Article ; Online: Phosphoregulation of Phase Separation by the SARS-CoV-2 N Protein Suggests a Biophysical Basis for its Dual Functions.
2020 Volume 80, Issue 6, Page(s) 1092–1103.e4
Abstract: ... function, but the underlying mechanism is not known. Here, we show that the N protein of SARS-CoV-2 ... The nucleocapsid (N) protein of coronaviruses serves two major functions: compaction of the RNA ... mediates such distinct functions. The N protein contains two RNA-binding domains surrounded by regions ...
| Abstract | The nucleocapsid (N) protein of coronaviruses serves two major functions: compaction of the RNA genome in the virion and regulation of viral gene transcription. It is not clear how the N protein mediates such distinct functions. The N protein contains two RNA-binding domains surrounded by regions of intrinsic disorder. Phosphorylation of the central disordered region promotes the protein's transcriptional function, but the underlying mechanism is not known. Here, we show that the N protein of SARS-CoV-2, together with viral RNA, forms biomolecular condensates. Unmodified N protein forms partially ordered gel-like condensates and discrete 15-nm particles based on multivalent RNA-protein and protein-protein interactions. Phosphorylation reduces these interactions, generating a more liquid-like droplet. We propose that distinct oligomeric states support the two functions of the N protein: unmodified protein forms a structured oligomer that is suited for nucleocapsid assembly, and phosphorylated protein forms a liquid-like compartment for viral genome processing. |
|---|---|
| MeSH term(s) | COVID-19 ; Coronavirus Nucleocapsid Proteins/chemistry ; Coronavirus Nucleocapsid Proteins/genetics ; Coronavirus Nucleocapsid Proteins/metabolism ; Humans ; Phosphoproteins/chemistry ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Domains ; Protein Multimerization ; RNA, Viral/chemistry ; RNA, Viral/genetics ; RNA, Viral/metabolism ; SARS-CoV-2/chemistry ; SARS-CoV-2/genetics ; SARS-CoV-2/metabolism |
| Chemical Substances | Coronavirus Nucleocapsid Proteins ; Phosphoproteins ; RNA, Viral ; nucleocapsid phosphoprotein, SARS-CoV-2 |
| Language | English |
| Publishing date | 2020-11-20 |
| Publishing country | United States |
| Document type | Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't |
| ZDB-ID | 1415236-8 |
| ISSN | 1097-4164 ; 1097-2765 |
| ISSN (online) | 1097-4164 |
| ISSN | 1097-2765 |
| DOI | 10.1016/j.molcel.2020.11.025 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
Full text online
More links
Kategorien
In stock of ZB MED Cologne/Königswinter
| Zs.A 5055: Show issues | Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG) |
Order via subito
This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.