Interactions of eukaryotic elongation factor 2 with actin: A possible link between protein synthetic machinery and cytoskeleton

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Abstract
Eukaryotic elongation factor 2 (EF‐2) was shown to bind to F‐actin as assayed by co‐sedimentation. In the presence of guanosine‐5′‐O‐(3‐thiotriphosphate) (GTPγS) binding was increased fourfold. At saturation level a molar ratio of about 0. 12 EF‐2 per F‐actin (subunit) was observed. Our results suggest a single type of binding site with an apparent dissociation constant of 0.85 μM. The stoichiometry was independent of the filament length, and ADP‐ribosylation had no effect on the binding. Experimental data indicated the involvement of SH‐groups of both EF‐2 and actin in the binding. The interaction EF‐2 with F‐actin appeared to be inhibited competitively by EF‐1α and non‐competitively by G‐actin.