Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5915917 | Molecular and Biochemical Parasitology | 2009 | 4 Pages |
Abstract
In animal cells, the exon junction complex (EJC) is deposited onto mRNAs during the second step of splicing, 20-24Â 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 5â² 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.
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Authors
Natalia Bercovich, Mariano J. Levin, Christine Clayton, Martin P. Vazquez,