期刊
出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2100198118
关键词
RNA chaperones; ribonucleoproteins; genome assembly rotavirus
资金
- Sir Henry Dale Fellowship - Wellcome Trust [213437/Z/18/Z, 220628/Z/20/Z]
- Sir Henry Dale Fellowship - Royal Society [213437/Z/18/Z, 220628/Z/20/Z]
- Biotechnology and Biological Sciences Research Council (BBSRC) White Rose DTP [BB/M011151/1]
- European Regional Development Fund [CZ.02.1.01/0.0/0.0/15_003/0000441]
- University of Leeds
- Biomedicine Discovery Scholarship
- ARC [DP190103407]
- NHMRC [APP1162921, APP1184637]
- Deutsche Forschungsgemeinschaft [SFB1032]
- Ludwig-Maximilians-Universitat, Munchen through the Center for NanoScience
- LMUinnovativ initiative BioImaging Network
- BBSRC [BB/M012573/1]
- Wellcome Trust [208385/Z/17/Z, 094232, 108466/Z/15/Z]
- Wellcome Trust [213437/Z/18/Z, 220628/Z/20/Z] Funding Source: Wellcome Trust
It was found that NSP2 autoregulates its chaperone activity through its C-terminal region, promoting RNA-RNA interactions. Additionally, structural proteomics data revealed that the CTR does not directly interact with RNA, but accelerates RNA release from NSP2.
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.
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