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...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Bercovich, N., Levin, M.J., Clayton, C., Vazquez, M.P.
Formato: JOUR
Materias:
EJC
Mago
mRNA export
Trypanosomes
Y14
heterodimer
messenger RNA
protozoal protein
article
evolutionary homology
exon
in vivo study
nonhuman
nucleotide sequence
priority journal
protein domain
RNA sequence
RNA splicing
trans splicing
Trypanosoma
yeast
Amino Acid Sequence
Animals
Exons
Humans
Molecular Sequence Data
Protein Binding
Protozoan Proteins
RNA Splicing
RNA Transport
RNA-Binding Proteins
Sequence Alignment
Trypanosoma brucei brucei
Trypanosoma cruzi
Trypanosomiasis
Animalia
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_01666851_v166_n2_p190_Bercovich
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario: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. © 2009 Elsevier B.V. All rights reserved.

Ejemplares similares