Author: Aravinth Kumar Jayabalan; Diane E. Griffin; Anthony K. L. Leung
Title: Alphavirus nsP3 ADP-ribosylhydrolase Activity Disrupts Stress Granule Formation Document date: 2019_6_20
ID: n8sjpcbs_29
Snippet: The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/629881 doi: bioRxiv preprint Page 13 nsP3 G32E mutant co-localized with FUS R495X as well as SG markers G3BP1 and eIF3b (Fig. 3c and data not shown). Given that the full length nsP3 protein possesses the G3BP-binding HVD, the reduction of SG-like aggregates was accompanied by formation of foci containing both nsP3 and G3BP1 (Fig. 3.....
Document: The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/629881 doi: bioRxiv preprint Page 13 nsP3 G32E mutant co-localized with FUS R495X as well as SG markers G3BP1 and eIF3b (Fig. 3c and data not shown). Given that the full length nsP3 protein possesses the G3BP-binding HVD, the reduction of SG-like aggregates was accompanied by formation of foci containing both nsP3 and G3BP1 (Fig. 3c) . On the contrary, co-transfection of nsP3 MD alone decreased formation of these aggregates by two-fold without the formation of nsP3/G3BP1 foci (Fig. 3c, e) , further pointing to the importance of the MD ADP-ribosylhydrolase activity.
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