Selected article for: "absence presence and activity assay"
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_39
    Snippet: ubiquitin-ligase activity was dependent on RNA, we performed the ubiquitination assay in the absence or presence of RNase A/T1. Remarkably, treatment with RNase A/T1 severely inhibited in vitro ubiquitination of T7-TRIM25 (Fig. 6d) . Interestingly, RNase A/T1 treated reactions still supported Tim25 monoubiquitination. This could be due to the direct transfer of ubiquitin from Ube2D to TRIM25. These results strongly indicate that RNA constitutes a.....
    Document: ubiquitin-ligase activity was dependent on RNA, we performed the ubiquitination assay in the absence or presence of RNase A/T1. Remarkably, treatment with RNase A/T1 severely inhibited in vitro ubiquitination of T7-TRIM25 (Fig. 6d) . Interestingly, RNase A/T1 treated reactions still supported Tim25 monoubiquitination. This could be due to the direct transfer of ubiquitin from Ube2D to TRIM25. These results strongly indicate that RNA constitutes an important component of the TRIM25 ubiquitin ligase activity.

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