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http://conacyt.repositorioinstitucional.mx/jspui/handle/1000/8183| Assembly of SARS-CoV-2 ribonucleosomes by truncated N* variant of the nucleocapsid protein | |
| Armin Adly Maxine Bi Christopher Carlson Abdullah Syed Alison Ciling Jennifer Doudna Yifan Cheng David Morgan | |
| Acceso Abierto | |
| Atribución-NoComercial-SinDerivadas | |
| https://doi.org/10.1101/2023.08.16.553581 | |
| https://www.biorxiv.org/content/10.1101/2023.08.16.553581v1 | |
| Abstract The Nucleocapsid (N) protein of SARS-CoV-2 compacts the RNA genome into viral ribonucleoprotein (vRNP) complexes within virions. Assembly of vRNPs is inhibited by phosphorylation of the N protein SR region. Several SARS-CoV-2 variants of concern carry N protein mutations that reduce phosphorylation and enhance the efficiency of viral packaging. Variants of the dominant B.1.1 viral lineage also encode a truncated N protein, termed N* or Δ(1-209), that mediates genome packaging despite lacking the N-terminal RNA-binding domain and SR region. Here, we show that Δ(1-209) and viral RNA assemble into vRNPs that are remarkably similar in size and shape to those formed with full-length N protein. We show that assembly of Δ(1-209) vRNPs requires the leucine-rich helix (LH) of the central disordered region, and that the LH promotes N protein oligomerization. We also find that fusion of a phosphomimetic SR region to Δ(1-209) inhibits RNA binding and vRNP assembly. Our results provide new insights into the mechanisms by which RNA binding promotes N protein self-association and vRNP assembly, and how this process is modulated by SR phosphorylation. | |
| bioRxiv | |
| 17-08-2023 | |
| Preimpreso | |
| Inglés | |
| Público en general | |
| VIRUS RESPIRATORIOS | |
| Aparece en las colecciones: | Materiales de Consulta y Comunicados Técnicos |
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| Assembly of SARS-CoV-2 ribonucleosomes by truncated N_variant of the nucleocapsid protein.pdf | 24.46 MB | Adobe PDF | Visualizar/Abrir |