About: Phosphorylation modulates liquid-liquid phase separation of the SARS-CoV-2 N protein

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About: Phosphorylation modulates liquid-liquid phase separation of the SARS-CoV-2 N protein Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Phosphorylation modulates liquid-liquid phase separation of the SARS-CoV-2 N protein
Creator	Morgan, David Asfaha, Jonathan Carlson, Christopher Ghent, Chloe Hartooni, Nairi Howard, Conor
Source	BioRxiv; Medline
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 in the infected cell1–3. The N protein contains two globular RNA-binding domains surrounded by regions of intrinsic disorder4. Phosphorylation of the central disordered region is required for normal viral genome transcription5,6, which occurs in a cytoplasmic structure called the replication transcription complex (RTC)7–11. It is not known how phosphorylation controls N protein function. Here we show that the N protein of SARS-CoV-2, together with viral RNA, forms biomolecular condensates12–15. Unmodified N protein forms partially ordered gel-like structures that depend on multivalent RNA-protein and protein-protein interactions. Phosphorylation reduces a subset of these interactions, generating a more liquid-like droplet. We speculate 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. Inhibitors of N protein phosphorylation could therefore serve as antiviral therapy.
has issue date	2020-06-29(xsd:dateTime)
bibo:doi	10.1101/2020.06.28.176248
bibo:pmid	32637943
has license	biorxiv
sha1sum (hex)	184caacde81a0c436a8f6cd5d110e49c47b90ac2
schema:url	https://doi.org/10.1101/2020.06.28.176248
resource representing a document's title	Phosphorylation modulates liquid-liquid phase separation of the SARS-CoV-2 N protein
has PubMed identifier	32637943
schema:publication	bioRxiv
resource representing a document's body	covid:184caacde81a0c436a8f6cd5d110e49c47b90ac2#body_text
is schema:about of	named entity 'regions' named entity 'infected' named entity 'serves' named entity 'RNA' named entity 'RNA' named entity 'The N' named entity 'genome' named entity 'nucleocapsid' named entity 'nucleocapsid' named entity 'gene transcription' named entity 'SARS-CoV-2' named entity 'Phosphorylation' named entity 'protein' named entity 'virion' named entity 'subgenomic' named entity 'phosphorylated' named entity 'phosphorylation' named entity 'nucleocapsid' named entity 'FEI' named entity 'protein structure' named entity 'cell cycle' named entity 'Hepes' named entity 'Cdk1' named entity 'protein oligomers' named entity 'viral RNA' named entity 'oligomers' named entity 'kinases' named entity 'phosphorylation' named entity 'aspartate' named entity 'protein' named entity 'SARS-CoV-2' named entity 'oligomers' named entity 'dimer' named entity 'mouse hepatitis virus' named entity 'recombinant' named entity 'serially diluted' named entity 'protein' named entity 'protein' named entity 'RNA' named entity 'catalytic domain' named entity 'autophosphorylation' named entity 'organelle' named entity 'genome' named entity 'phosphorylated' named entity 'MHV' named entity 'protein phosphorylation' named entity 'infection' named entity 'cleavage' named entity 'liquid droplets' named entity 'GSK-3' named entity 'GSK-3' named entity 'CTF' named entity 'protein' named entity 'protein' named entity 'helical' named entity 'RNA' named entity 'transcription' named entity 'Turbidity' named entity 'structural protein gene' named entity 'condensates' named entity 'wild-type' named entity 'RNA' named entity 'ddH2O' named entity 'microscope' named entity 'morphology' named entity 'RNA binding' named entity 'kinase' named entity 'protein structures' named entity 'protein' named entity 'lysed' named entity 'kDa' named entity 'protein' named entity 'fluorescence recovery after photobleaching' named entity 'imidazole' named entity 'RNA' named entity 'biomolecular condensates' named entity 'ddH2O'

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