Summary for 9G6Z
| Entry DOI | 10.2210/pdb9g6z/pdb |
| Descriptor | Embryonic developmental protein tofu-6, Protein tofu-1, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | pirna biogenesis, tudor domain, rna binding protein, protein binding |
| Biological source | Caenorhabditis elegans More |
| Total number of polymer chains | 2 |
| Total formula weight | 26875.88 |
| Authors | |
| Primary citation | Podvalnaya, N.,Bronkhorst, A.W.,Lichtenberger, R.,Hellmann, S.,Nischwitz, E.,Falk, T.,Karaulanov, E.,Butter, F.,Falk, S.,Ketting, R.F. piRNA processing by a trimeric Schlafen-domain nuclease. Nature, 622:402-409, 2023 Cited by PubMed Abstract: Transposable elements are genomic parasites that expand within and spread between genomes. PIWI proteins control transposon activity, notably in the germline. These proteins recognize their targets through small RNA co-factors named PIWI-interacting RNAs (piRNAs), making piRNA biogenesis a key specificity-determining step in this crucial genome immunity system. Although the processing of piRNA precursors is an essential step in this process, many of the molecular details remain unclear. Here, we identify an endoribonuclease, precursor of 21U RNA 5'-end cleavage holoenzyme (PUCH), that initiates piRNA processing in the nematode Caenorhabditis 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 a 7-methyl-G cap (mG-cap) and a uracil at position three. We also demonstrate how PUCH interacts with PETISCO, a complex that binds to piRNA precursors, and that this interaction enhances piRNA production in vivo. The identification of PUCH concludes the search for the 5'-end piRNA biogenesis factor in C. elegans and uncovers a type of RNA endonuclease formed by three SLFL proteins. Mammalian Schlafen (SLFN) genes have been associated with immunity, exposing a molecular link between immune responses in mammals and deeply conserved RNA-based mechanisms that control transposable elements. PubMed: 37758951DOI: 10.1093/nar/gkab1038 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.22 Å) |
Structure validation
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