A., Charlier, D., Lissens, W., Feller, A., Glansdorff, N. J. Bacteriol. (1982) [Pubmed]
  3. Turn-on of inactive genes by promoter recruitment in Escherichia coli: inverted repeats resulting in artificial divergent operons. Charlier, D., Severne, Y., Zafarullah, M., Glansdorff, N. Genetics (1983) [Pubmed]
  4. Identification and characterization of the Myxococcus xanthus argE gene. Harris, B.Z., Singer, M. J. Bacteriol. (1998) [Pubmed]
  5. Nucleotide sequence analysis of a gene cloned from Leptospira biflexa serovar patoc which complements an argE defect in Escherichia coli. Zuerner, R.L., Charon, N.W. J. Bacteriol. (1988) [Pubmed]
  6. Two regions in human DNA polymerase beta mRNA suppress translation in Escherichia coli. Date, T., Tanihara, K., Yamamoto, S., Nomura, N., Matsukage, A. Nucleic Acids Res. (1992) [Pubmed]
  7. The regulatory region of the divergent argECBH operon in Escherichia coli K-12. Piette, J., Cunin, R., Boyen, A., Charlier, D., Crabeel, M., Van Vliet, F., Glansdorff, N., Squires, C., Squires, C.L. Nucleic Acids Res. (1982) [Pubmed]
  8. Male sterility in transgenic tobacco plants induced by tapetum-specific deacetylation of the externally applied non-toxic compound N-acetyl-L-phosphinothricin. Kriete, G., Niehaus, K., Perlick, A.M., Pühler, A., Broer, I. Plant J. (1996) [Pubmed]
  9. Characterization and kinetic mechanism of mono- and bifunctional ornithine acetyltransferases from thermophilic microorganisms. Marc, F., Weigel, P., Legrain, C., Almeras, Y., Santrot, M., Glansdorff, N., Sakanyan, V. Eur. J. Biochem. (2000) [Pubmed]
  10. Gene cloning, sequence analysis, purification, and characterization of a thermostable aminoacylase from Bacillus stearothermophilus. Sakanyan, V., Desmarez, L., Legrain, C., Charlier, D., Mett, I., Kochikyan, A., Savchenko, A., Boyen, A., Falmagne, P., Pierard, A. Appl. Environ. Microbiol. (1993) [Pubmed]
  11. The argG gene of Streptomyces clavuligerus has low homology to unstable argG from other actinomycetes: effect of amplification on clavulanic acid biosynthesis. Rodríguez-García, A., Martín, J.F., Liras, P. Gene (1995) [Pubmed]
  12. Identification of the structural genes for glutamate synthase and genetic characterization of this region of the Salmonella typhimurium chromosome. Fuchs, R.L., Madonna, M.J., Brenchley, J.E. J. Bacteriol. (1982) [Pubmed]
  13. In vitro transcription of the Escherichia coli K-12 argA, argE, and argCBH operons. Sens, D., Natter, W., James, E. J. Bacteriol. (1977) [Pubmed]
  14. Immunological and genetic properties of Escherichia coli K12 argE mutants. Kadikiran, A.E., Baumberg, S. Mol. Gen. Genet. (1980) [Pubmed]
  15. Structural and biochemical characterization of the Escherichia coli argE gene product. Meinnel, T., Schmitt, E., Mechulam, Y., Blanquet, S. J. Bacteriol. (1992) [Pubmed]
  16. Positive control of expression of the argECBH gene cluster in vitro by guanosine 5'-diphosphate 3'-diphosphate. Zidwick, M.J., Korshus, J., Rogers, P. J. Bacteriol. (1984) [Pubmed]
  17. Mechanistic analysis of the argE-encoded N-acetylornithine deacetylase. Javid-Majd, F., Blanchard, J.S. Biochemistry (2000) [Pubmed]
  18. Structural and regulatory mutations allowing utilization of citrulline or carbamoylaspartate as a source of carbamoylphosphate in Escherichia coli K-12. Legrain, C., Stalon, V., Glansdorff, N., Gigot, D., Piéard, A., Crabeel, M. J. Bacteriol. (1976) [Pubmed]
  19. Regulation and coupling of argECBH mRNA and enzyme synthesis in cell extracts of Escherichia coli. Zidwick, M.J., Keller, G., Rogers, P. J. Bacteriol. (1984) [Pubmed]
  20. Parameters of gene expression in the bipolar argECBH operon of E. coli K12. The question of translational control. Cunin, R., Boyen, A., Pouwels, P., Glansdorff, N., Crabeel, M. Mol. Gen. Genet. (1975) [Pubmed]
  21. Expression of biosynthetic genes from Pseudomonas aeruginosa and Escherichia coli in the heterologous host. Jeenes, D.J., Soldati, L., Baur, H., Watson, J.M., Mercenier, A., Reimmann, C., Leisinger, T., Haas, D. Mol. Gen. Genet. (1986) [Pubmed]
  22. Arginine biosynthesis in Campylobacter jejuni TGH9011: determination of the argCOBD cluster. Hani, E.K., Ng, D., Chan, V.L. Can. J. Microbiol. (1999) [Pubmed]
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