Serge Urbach

Abstract The HSP90/R2TP quaternary chaperone assembles key cellular machines, including the three nuclear RNA polymerases and many non-coding RNPs. Here, we characterize the RNAs associated with R2TP and find that it binds many proteins co-translationally. Its co-translational interactome reveals potential clients and distinguishes clients bound only co-translationally, only post-translationally, or both.

Abstract Interferon-induced antiviral proteins act on the first line of defence against viruses, including influenza A virus (IAV). Among those, the short isoform of Nuclear Receptor Coactivator 7 (NCOA7-AS) has been shown to inhibit IAV entry and more especially the fusion between endosomal and viral membranes. Ectopic expression of NCOA7-AS leads to the increased acidification of the endolysosomal pathway, putatively through NCOA7-AS interaction with the vacuolar ATPase (V-ATPase).