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_2
Snippet: binding activity in vitro ( Fig. 1c-1d ). EMSA analysis with increasing amounts of His-TRIM25ΔRBD revealed no shift in the pre-let-7a-1 substrate (Fig. 1c) . Likewise, RNA pulldown assays in HeLa cell extracts showed that endogenous and T7-tagged TRIM25 were efficiently pulled down with pre-let-7a-1, whereas T7-tagged TRIM25ΔRBD was not (Fig. 1e ). These results strongly indicate that the TRIM25 PRY/SPRY domain harbors its RNAbinding activity.....
Document: binding activity in vitro ( Fig. 1c-1d ). EMSA analysis with increasing amounts of His-TRIM25ΔRBD revealed no shift in the pre-let-7a-1 substrate (Fig. 1c) . Likewise, RNA pulldown assays in HeLa cell extracts showed that endogenous and T7-tagged TRIM25 were efficiently pulled down with pre-let-7a-1, whereas T7-tagged TRIM25ΔRBD was not (Fig. 1e ). These results strongly indicate that the TRIM25 PRY/SPRY domain harbors its RNAbinding activity.
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