RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain and is required for ubiquitination

TRIM25 E3 ubiquitin ligase is a new RNA-binding protein. We present the first high-throughput analysis of the molecular interactomes of TRIM25. We show that TRIM25 is a bona fide RNA-binding protein that interacts with numerous coding and non-coding transcripts. This suggests that TRIM25 could play a role in the regulation of RNA metabolism. We performed UV crosslinking and immunoprecipitations in HeLa cells transiently expressing T7-tagged TRIM25, followed by high-throughput sequencing of TRIM25-associated RNAs (CLIP-seq). This was done in three biological replicates. Please note that each processed data is genrated from Trim25 and Mock dataset pairs (e.g. e.g.Trim25_exp1_significant_clusters.gtf.gz generated from both Trim25 CLIP-seq exp1 and Mock CLIP-seq exp1 ) and linked to the corresponding Trim25 CLIP-seq sample records.