Truncation of the A,A∗,A' helices segment impairs the actin bundling activity of mammalian eEF1A1

Abstract

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.