Premium
The Nuclear RNA ‐binding Protein RBSR 1 Interactome in Trypanosoma cruzi
Author(s) -
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.
Publication year - 2018
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/jeu.12666
Subject(s) - biology , interactome , trypanosoma cruzi , rna binding protein , rna , ribonucleoprotein , small nucleolar rna , rna splicing , rna recognition motif , sr protein , microbiology and biotechnology , genetics , non coding rna , computational biology , gene , parasite hosting , world wide web , computer science
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.