Dynamic association of human Ebp1 with the ribosome
- Varun Bhaskar1,
- Jessica Desogus2,
- Alexandra Graff-Meyer2,
- Andreas D. Schenk2,
- Simone Cavadini2 and
- Jeffrey A. Chao3,4
- 1 The Friedrich Miescher Institute for Biomedical Research;
- 2 Friedrich Miescher Institute for Biomedical Research;
- 3 The Friedrich Miescher Institute (FMI) in Basel
- ↵* Corresponding author; email: jeffrey.chao{at}fmi.ch
Abstract
Ribosomes are the macromolecular machines at the heart of protein synthesis, however, their function can be modulated by a variety of additional protein factors that directly interact with them. Here, we report the cryo-EM structure of human Ebp1 (p48 isoform) bound to the human 80S ribosome at 3.3 Å resolution. Ebp1 binds in the vicinity of the peptide exit tunnel on the 80S ribosome and this binding is enhanced upon puromycin-mediated translational inhibition. The association of Ebp1 with the 80S ribosome centers around its interaction with ribosomal proteins eL19 and uL23 and the 28S rRNA. Further analysis of the Ebp1¬–ribosome complex suggests that Ebp1 can rotate around its insert domain, which may enable it assume a wide range of conformations while maintaining its interaction with the ribosome. Structurally, Ebp1 shares homology with the methionine aminopeptidase 2 family of enzymes, therefore, this inherent flexibility may also be conserved.
- Received August 12, 2020.
- Accepted January 2, 2021.
- Published by Cold Spring Harbor Laboratory Press for the RNA Society
This article, published in RNA, is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.
