INTERACTIONS OF EUKARYOTIC ELONGATION-FACTOR-2 WITH ACTIN - A POSSIBLE LINK BETWEEN PROTEIN SYNTHETIC MACHINERY AND CYTOSKELETON


BEKTAS M., NURTEN R., GUREL Z., SAYERS Z., BERMEK E.

FEBS LETTERS, vol.356, no.1, pp.89-93, 1994 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 356 Issue: 1
  • Publication Date: 1994
  • Doi Number: 10.1016/0014-5793(94)01239-3
  • Journal Name: FEBS LETTERS
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.89-93
  • Istanbul University Affiliated: Yes

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 mu M. 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.