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In  C .  elegans , efficient RNA silencing requires small RNA amplification mediated by RNA-dependent RNA polymerases (RdRPs). RRF-1, an RdRP, and other  Mutator  complex proteins localize to  Mutator  foci, which are perinuclear germline foci that associate with nuclear pores and P granules to facilitate small RNA amplification. The  Mutator  complex protein MUT-16 is critical for  Mutator  foci assembly. By analyzing small deletions of MUT-16, we identify specific regions of the protein that recruit other  Mutator  complex components and demonstrate that it acts as a scaffolding protein. We further determine that the C-terminal region of MUT-16, a portion of which contains predicted intrinsic disorder, is necessary and sufficient to promote  Mutator  foci formation. Finally, we establish that MUT-16 foci have many properties consistent with a phase-separated condensate and propose that  Mutator  foci form through liquid-liquid phase separation of MUT-16. P granules, which contain additional RNA silencing proteins, have previously been shown to have liquid-like properties. Thus, RNA silencing in  C .  elegans  germ cells may rely on multiple phase-separated compartments through which sorting, processing, and silencing of mRNAs occurs.

plos genetics

Distinct regions of the intrinsically disordered protein MUT-16 mediate assembly of a small RNA amplification complex and promote phase separation of Mutator foci