Interactions of eukaryotic elongation factor 2 with actin: a possible link between protein synthetic machinery and cytoskeleton.
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.
Bektaş
M
M
Department of Biophysics, Istanbul University, Istanbul Faculty of Medicine, Turkey.
Nurten
R
R
Gürel
Z
Z
Sayers
Z
Z
Bermek
E
E
D000199:Actins / Q000378:metabolism*; D000818:Animals; D003599:Cytoskeleton / Q000378:metabolism*; D016244:Guanosine 5'-O-(3-Thiotriphosphate) / Q000378:metabolism; D018482:Muscle, Skeletal / Q000378:metabolism; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors / Q000378:metabolism*; D011485:Protein Binding; D014176:Protein Biosynthesis; D011817:Rabbits; D051381:Rats
D000199:Actins; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors; D016244:Guanosine 5'-O-(3-Thiotriphosphate)