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- W3131773397 abstract "The germline of sexually reproducing animals contains conserved non-membrane-bound compartments containing proteins and RNAs called ‘germ granules’. Mutations that disrupt assembly of germ granules result in sterility. A germ granule in C. elegans, called ‘P granules’, has been shown to assemble via liquid-liquid phase separation (LLPS) of proteins and RNAs from the surrounding cytoplasm in adult gonads. Approximately 85% of proteins that concentrate in P granules are involved in different aspects of RNA metabolism, suggesting that the P granule phase could process and/or store RNA. To elucidate the underlying molecular mechanisms, it is important to understand the biophysical nature of the P granule phase. Specifically, the molecular and structural determinants that regulate diffusion rates within the P granule phase remains unclear. We used an in vitro reconstitution-based approach to address this question and studied the LLPS behavior of the protein PGL-3, one of the most abundant proteins in P granules, in presence and absence of other P granule components. We found that a folded domain of PGL-3 drives LLPS, and dynamics within phase-separated condensates correlates with alpha-helicity of the folded domain. We investigated the effect on dynamics in condensates when other components of P granules are added to condensates of PGL-3. Our findings suggest that the complex composition of P granules favor fast dynamics within the phase." @default.
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- W3131773397 date "2021-02-01" @default.
- W3131773397 modified "2023-09-27" @default.
- W3131773397 title "Structural and Molecular Determinants of Dynamics in P Granules of C. Elegans" @default.
- W3131773397 doi "https://doi.org/10.1016/j.bpj.2020.11.479" @default.
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