Abstract Translation elongation factor eEF1A is a G-protein which has a crucial role in the ribosomal polypeptide elongation and possesses a number of non-translational functions. Here, we show that the A,A∗,A' helices segment of mammalian eEF1A is dispensable for the eEF1A∗ eEF1Bα complex formation. The A,A∗,A' helices region did not interact with actin; however, its removal eliminates the actin bundling activity of eEF1A, probably due to the destruction of a dimeric structure of eEF1A. The translation function of monomers and the actin-bundling function of dimers of mammalian eEF1A is suggested.
Vlasenko, D. O., Novosylna, O. V., Negrutskii, B. S., & El’skaya, A. V. (2015). Truncation of the A,A∗,A’ helices segment impairs the actin bundling activity of mammalian eEF1A1. FEBS Letters, 589(11), 1187–1193. https://doi.org/10.1016/j.febslet.2015.03.030