RT Journal Article
SR Electronic
T1 RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain and is required for ubiquitination
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 200410
DO 10.1101/200410
A1 Nila Roy Choudhury
A1 Gregory Heikel
A1 Maryia Trubitsyna
A1 Peter Kubik
A1 Jakub Stanislaw Nowak
A1 Shaun Webb
A1 Sander Granneman
A1 Christos Spanos
A1 Juri Rappsilber
A1 Alfredo Castello
A1 Gracjan Michlewski
YR 2017
UL http://biorxiv.org/content/early/2017/10/09/200410.abstract
AB TRIM25 is a novel RNA-binding protein and a member of the Tripartite Motif (TRIM) family of E3 ubiquitin ligases, which plays a pivotal role in the innate immune response. Almost nothing is known about its RNA-related roles in cell biology. Furthermore, its RNA-binding domain has not been characterized. Here, we reveal that RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain, which we postulate to be a novel RNA-binding domain. Using CLIP-seq and SILAC-based co-immunoprecipitation assays, we uncover TRIM25’s endogenous RNA targets and protein binding partners. Finally, we show that the RNA-binding activity of TRIM25 is important for its ubiquitin ligase function. These results reveal new insights into the molecular roles and characteristics of RNA-binding E3 ubiquitin ligases and demonstrate that RNA could be an essential factor for their biological functions.