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-Structure paper
| Title | Structural basis of rotavirus RNA chaperone displacement and RNA annealing. |
|---|---|
| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 118, Issue 41, Year 2021 |
| Publish date | Oct 12, 2021 |
 Authors | Jack P K Bravo / Kira Bartnik / Luca Venditti / Julia Acker / Emma H Gail / Alice Colyer / Chen Davidovich / Don C Lamb / Roman Tuma / Antonio N Calabrese / Alexander Borodavka /     |
| PubMed Abstract | Rotavirus genomes are distributed between 11 distinct RNA molecules, all of which must be selectively copackaged during virus assembly. This likely occurs through sequence-specific RNA interactions ...Rotavirus genomes are distributed between 11 distinct RNA molecules, all of which must be selectively copackaged during virus assembly. This likely occurs through sequence-specific RNA interactions facilitated by the RNA chaperone NSP2. Here, we report that NSP2 autoregulates its chaperone activity through its C-terminal region (CTR) that promotes RNA-RNA interactions by limiting its helix-unwinding activity. Unexpectedly, structural proteomics data revealed that the CTR does not directly interact with RNA, while accelerating RNA release from NSP2. Cryo-electron microscopy reconstructions of an NSP2-RNA complex reveal a highly conserved acidic patch on the CTR, which is poised toward the bound RNA. Virus replication was abrogated by charge-disrupting mutations within the acidic patch but completely restored by charge-preserving mutations. Mechanistic similarities between NSP2 and the unrelated bacterial RNA chaperone Hfq suggest that accelerating RNA dissociation while promoting intermolecular RNA interactions may be a widespread strategy of RNA chaperone recycling. |
 External links | Proc Natl Acad Sci U S A / PubMed:34615715 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.1 - 3.9 Å |
| Structure data | EMDB-13474, PDB-7pko:  EMDB-13475: EMDB-13476, PDB-7pkp: |
| Source |
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 Keywords |  VIRAL PROTEIN / RNA chaperone Rotavirus RNA folding / RNA Chaperone RNA folding Rotavirus |
