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The SARS-CoV-2 nucleocapsid phosphoprotein forms mutually exclusive condensates with RNA and the membrane-associated M protein.
Lu, Shan; Ye, Qiaozhen; Singh, Digvijay; Cao, Yong; Diedrich, Jolene K; Yates, John R; Villa, Elizabeth; Cleveland, Don W; Corbett, Kevin D.
  • Lu S; Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA, 92093, USA.
  • Ye Q; Ludwig Institute for Cancer Research, San Diego Branch, La Jolla, CA, 92093, USA.
  • Singh D; Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA, 92093, USA.
  • Cao Y; Section of Molecular Biology, Division of Biological Sciences, University of California San Diego, La Jolla, CA, 92093, USA.
  • Diedrich JK; National Institute of Biological Sciences, 102206, Beijing, China.
  • Yates JR; The Scripps Research Institute, La Jolla, CA, 92037, USA.
  • Villa E; The Scripps Research Institute, La Jolla, CA, 92037, USA.
  • Cleveland DW; Section of Molecular Biology, Division of Biological Sciences, University of California San Diego, La Jolla, CA, 92093, USA.
  • Corbett KD; Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA, 92093, USA. dcleveland@health.ucsd.edu.
Nat Commun ; 12(1): 502, 2021 01 21.
Article in English | MEDLINE | ID: covidwho-1387327
ABSTRACT
The multifunctional nucleocapsid (N) protein in SARS-CoV-2 binds the ~30 kb viral RNA genome to aid its packaging into the 80-90 nm membrane-enveloped virion. The N protein is composed of N-terminal RNA-binding and C-terminal dimerization domains that are flanked by three intrinsically disordered regions. Here we demonstrate that the N protein's central disordered domain drives phase separation with RNA, and that phosphorylation of an adjacent serine/arginine rich region modulates the physical properties of the resulting condensates. In cells, N forms condensates that recruit the stress granule protein G3BP1, highlighting a potential role for N in G3BP1 sequestration and stress granule inhibition. The SARS-CoV-2 membrane (M) protein independently induces N protein phase separation, and three-component mixtures of N + M + RNA form condensates with mutually exclusive compartments containing N + M or N + RNA, including annular structures in which the M protein coats the outside of an N + RNA condensate. These findings support a model in which phase separation of the SARS-CoV-2 N protein contributes both to suppression of the G3BP1-dependent host immune response and to packaging genomic RNA during virion assembly.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: RNA, Viral / Viral Matrix Proteins / Coronavirus Nucleocapsid Proteins / SARS-CoV-2 / COVID-19 Limits: Humans Language: English Journal: Nat Commun Journal subject: Biology / Science Year: 2021 Document Type: Article Affiliation country: S41467-020-20768-Y

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Full text: Available Collection: International databases Database: MEDLINE Main subject: RNA, Viral / Viral Matrix Proteins / Coronavirus Nucleocapsid Proteins / SARS-CoV-2 / COVID-19 Limits: Humans Language: English Journal: Nat Commun Journal subject: Biology / Science Year: 2021 Document Type: Article Affiliation country: S41467-020-20768-Y