| Literature DB >> 25862498 |
Dmytro O Vlasenko1, Oleksandra V Novosylna1, Boris S Negrutskii2, Anna V El'skaya1.
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.Entities:
Keywords: Actin bundling; Eukaryotic translation; Translation elongation factor
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Year: 2015 PMID： 25862498 DOI： 10.1016/j.febslet.2015.03.030
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124