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Volume 270, Number 24, Issue of June 16, pp. 14439-14444, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Annie Brevet , Josiane Chen , Franoise Lévque , Sylvain Blanquet , Pierre Plateau

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 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.

Homogeneous LysU and LysS were also compared in ApA 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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