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. 1973 May;114(2):632–640. doi: 10.1128/jb.114.2.632-640.1973

Regulation of argE-argH Expression with Arginine Derivatives in Escherichia coli: Extreme Non-uniformity of Repression and Conditional Repressive Action

Arthur P Bollon a,1, Henry J Vogel a
PMCID: PMC251819  PMID: 4574695

Abstract

In regulatory studies of the arginine biosynthetic system of Escherichia coli, α-N-acetyl-l-arginine (AcA) is a useful restrictive arginine source. In strain 39A-23R3 (argA−), at 25 μg/ml, AcA gives suboptimal growth rates and is fully derepressive for acetylornithinase (specified by argE) and approximately 50% derepressive for argininosuccinase (specified by argH). At 10 μg/ml, the growth rate decreases, whereas the extent of derepression is unchanged; at 500 μg/ml, full repression results. In strain 3670 (argB−argG−), AcA (25 μg/ml) leads to partial derepression of acetylornithinase but full repression of argininosuccinase. Thus, the repression patterns for both strains, although not identical, are nonuniform. AcA utilization is antagonized by α-N-acetyl-l-ornithine (AcO). In strain 3670 (blocked before and after acetylornithinase), the growth rate on AcA (25 μg/ml) is lowered by AcO (500 μg/ml); acetylornithinase is completely derepressed, whereas argininosuccinase is fully repressed. This difference in regulatory behavior represents extreme nonuniform repression. Unexpectedly, the effect of AcO is attributable to the conversion of AcO to citrulline (Cit). In strain 3670, mixtures of AcA (25 μg/ml) and Cit (300 μg/ml) permit complete derepression of acetylornithinase; there is evidence that Cit enters the cell. In contrast, in the arginine-limited chemostat, Cit represses acetylornithinase. These opposite regulatory effects of Cit appear to stem from the difference in arginine restriction. AcA enters the cell via AcO permease and is deacylated by acetylornithinase (Km, 5.0 mM). AcA competitively inhibits AcO cleavage (Ki, 2.4 mM), but Cit is not inhibitory. The antagonism of AcA utilization by AcO or Cit is thought to be exerted at the AcO permease.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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