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

FEBS Letters

Bektaş, M.¹  Sayers, Z.²  Bermek, E.¹  Nurten, R.¹  Gürel, Z.¹ 

[1] Department of Biophysics, Instanbul University Faculty of Medicine, 34390 Çapa-Istanbul, Turkey;TÜBITAK Marmara Research Center, 41470 Gebze-Kocaeli Turkey

关键词: Elongation factor 2;    Actin;    Cytoskeleton;    Protein synthesis;    ADPR-EP-2;    adenosine diphosphate ribosylated-eukaryotic elongation factor 2;    EF-1α;    eukaryotic elongation factor 1α;    F-actin;    filamentous actin;    G-actin;    globular actin monomer;    ABP;    actin- binding protein;    DT;    diphtheria toxin;    DTT;    dithiothreitol;    GTPγS;    guanosine-5′-O-(3-thiotriphosphate);    NAD;    nicotinamide adenine dinucleotide;    NEM;    N-ethylmaleimide;    ME;    2-mercaptoethanol;    SDS-PAGE;    sodium dodecylsulfate-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(94)01239-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown