piRNA processing by a trimeric Schlafen-domain nuclease

Author:

Podvalnaya Nadezda,Bronkhorst Alfred W.ORCID,Lichtenberger Raffael,Hellmann Svenja,Nischwitz EmilyORCID,Falk TorbenORCID,Karaulanov Emil,Butter FalkORCID,Falk SebastianORCID,Ketting René F.ORCID

Abstract

AbstractTransposable elements are genomic parasites that expand within and spread between genomes1. Piwi proteins control transposon activity, notably in the germline2,3. These proteins recognize their targets through small RNA co-factors named piRNAs, making piRNA biogenesis a key specificity-determining step in this crucial genome immunity system. While the processing of piRNA precursors is an essential step in this process, many molecular details of this process remain unknown. We identify a novel endoribonuclease, PUCH, that initiates piRNA processing in the nematodeCaenorhabditis elegans. Genetic and biochemical studies show that PUCH, a trimer of Schlafen-like-domain proteins (SLFL proteins), executes 5’-end piRNA precursor cleavage. PUCH-mediated processing strictly requires an m7G-Cap and a uracil at position three. We also demonstrate how PUCH interacts with PETISCO, a complex that binds piRNA precursors4, and that this interaction enhances piRNA productionin vivo. The identification of PUCH completes the repertoire ofC. eleganspiRNA biogenesis factors and uncovers a novel type of RNA endonuclease formed by three SLFL proteins. Mammalian Schlafen (Slfn) genes have been associated with immunity responses5, exposing a thus far unknown molecular link between immune responses in mammals and deeply conserved RNA-based mechanisms that control transposable elements.

Publisher

Cold Spring Harbor Laboratory

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