FEBS Letters | |
Interactions of eukaryotic elongation factor 2 with actin: A possible link between protein synthetic machinery and cytoskeleton | |
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
【 预 览 】
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