RNA-protein condensates

Argonaute proteins often to not work alone--in many cases Argonautes recruit additional repressive factors to RNA transcripts identified for silencing. We recently found that multivalent interactions between Argonaute2 and the protein TNRC6B drive condensation of phase-separated droplets (green spots in image to the right). Condensation is accompanied by accelerated degradation of RNAs targeted for silencing by Argonaute2. We are working to determine the molecular mechanism of phase separation, the structural and biochemical properties of the condensed protein/RNA material, and how phase separation of Argonaute-interacting components intersects with other membraneless organelles involved in RNA metabolism.