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Dynamic association of human Ebp1 with the ribosome.

Bashkar, Varun, Desogus, Jessica, Graff-Meyer, Alexandra, Schenk, Andreas, Cavadini, Simone and Chao, Jeffrey A (2021) Dynamic association of human Ebp1 with the ribosome. RNA (New York, N.Y.), 27 (4). pp. 411-419. ISSN 1469-9001


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 to 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.

Item Type: Article
Date Deposited: 12 Aug 2021 00:45
Last Modified: 12 Aug 2021 00:45


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