Identification of core components of the exon junction complex in trypanosomes.

In animal cells, the exon junction complex (EJC) is deposited onto mRNAs during the second step of splicing, 20-24 nt upstream of the exon-exon junction. The EJC core contains four proteins: Mago, Y14, eIF4AIII and Btz. In trypanosomes, cis-splicing is very rare but all mRNAs are subject to 5'trans-splicing of a 39-nt RNA sequence. Here we show that trypanosomes have a conserved Mago and a divergent Y14 protein, but we were unable to identify a Btz orthologue. We demonstrate that Mago and Y14 form a stable heterodimer using yeast two hybrid analyses. We also show that this complex co-purifies in vivo in trypanosomes with a protein containing an NTF2 domain, typically involved in mRNA transport.

• Publication year

  2009

• Venue

  Molecular and biochemical parasitology (Print)

• Publication date

  2009-08-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/j.molbiopara.2009.03.008PMID 19450736
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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