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A molecular network of conserved factors keeps ribosomes dormant in the egg

ABSTRACT:

SUBMITTER: David Haselbach

PROVIDER: EMPIAR-11274 | biostudies-other |

REPOSITORIES: biostudies-other

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A molecular network of conserved factors keeps ribosomes dormant in the egg.

Leesch Friederike F Lorenzo-Orts Laura L Pribitzer Carina C Grishkovskaya Irina I Roehsner Josef J Chugunova Anastasia A Matzinger Manuel M Roitinger Elisabeth E Belačić Katarina K Kandolf Susanne S Lin Tzi-Yang TY Mechtler Karl K Meinhart Anton A Haselbach David D Pauli Andrea A

Nature 20230118 7945

Ribosomes are produced in large quantities during oogenesis and are stored in the egg. However, the egg and early embryo are translationally repressed<sup>1-4</sup>. Here, using mass spectrometry and cryo-electron microscopy analyses of ribosomes isolated from zebrafish (Danio rerio) and Xenopus laevis eggs and embryos, we provide molecular evidence that ribosomes transition from a dormant state to an active state during the first hours of embryogenesis. Dormant ribosomes are associated with fou ...[more]

PMID: 36653451

Similar Datasets

A molecular network of conserved factors keeps ribosomes dormant in the egg

Project description:Ribosomes are produced in large quantities during oogenesis and stored in the egg. However, the egg and early embryo are translationally inactive. How translation is activated during embryogenesis is poorly understood. Using mass-spectrometry and cryo-EM analyses of ribosomes isolated from zebrafish and Xenopus eggs and embryos, we find that ribosomes transition from a dormant to an active state during the first hours of embryogenesis. Dormant ribosomes are associated with four factors that form two modules: a Habp4-eEF2 module that stabilizes ribosome levels and a Dap1b/Dapl1-eIF-5a module that represses translation. Dap/Dap1b is a newly discovered translational inhibitor that stably inserts into the polypeptide exit tunnel. Thus, a developmentally programmed, unique ribosome state plays a key role in ribosome storage and translational repression in the egg.

2022-11-03 | PXD026866 | Pride

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Project description:Ribosomes frequently stall during mRNA translation, resulting in the context-dependent activation of quality control pathways to maintain proteostasis. However, surveillance mechanisms that specifically respond to stalled ribosomes with an occluded A site have not been identified. We discovered that the elongation factor-1α (eEF1A) inhibitor, ternatin-4, triggers the ubiquitination and degradation of eEF1A on stalled ribosomes. Using a chemical genetic approach, we unveiled a signaling network comprising two E3 ligases, RNF14 and RNF25, which are required for eEF1A degradation. Quantitative proteomics revealed the RNF14 and RNF25-dependent ubiquitination of eEF1A and a discrete set of ribosomal proteins. The ribosome collision sensor GCN1 plays an essential role by engaging RNF14, which directly ubiquitinates eEF1A. The site-specific, RNF25-dependent ubiquitination of the ribosomal protein RPS27A/eS31 provides a second essential signaling input. Our findings illuminate a ubiquitin signaling network that monitors the ribosomal A site and promotes the degradation of stalled translation factors, including eEF1A and the termination factor eRF1.

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An E3 ligase network engages GCN1 to promote degradation of translation factors on stalled ribosomes

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