Rabbit Anti-Human EEF1A1 (a.a. 144-462) Polyclonal antibody

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 * eEF1B alpha 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. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Pseudouridine (psi) is the most abundant post-transcriptional RNA modification, yet little is known about its prevalence, mechanism and function in mRNA. Here, we performed quantitative MS analysis and show that psi is much more prevalent (psi/U ratio similar to 0.2-0.6%) in mammalian mRNA than previously believed. We developed N-3-CMC-enriched pseudouridine sequencing (CeU-Seq), a selective chemical labeling and pulldown method, to identify 2,084 psi sites within 1,929 human transcripts, of which four (in ribosomal RNA and EEF1A1 mRNA) are biochemically verified. We show that hPUS1, a known psi synthase, acts on human mRNA; under stress, CeU-Seq demonstrates inducible and stress-specific mRNA pseudouridylation. Applying CeU-Seq to the mouse transcriptome revealed conserved and tissue-specific pseudouridylation. Collectively, our approaches allow comprehensive analysis of transcriptome-wide pseudouridylation and provide tools for functional studies of psi-mediated epigenetic regulation.