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Elife. 2018 Oct 24;7. pii: e40486. doi: 10.7554/eLife.40486.

Structures of translationally inactive mammalian ribosomes.

Author information

1
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, United States.
2
Department of Cell Biology, Harvard Medical School, Boston, United States.
3
MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.

Abstract

The cellular levels and activities of ribosomes directly regulate gene expression during numerous physiological processes. The mechanisms that globally repress translation are incompletely understood. Here, we use electron cryomicroscopy to analyze inactive ribosomes isolated from mammalian reticulocytes, the penultimate stage of red blood cell differentiation. We identify two types of ribosomes that are translationally repressed by protein interactions. The first comprises ribosomes sequestered with elongation factor 2 (eEF2) by SERPINE mRNA binding protein 1 (SERBP1) occupying the ribosomal mRNA entrance channel. The second type are translationally repressed by a novel ribosome-binding protein, interferon-related developmental regulator 2 (IFRD2), which spans the P and E sites and inserts a C-terminal helix into the mRNA exit channel to preclude translation. IFRD2 binds ribosomes with a tRNA occupying a noncanonical binding site, the 'Z site', on the ribosome. These structures provide functional insights into how ribosomal interactions may suppress translation to regulate gene expression.

KEYWORDS:

electron cryomicroscopy; in vitro reconstitution; molecular biophysics; none; ribosome; structural biology

PMID:
30355441
DOI:
10.7554/eLife.40486
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