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Reconstitution of the SARS-CoV-2 ribonucleosome provides insights into genomic RNA packaging and regulation by phosphorylation

View ORCID ProfileChristopher R. Carlson, Armin N. Adly, Maxine Bi, Yifan Cheng, View ORCID ProfileDavid O. Morgan
doi: https://doi.org/10.1101/2022.05.23.493138
Christopher R. Carlson
1Department of Physiology, University of California, San Francisco CA 94143
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Armin N. Adly
1Department of Physiology, University of California, San Francisco CA 94143
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Maxine Bi
2Department of Biochemistry & Biophysics, University of California, San Francisco CA 94143
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Yifan Cheng
2Department of Biochemistry & Biophysics, University of California, San Francisco CA 94143
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David O. Morgan
1Department of Physiology, University of California, San Francisco CA 94143
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  • For correspondence: David.Morgan@ucsf.edu
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Abstract

The nucleocapsid (N) protein of coronaviruses is responsible for compaction of the ∼30-kb RNA genome in the ∼100-nm virion. Cryo-electron tomography suggests that each virion contains 35-40 viral ribonucleoprotein (vRNP) complexes, or ribonucleosomes, arrayed along the genome. There is, however, little mechanistic understanding of the vRNP complex. Here, we show that N protein, when combined with viral RNA fragments in vitro, forms cylindrical 15-nm particles similar to the vRNP structures observed within coronavirus virions. These vRNPs form in the presence of stem-loop-containing RNA and depend on regions of N protein that promote protein-RNA and protein-protein interactions. Phosphorylation of N protein in its disordered serine/arginine (SR) region weakens these interactions and disrupts vRNP assembly. We propose that unmodified N binds stem-loop-rich regions in genomic RNA to form compact vRNP complexes within the nucleocapsid, while phosphorylated N maintains uncompacted viral RNA to promote the protein’s transcriptional function.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted May 24, 2022.
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Reconstitution of the SARS-CoV-2 ribonucleosome provides insights into genomic RNA packaging and regulation by phosphorylation
Christopher R. Carlson, Armin N. Adly, Maxine Bi, Yifan Cheng, David O. Morgan
bioRxiv 2022.05.23.493138; doi: https://doi.org/10.1101/2022.05.23.493138
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Reconstitution of the SARS-CoV-2 ribonucleosome provides insights into genomic RNA packaging and regulation by phosphorylation
Christopher R. Carlson, Armin N. Adly, Maxine Bi, Yifan Cheng, David O. Morgan
bioRxiv 2022.05.23.493138; doi: https://doi.org/10.1101/2022.05.23.493138

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