Novel data on interactions of elongation factor Ts

Abstract

Interactions of EF-Ts with EF-Tu at all steps of the elongation cycle were studied by limited trypsinolysis, gel-filtration, analytical centrifugation and fluorescence polarization techniques. It is shown that EF-Ts does not dissociate from EF-Tu after GDP to GTP exchange, but remains bound to the Aa-tRNA-EF-Tu-GTP complex up to GTP hydrolysis stage on the ribosome. The possible role of these interactions is discussed.