Author: Nila Roy Choudhury; Gregory Heikel; Maryia Trubitsyna; Peter Kubik; Jakub Stanislaw Nowak; Shaun Webb; Sander Granneman; Christos Spanos; Juri Rappsilber; Alfredo Castello; Gracjan Michlewski
Title: RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain and is required for ubiquitination Document date: 2017_10_9
ID: ifla4aix_42
Snippet: The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/200410 doi: bioRxiv preprint chimeric TRIM25 proteins, apart from T7-TRIM25ΔRBD_src, showed efficient binding to RNA ( Fig. 7d-7e) . Notably, we did not observe modified bands for TRIM25 in the RNA pulldown assays because the total protein amounts loaded on the gel were one order of magnitude lower than those in the overexpression.....
Document: The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/200410 doi: bioRxiv preprint chimeric TRIM25 proteins, apart from T7-TRIM25ΔRBD_src, showed efficient binding to RNA ( Fig. 7d-7e) . Notably, we did not observe modified bands for TRIM25 in the RNA pulldown assays because the total protein amounts loaded on the gel were one order of magnitude lower than those in the overexpression experiments. To our surprise, there was a strong positive correlation (correlation coefficient 0.87, p-value 0.01) between protein modification and RNA pull-down efficiencies (Fig. 7f) . Altogether, these results imply that RNA-binding is an important element in TRIM25 ubiquitination efficiency and suggest that many other TRIM proteins with the PRY/SPRY domain could harbor yet uncharacterized RNA-binding potential.
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