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10.1101/2021.06.14.448452

http://scihub22266oqcxt.onion/10.1101/2021.06.14.448452
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34159327!8219091!34159327
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suck abstract from ncbi


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pmid34159327      bioRxiv 2021 ; ä (ä): ä
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  • Double-stranded RNA drives SARS-CoV-2 nucleocapsid protein to undergo phase separation at specific temperatures #MMPMID34159327
  • Roden CA; Dai Y; Seim I; Lee M; Sealfon R; McLaughlin GA; Boerneke MA; Iserman C; Wey SA; Ekena JL; Troyanskaya OG; Weeks KM; You L; Chilkoti A; Gladfelter AS
  • bioRxiv 2021[Jun]; ä (ä): ä PMID34159327show ga
  • Betacoronavirus SARS-CoV-2 infections caused the global Covid-19 pandemic. The nucleocapsid protein (N-protein) is required for multiple steps in the betacoronavirus replication cycle. SARS-CoV-2-N-protein is known to undergo liquid-liquid phase separation (LLPS) with specific RNAs at particular temperatures to form condensates. We show that N-protein recognizes at least two separate and distinct RNA motifs, both of which require double-stranded RNA (dsRNA) for LLPS. These motifs are separately recognized by N-protein's two RNA binding domains (RBDs). Addition of dsRNA accelerates and modifies N-protein LLPS in vitro and in cells and controls the temperature condensates form. The abundance of dsRNA tunes N-protein-mediated translational repression and may confer a switch from translation to genome packaging. Thus, N-protein's two RBDs interact with separate dsRNA motifs, and these interactions impart distinct droplet properties that can support multiple viral functions. These experiments demonstrate a paradigm of how RNA structure can control the properties of biomolecular condensates.
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