Abstract
Regulators encoded by the beta-glucoside (bgl) operon of Escherichia coli are known to influence the expression of downstream target genes that confer a fitness advantage in stationary phase. We have examined the role of bglG in the regulation of ridA that encodes an enamine/imine deaminase essential for the elimination of reactive intermediates generated during the catabolism of amino acids such as serine. We report here that ridA is positively regulated by leucine responsive regulatory protein (Lrp) and leucine antagonizes the activation by Lrp. We also show that Lrp itself is under the indirect regulation of BglG, which brings about the overexpression of ridA in Bgl+ strains during stationary phase. Loss of ridA function in a Bgl+ background results in a significant growth retardation in serine-containing media compared to that in a Bgl- background. We propose that overexpression of ridA in Bgl+ background during stationary phase is physiologically relevant to eliminate toxic metabolites generated by the catabolism of serine-containing peptides as a result of elevated levels of their uptake.
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