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_58
Snippet: forty-three of them have PRY/SPRY domains (subfamilies C-I and C-IV). Although there is a high degree of similarity between them, only TRIM25 (from TRIM proteins containing PRY/SPRY) was identified in HeLa (Castello et al., 2012) and mESC (Kwon et al., 2013) screens for proteins that bind to RNAs. This could reflect a lack of saturation of RNA-capture screens or lack of expression of many other PRY/SPRY-containing TRIM proteins in the cell lines .....
Document: forty-three of them have PRY/SPRY domains (subfamilies C-I and C-IV). Although there is a high degree of similarity between them, only TRIM25 (from TRIM proteins containing PRY/SPRY) was identified in HeLa (Castello et al., 2012) and mESC (Kwon et al., 2013) screens for proteins that bind to RNAs. This could reflect a lack of saturation of RNA-capture screens or lack of expression of many other PRY/SPRY-containing TRIM proteins in the cell lines used for these assays. Interestingly, another protein from the TRIM family, TRIM71, was shown to use its NHL, but not its CC, domain to bind RNA (Kwon et al., 2013; Loedige All rights reserved. No reuse allowed without permission.
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