Detlev Riesner

TL;DR: The interaction between phenylalanyl-tRNA synthetase from yeast and Escherichia coli and tRNAPhe, tRNASer (yeast), tRNA1Val (E. coli) has been investigated by ultracentrifugation analysis, fluorescence titrations and fast kinetic techniques.

TL;DR: The kinetics of the interaction of tRNASer and seryl-tRNA synthetase from yeast as well as of t RNATyr and tyrosyl-t RNA synthetases from Escherichia coli have been investigated by temperature-jump experiments and it was shown that complex formation proceeds in two distinct steps.

TL;DR: Complexes between tRNAPhe, tRNASer, tRNAAla and tRNATyr and their cognate aminoacyl-tRNA synthetases have been studied by sedimentation velocity runs in an analytical ultracentrifuge and binding data are discussed with respect to the tertiary structure of the tRNAs, the subunitructure of the synthetase and the possible physical basis for the non-equivalence of binding sites.

TL;DR: The kinetics of the melting transitions of tRNA Phe (yeast) were followed by the fluorescence of the Y-base and of formycin substituted for the 3'-terminal adenine, resulting in a coupled opening of the anticodon and acceptor branches.

TL;DR: Using fluoresceinylthiocarbamoyl-tRNATyr, it could be demonstrated that the binding of two tRNA-molecules is anti-cooperative: the binding sites for tRNA on the synthetase are a priori identical, but when one tRNA is bound, thebinding of the second t RNA is disfavoured.