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Nucleic Acids Research, 1978, Vol. 5, No. 3 975-986
© 1978

Articles

Yeast seryl tRNA synthetase: interactions between the ATP binding site and the sites for tRNASer and L-serine

Ulrich Pachmann and Hans G. Zachau

Institut für Physiologische Chemie, Physikalische Biochemie und Zellbiologie der Universität München Goethestrasse 33, D-8000 München 2, GFR

Received January 20, 1978. T1 ribonuclease digestion of yeast tRNASer in the presence of seryl tRNA synthetase was used for monitoring the relationship between the substrate binding sites on the synthetase. It was found that (a) ATP displaces the tRNA from the synthetase with an effector affinity constant corresponding to the Km for ATP of 10 µM; (b) AMP and a number of nucleoside tri-phosphates, while influencing the rate of aminoacylation, do not displace the tRNA from the enzyme; (c) ADP and PPi inhibit the aminoacylation and the binding of tRNASer; (d) adenylyl diphosphonate is bound to the synthetase and lowers the protection of the tRNA against the nuclease attack in a similar way as does ATP; (e) interactions between the sites of L-serine and tRNASer could only be shown when both sites for serine were saturated and, in addition, the ATP analog or ADP was present. It is concluded that in seryl tRNA synthetase binding sites for ATP interact with the ones for tRNA as well as with the ones for serine. These findings contribute to the understanding of the mechanism of aminoacylation.


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