Selected article for: "presence absence and RNase T1 treatment"
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_45
    Snippet: The copyright holder for this preprint (which was not peer-reviewed) is the author/funder.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 could be explained by increased concentrations of the proteins from the ubiquitination pathway and ZAP stimulatory activity towards TRIM25 . Finally, to see if TRIM25 E3 ubiquitin ligase activity towards ZAP was dependent on RNA, we performed the ubiquitination assay in the absence or presence of RNase .....
    Document: The copyright holder for this preprint (which was not peer-reviewed) is the author/funder.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 could be explained by increased concentrations of the proteins from the ubiquitination pathway and ZAP stimulatory activity towards TRIM25 . Finally, to see if TRIM25 E3 ubiquitin ligase activity towards ZAP was dependent on RNA, we performed the ubiquitination assay in the absence or presence of RNase A/T1. Importantly, the treatment with RNase A/T1 severely inhibited in vitro T7-ZAP ubiquitination by T7-TRIM25 (Fig. 8c) .

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