Metabolites influence control of lysine transfer ribonucleic acid synthetase formation in Escherichia coli K-12.

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Abstract
A mutant of E. coli K-12 has been isolated which has only 1-3% of the wild-type lysyl-tRNA synthetase activity [L-lysine:tRNA ligase (AMP forming), EC 6.1.1.6]. Additions of 20 mM L-alanine or 6 mM leucine dipeptides to the culture medium can restore the activity of lysyl-tRNA synthetase in the mutant strain to the wild-type level. Experiments on the in vivo charging of lysine tRNA in the mutant show that in the absence of the metabolites lysine tRNA is charged 15-23%. Upon the addition of 3 mM L-leucyl-L-alanine to the medium the lysyl tRNA synthetase activity increases 25-fold and the in vivo charging of lysine tRNA returns to the wild-type level. Experiments with antibody against lysyl-tRNA synthetase show that the stimulation of lysyl-tRNA synthetase activity by the metabolites is the result of new protein synthesis.

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