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Gene Review

argH  -  argininosuccinate lyase

Escherichia coli CFT073

 
 
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Disease relevance of argH

  • The mutation causing the altered electrophoretic mobility is located between argH and rif (79 min on the E. coli genetic map) [1].
  • When the bfe+ allele, which is closely linked to the argH locus, was introduced into an argH bfe recipient by conjugation, arg+ recombinant cells rapidly and simultaneously acquired sensitivity to colicin E3 and phage BF23 [2].
 

High impact information on argH

  • In the reciprocal experiment introducing bfe into an argH bfe+ recipient, it was found that colicin E3-resistant, arg+ cells began to appear shortly after the arg+ recombinant population began to divide [2].
  • The ratios of steady-state argE and argH enzyme synthesis without arginine to that with arginine were 12 and 20, respectively, whereas the similar ratio for argECBH mRNA was 2 to 3 [3].
  • In a comparative cross employing a haploid E. coli Hfr, in which rha inheritance was similar at 56%, argH inheritance was 41% [4].
  • By inserting a T7 bacteriophage promoter into the plasmid, a version of the cDNA which is able to complement both the C. reinhardtii arg7 mutant and the Escherichia coli argH mutant has been created [5].
  • The argH open reading frame encodes a protein comprised of 461 amino acids with a calculated molecular mass of 51,349 Da [6].
 

Biological context of argH

  • Attempts to create an argH auxotroph of M. maripaludis by disrupting the genomic allele were unsuccessful: although a knockout allele of argH was integrated into the M. maripaludis chromosome by homologous recombination, the intact copy was not excluded, suggesting that the argH gene is essential [7].
 

Associations of argH with chemical compounds

  • Genes argF and argH were not linked to other arginine biosynthetic genes by cross-complementation analysis [8].

References

  1. A mutant of Escherichia coli with an altered elongation factor Tu. Pedersen, S., Blumenthal, R.M., Reeh, S., Russell, L.B., Lemaux, P., Laursen, R.A., Nagarkatti, S., Friesen, J.D. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  2. Biosynthesis of the outer membrane receptor for vitamin B12, E colicins, and bacteriophage BF23 by Escherichia coli: kinetics of phenotypic expression after the introduction of bfe+ and bfe alleles. Bassford, P.J., Kadner, R.J., Schnaitman, C.A. J. Bacteriol. (1977) [Pubmed]
  3. Dual regulation by arginine of the expression of the Escherichia coli argECBH operon. Kryzek, R.A., Rogers, P. J. Bacteriol. (1976) [Pubmed]
  4. Conservation of Salmonella typhimurium deoxyribonucleic acid by chromosomal insertion in a partially diploid Escherichia coli hybrid. Johnson, E.M., Placek, B.P., Snellings, N.J., Baron, L.S. J. Bacteriol. (1975) [Pubmed]
  5. The argininosuccinate lyase gene of Chlamydomonas reinhardtii: cloning of the cDNA and its characterization as a selectable shuttle marker. Auchincloss, A.H., Loroch, A.I., Rochaix, J.D. Mol. Gen. Genet. (1999) [Pubmed]
  6. Cloning, characterization, and functional expression in Escherichia coli of argH encoding argininosuccinate lyase in the cyanobacterium Nostoc sp. strain PCC 73102. Troshina, O., Hansel, A., Lindblad, P. Curr. Microbiol. (2001) [Pubmed]
  7. Functional conservation between the argininosuccinate lyase of the archaeon Methanococcus maripaludis and the corresponding bacterial and eukaryal genes. Cohen-Kupiec, R., Kupiec, M., Sandbeck, K., Leigh, J.A. FEMS Microbiol. Lett. (1999) [Pubmed]
  8. 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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