4.1 Article

The Nuclear RNA-binding Protein RBSR1 Interactome in Trypanosoma cruzi

Journal

JOURNAL OF EUKARYOTIC MICROBIOLOGY
Volume 66, Issue 2, Pages 244-253

Publisher

WILEY
DOI: 10.1111/jeu.12666

Keywords

Gene expression regulation; immunoprecipitation complex; nucleus

Categories

Funding

  1. Conselho Nacional do Desenvolvimento Cientifico e Tecnologico (CNPq)
  2. Fundacao Oswaldo Cruz (Fiocruz, PAPES)
  3. Fundacao Araucaria
  4. Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)

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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. RBSR1 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. RBSR1 interacts with other RBPs, such as UBP1 and UBP2, and the nuclear SR-protein TRRM1. Phylogenetic analysis indicated that RBSR1 is orthologous to the human splicing factor SRSF7, what might indicate its possible involvement in pre-RNA processing. Accordingly, ribonomics data showed the enrichment of snoRNAs and snRNAs in the RBSR1 immunoprecipiatation complex, hence reinforcing the supposition that this protein might be involved in RNA processing in the nucleus.

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