Dynamic association of human Ebp1 with the ribosome

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...

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Bibliographic Details
Published in:RNA (Cambridge) 2021-04, Vol.27 (4), p.411-419
Main Authors: Bhaskar, Varun, Desogus, Jessica, Graff-Meyer, Alexandra, Schenk, Andreas D, Cavadini, Simone, Chao, Jeffrey A
Format: Article
Language:English
Subjects:
Adaptor Proteins, Signal Transducing - chemistry
Adaptor Proteins, Signal Transducing - genetics
Adaptor Proteins, Signal Transducing - metabolism
Aminopeptidase
Binding Sites
Cryoelectron Microscopy
EBP1 protein
Homology
Humans
Macromolecules
Methionine
Models, Molecular
Protein Binding
Protein biosynthesis
Protein Biosynthesis - drug effects
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Protein Synthesis Inhibitors - pharmacology
Puromycin
Puromycin - pharmacology
Ribosomal proteins
Ribosomal Proteins - chemistry
Ribosomal Proteins - genetics
Ribosomal Proteins - metabolism
Ribosomes
Ribosomes - chemistry
Ribosomes - genetics
Ribosomes - metabolism
RNA, Ribosomal - chemistry
RNA, Ribosomal - genetics
RNA, Ribosomal - metabolism
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
rRNA 28S
Thermodynamics
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Summary: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.
ISSN:1355-8382
1469-9001
DOI:10.1261/rna.077602.120