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Reconstitution of the SARS-CoV-2 ribonucleosome provides insights into genomic RNA packaging and regulation by phosphorylation.
Carlson, Christopher R; Adly, Armin N; Bi, Maxine; Howard, Conor J; Frost, Adam; Cheng, Yifan; Morgan, David O.
  • Carlson CR; Department of Physiology, University of California, San Francisco, California, USA.
  • Adly AN; Department of Physiology, University of California, San Francisco, California, USA.
  • Bi M; Department of Biochemistry & Biophysics, University of California, San Francisco, California, USA.
  • Howard CJ; Department of Biochemistry & Biophysics, University of California, San Francisco, California, USA.
  • Frost A; Department of Biochemistry & Biophysics, University of California, San Francisco, California, USA.
  • Cheng Y; Department of Biochemistry & Biophysics, University of California, San Francisco, California, USA.
  • Morgan DO; Department of Physiology, University of California, San Francisco, California, USA. Electronic address: David.Morgan@ucsf.edu.
J Biol Chem ; 298(11): 102560, 2022 11.
Article in English | MEDLINE | ID: covidwho-2105268
ABSTRACT
The nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus 2 is responsible for compaction of the ∼30-kb RNA genome in the ∼90-nm virion. Previous studies suggest that each virion contains 35 to 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 in vitro with short fragments of the viral genome, forms 15-nm particles similar to the vRNP structures observed within virions. These vRNPs depend on regions of N protein that promote protein-RNA and protein-protein interactions. Phosphorylation of N protein in its disordered serine/arginine region weakens these interactions to generate less compact vRNPs. We propose that unmodified N protein binds structurally diverse regions in genomic RNA to form compact vRNPs within the nucleocapsid, while phosphorylation alters vRNP structure to support other N protein functions in viral transcription.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 Limits: Humans Language: English Journal: J Biol Chem Year: 2022 Document Type: Article Affiliation country: J.jbc.2022.102560

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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 Limits: Humans Language: English Journal: J Biol Chem Year: 2022 Document Type: Article Affiliation country: J.jbc.2022.102560