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In Escherichia coli, lysyl-tRNA synthetase activity is
encoded by either a constitutive lysS gene or an inducible
one, lysU. The two corresponding enzymes could be purified at
homogeneity from a
Homogeneous LysU
and LysS were also compared in Ap
lysU and a lysS strain,
respectively. Comparison of the pure enzymes, LysS and LysU, indicates
that, in the presence of saturating substrates, LysS is about twice
more active than LysU in the ATP-PP
exchange as well as in
the tRNA aminoacylation reaction. Moreover, the
dissociation constant of the LysU-lysine complex is 8-fold smaller than
that of the LysS-lysine complex. In agreement with this difference, the
activity of LysU is less sensitive than that of LysS to the addition of
cadaverine, a decarboxylation product of lysine and a competitive
inhibitor of lysine binding to its synthetase. This observation points
to a possible useful role of LysU, under physiological conditions
causing cadaverine accumulation in the bacterium. Remarkably, these
conditions also induce lysU expression.
A synthesis. LysU is only
2-fold more active than LysS in the production of this dinucleotide.
This makes unlikely that the heat-inducible LysU species could be
preferentially involved in the accumulation of ApA inside
stressed Escherichia coli cells. This conclusion could be
strengthened by determining the concentrations of ApN (N
= A, C, G, or U) in a lysU as well as in a lysU strain, before and after a 1-h
temperature shift at 48 °C. The measured concentration values were
the same in both strains.
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