GSE106934
Ribonomic identification of mRNAs associated with RNA binding proteins TcRBP7 and TcRBP40 from Trypanosoma cruzi
TcRBP7 and TcRBP40 proteins are adjacent paralogs in T. cruzi with a conserved RRM structure and similar protein localization at specific foci at the posterior region. We identified their targets in order to compare their function, infering about the evolutionary implication of regulatory proteins duplication. Surprisingly, the mRNA targets co-immunoprecipitated with each RBP were distinct, pointing to a subfunctionalization outcome. In addition, TcRBP40 bound to transcripts of mucin-associated surface proteins (MASPs), which work in T. cruzi's host-cell invasion. Both proteins recognize similar putative target sequences despite showing different binding behavior. This study shows the rearrangement potential in gene expression networks in the face of duplication of regulatory proteins. Overall design: mRNAs isolated in vivo by co-immunoprecipitation of GFP-tagged TcRBP7 and TcRBP40, in triplicates. GFP-tag alone was used as a control, in triplicate. mRNAs were sequenced in SOLiD4 System.