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

FEBS Lett. 1994 Dec 12;356(1):89-93. doi: 10.1016/0014-5793(94)01239-3.

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) (GTP gamma S) 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 microM. 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-1 alpha and non-competitively by G-actin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Animals
  • Cytoskeleton / metabolism*
  • Guanosine 5'-O-(3-Thiotriphosphate) / metabolism
  • Muscle, Skeletal / metabolism
  • Peptide Elongation Factor 2
  • Peptide Elongation Factors / metabolism*
  • Protein Binding
  • Protein Biosynthesis*
  • Rabbits
  • Rats

Substances

  • Actins
  • Peptide Elongation Factor 2
  • Peptide Elongation Factors
  • Guanosine 5'-O-(3-Thiotriphosphate)