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Recruitment of mRNAs to P granules by condensation with intrinsically-disordered proteins.


ABSTRACT: RNA granules are protein/RNA condensates. How specific mRNAs are recruited to cytoplasmic RNA granules is not known. Here, we characterize the transcriptome and assembly of P granules, RNA granules in the C. elegans germ plasm. We find that P granules recruit mRNAs by condensation with the disordered protein MEG-3. MEG-3 traps mRNAs into non-dynamic condensates in vitro and binds to ~500 mRNAs in vivo in a sequence-independent manner that favors embryonic mRNAs with low ribosome coverage. Translational stress causes additional mRNAs to localize to P granules and translational activation correlates with P granule exit for two mRNAs coding for germ cell fate regulators. Localization to P granules is not required for translational repression but is required to enrich mRNAs in the germ lineage for robust germline development. Our observations reveal similarities between P granules and stress granules and identify intrinsically-disordered proteins as drivers of RNA condensation during P granule assembly.

SUBMITTER: Lee CS 

PROVIDER: S-EPMC7007223 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature

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Recruitment of mRNAs to P granules by condensation with intrinsically-disordered proteins.

Lee Chih-Yung S CS   Putnam Andrea A   Lu Tu T   He ShuaiXin S   Ouyang John Paul T JPT   Seydoux Geraldine G  

eLife 20200124


RNA granules are protein/RNA condensates. How specific mRNAs are recruited to cytoplasmic RNA granules is not known. Here, we characterize the transcriptome and assembly of P granules, RNA granules in the <i>C. elegans</i> germ plasm. We find that P granules recruit mRNAs by condensation with the disordered protein MEG-3. MEG-3 traps mRNAs into non-dynamic condensates in vitro and binds to ~500 mRNAs in vivo in a sequence-independent manner that favors embryonic mRNAs with low ribosome coverage.  ...[more]

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