The Nuclear RNA ‐binding Protein RBSR 1 Interactome in Trypanosoma cruzi

• Published in: The Journal of eukaryotic microbiology Vol. 66; no. 2; pp. 244 - 253
• Main Authors: Wippel, Helisa H., Malgarin, Juliane S., Martins, Sharon de Toledo, Vidal, Newton M., Marcon, Bruna H., Miot, Hálisson T., Marchini, Fabricio K., Goldenberg, Samuel, Alves, Lysangela R.
• Format: Journal Article
• Language: English
• Published: 01.03.2019
• ISSN: 1066-5234; 1550-7408
• DOI: 10.1111/jeu.12666

Abstract Trypanosoma cruzi , the etiological agent of Chagas disease, has been widely studied, reflecting both its medical importance and the particular features that make this pathogen an attractive model for basic biological studies. The repression of transcripts by messenger ribonucleoprotein ( mRNP ) complexes is an important pathway of post‐transcriptional regulation in eukaryotes, including T. cruzi . RBSR 1 is a serine‐arginine ( SR )‐rich RNA ‐binding protein ( RBP ) in T. cruzi that contains one RNA ‐recognition motif ( RRM ); this protein has a primarily nuclear localization and is developmentally regulated, not being detected in metacyclic trypomastigotes. RBSR 1 interacts with other RBP s, such as UBP 1 and UBP 2, and the nuclear SR ‐protein TRRM 1. Phylogenetic analysis indicated that RBSR 1 is orthologous to the human splicing factor SRSF 7, what might indicate its possible involvement in pre‐ RNA processing. Accordingly, ribonomics data showed the enrichment of sno RNA s and sn RNA s in the RBSR 1 immunoprecipiatation complex, hence reinforcing the supposition that this protein might be involved in RNA processing in the nucleus.