Idioma:

Phosphoregulation of Phase Separation by the SARS-CoV-2 N Protein Suggests a Biophysical Basis for its Dual Functions

Carlson, Christopher R. ; Asfaha, Jonathan B. ; Ghent, Chloe M. ; Howard, Conor J. ; Hartooni, Nairi ; Safari, Maliheh ; Frankel, Alan D. ; Morgan, David O.

Molecular cell, 2020-12, Vol.80 (6), p.1092-1103.e4 [Periódico revisado por pares]

United States: Elsevier Inc

Texto completo disponível

Citações Citado por

Enviar para

Título:
Phosphoregulation of Phase Separation by the SARS-CoV-2 N Protein Suggests a Biophysical Basis for its Dual Functions
Autor: Carlson, Christopher R. ; Asfaha, Jonathan B. ; Ghent, Chloe M. ; Howard, Conor J. ; Hartooni, Nairi ; Safari, Maliheh ; Frankel, Alan D. ; Morgan, David O.
Assuntos: biomolecular condensate ; Coronavirus ; Coronavirus Nucleocapsid Proteins - chemistry ; Coronavirus Nucleocapsid Proteins - genetics ; Coronavirus Nucleocapsid Proteins - metabolism ; COVID-19 ; Humans ; N protein ; nucleocapsid ; phase separation ; Phosphoproteins - chemistry ; Phosphoproteins - genetics ; Phosphoproteins - metabolism ; Phosphorylation ; Protein Domains ; Protein Multimerization ; RNA, Viral - chemistry ; RNA, Viral - genetics ; RNA, Viral - metabolism ; SARS-CoV-2 ; SARS-CoV-2 - chemistry ; SARS-CoV-2 - genetics ; SARS-CoV-2 - metabolism ; Short
É parte de: Molecular cell, 2020-12, Vol.80 (6), p.1092-1103.e4
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Lead Contact
These authors contributed equally
Descrição: 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. [Display omitted] •Nucleocapsid protein of SARS-CoV-2 forms biomolecular condensates with viral RNA•Unmodified N protein forms gel-like condensates containing discrete RNP particles•Phosphorylated N protein forms dynamic, liquid-like condensates•The two condensate forms are well suited for the two major functions of N protein Carlson et al. demonstrate that the nucleocapsid (N) protein of SARS-CoV-2, together with viral RNA, forms gel-like biomolecular condensates and particles that are consistent with its genome-packaging role. Phosphorylation transforms condensates into liquid-like droplets, which may provide a cytoplasmic compartment to support the protein’s function in viral genome transcription.
Editor: United States: Elsevier Inc
Idioma: Inglês

Links

View this record in MEDLINE/PubMed

Voltar para lista de resultados

Anterior Resultado 17 Avançar Ir para próxima página

Realização: Logos de Redes Sociais:

Phosphoregulation of Phase Separation by the SARS-CoV-2 N Protein Suggests a Biophysical Basis for its Dual Functions

Carlson, Christopher R. ; Asfaha, Jonathan B. ; Ghent, Chloe M. ; Howard, Conor J. ; Hartooni, Nairi ; Safari, Maliheh ; Frankel, Alan D. ; Morgan, David O.

United States: Elsevier Inc

Buscando em bases de dados remotas. Favor aguardar.