Exon-junction complex association with stalled ribosomes and slow translation-independent disassembly

Olivier Bensaude (), Isabelle Barbosa, Lucia Morillo, Rivka Dikstein and Hervé Hir ()
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Olivier Bensaude: PSL Research University
Isabelle Barbosa: PSL Research University
Lucia Morillo: PSL Research University
Rivka Dikstein: The Weizmann Institute of Science
Hervé Hir: PSL Research University

Nature Communications, 2024, vol. 15, issue 1, 1-14

Abstract: Abstract Exon junction complexes are deposited at exon-exon junctions during splicing. They are primarily known to activate non-sense mediated degradation of transcripts harbouring premature stop codons before the last intron. According to a popular model, exon-junction complexes accompany mRNAs to the cytoplasm where the first translating ribosome pushes them out. However, they are also removed by uncharacterized, translation-independent mechanisms. Little is known about kinetic and transcript specificity of these processes. Here we tag core subunits of exon-junction complexes with complementary split nanoluciferase fragments to obtain sensitive and quantitative assays for complex formation. Unexpectedly, exon-junction complexes form large stable mRNPs containing stalled ribosomes. Complex assembly and disassembly rates are determined after an arrest in transcription and/or translation. 85% of newly deposited exon-junction complexes are disassembled by a translation-dependent mechanism. However as this process is much faster than the translation-independent one, only 30% of the exon-junction complexes present in cells at steady state require translation for disassembly. Deep RNA sequencing shows a bias of exon-junction complex bound transcripts towards microtubule and centrosome coding ones and demonstrate that the lifetimes of exon-junction complexes are transcript-specific. This study provides a dynamic vision of exon-junction complexes and uncovers their unexpected stable association with ribosomes.

Date: 2024
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DOI: 10.1038/s41467-024-48371-5

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