title: Truncation of the A,A(∗),A' helices segment impairs the actin bundling activity of mammalian eEF1A1.
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.
authors: Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, 150 Zabolotnogo Str., 03143 Kiev, Ukraine.
authors: Dmytro O
authors: DO
authors: Vlasenko
authors: Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, 150 Zabolotnogo Str., 03143 Kiev, Ukraine.
authors: Oleksandra V
authors: OV
authors: Novosylna
authors: Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, 150 Zabolotnogo Str., 03143 Kiev, Ukraine. Electronic address: negrutskii@imbg.org.ua.
authors: Boris S
authors: BS
authors: Negrutskii
authors: Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, 150 Zabolotnogo Str., 03143 Kiev, Ukraine.
authors: Anna V
authors: AV
authors: El'skaya
mesh_terms: D000199:Actins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D020648:Peptide Elongation Factor 1 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D011817:Rabbits; D017384:Sequence Deletion
chemical_list: D000199:Actins; D020648:Peptide Elongation Factor 1
keywords: Actin bundling; Eukaryotic translation; Translation elongation factor