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Exon Junction Complex (EJC) proteins bind nascent transcripts independently of pre-mRNA splicing in Drosophila melanogaster

ABSTRACT: ChIP-seq Y14

ORGANISM(S): Drosophila melanogaster

PROVIDER: GSE84595 | GEO | 2016/11/22

SECONDARY ACCESSION(S): PRJNA330543

REPOSITORIES: GEO

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Exon junction complex proteins bind nascent transcripts independently of pre-mRNA splicing in <i>Drosophila melanogaster</i>.

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Chemical inhibition of exon junction complex assembly impairs mRNA localization and neural stem cells ciliogenesis

Project description:The Exon Junction Complex (EJC) is formed by the essential eIF4A3, MAGOH and Y14 core proteins. It is universally deposited during splicing at exon-exon junctions. The EJC is known to impact almost every post-transcriptional regulatory step throughout the life of mRNAs including their modifications, splicing, decay and trafficking. Its dysregulation leads to neurodevelopmental pathologies. Here we show that EJC-i, a compound known to block the ATPase activity of eIF4A3, inhibits de novo EJC assembly. EJC-i and targeted knockdown of either eIF4A3 or Y14 core EJC subunits lead to very similar phenotypes by impacting the destiny of mRNAs due to alterations in alternative splicing, nonsense-mediated mRNA decay, genome-wide m6A methylation and proper intracellular addressing of specific transcripts, in particular to the centrosome. Both EJC impairment methods disrupt the centrosome structure that might be responsible for mitotic arrest at prometaphase. However, as a small molecule that readily diffuses into cells, EJC-i is a particularly attractive easy to use and versatile tool to investigate EJC functions in live cells or whole organism that are not prone to genetic manipulation. Indeed, this property was used to disrupt ciliogenesis in primary neural stem cells.

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Magoh, Y14, eIF4AIII interactomes by TurboID proximity labelling provide no evidence for a canonical EJC in (almost) intron-less trypanosomatids

Project description:In metazoans, mRNA quality is tightly monitored from transcription to translation. A key role lies with the exon junction complex (EJC) that is placed upstream of the exon-exon junction after splicing. The EJC inner core is composed of Magoh, Y14, eIF4AIII and BTZ and the outer core of proteins involved in mRNA splicing (CWC22), export (Yra1), translation (PYM) and non-sense mediated decay (NMD, UPF1/2/3). The protozoan parasite Trypanosoma brucei encodes only two genes with introns, but all mRNAs are processed by trans-splicing. The presence of the three core EJC proteins and a potential BTZ homologue (Rbp25) in trypanosomes has been suggested as an adaptation of the EJC function to mark trans-spliced mRNAs. Here we explore the interactome of Magoh, Y14, eIF4AIII in T. brucei by TurboID proximity labelling.

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