About: Phosphorylation of the arginine/serine dipeptide‐rich motif of the severe acute respiratory syndrome coronavirus nucleocapsid protein modulates its multimerization, translation inhibitory activity and cellular localization

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About: Phosphorylation of the arginine/serine dipeptide‐rich motif of the severe acute respiratory syndrome coronavirus nucleocapsid protein modulates its multimerization, translation inhibitory activity and cellular localization Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.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 of the arginine/serine dipeptide‐rich motif of the severe acute respiratory syndrome coronavirus nucleocapsid protein modulates its multimerization, translation inhibitory activity and cellular localization
Creator	Tarn, Woan-Yuh Lee, Kuan-Rong Peng, Tsui-Yi
Source	Medline; PMC
abstract	Coronavirus nucleocapsid protein is abundant in infected cells and participates in viral RNA replication and transcription. The central domain of the nucleocapsid protein contains several arginine/serine (RS) dipeptides, the biological significance of which has not been well investigated. In the present study, we demonstrate that the severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated primarily within the RS‐rich region in cells and by SR protein kinase 1 in vitro. The nucleocapsid protein could suppress translation and its RS motif is essential for such an activity. Moreover, phosphorylation of the RS motif could modulate the translation inhibitory activity of the nucleocapsid protein. We further found that RS motif phosphorylation did not significantly affect RNA binding of the nucleocapsid protein but impaired its multimerization ability. We observed that the nucleocapsid protein could translocate to cytoplasmic stress granules in response to cellular stress. Deletion or mutations of the RS motif enhanced stress granule localization of the nucleocapsid protein, whereas overexpression of SR protein kinase 1 inhibited nucleocapsid protein localization to stress granules. The nucleocapsid protein lacking the RS motif formed high‐order RNP complexes, which may also account for its enhanced stress granule localization. Taken together, phosphorylation of the severe acute respiratory syndrome‐CoV nucleocapsid protein modulates its activity in translation control and also interferes with its oligomerization and aggregation in stress granules.
has issue date	2008-07-09(xsd:dateTime)
bibo:doi	10.1111/j.1742-4658.2008.06564.x
bibo:pmid	18631359
has license	no-cc
sha1sum (hex)	4f394214d79be643597d3716bbf80a061a6ad04d
schema:url	https://doi.org/10.1111/j.1742-4658.2008.06564.x
resource representing a document's title	Phosphorylation of the arginine/serine dipeptide‐rich motif of the severe acute respiratory syndrome coronavirus nucleocapsid protein modulates its multimerization, translation inhibitory activity and cellular localization
has PubMed Central identifier	PMC7164085
has PubMed identifier	18631359
schema:publication	FEBS J
resource representing a document's body	covid:4f394214d79be643597d3716bbf80a061a6ad04d#body_text
is schema:about of	named entity 'inhibitory activity' named entity 'multimerization' named entity 'motif' named entity 'viral RNA replication' named entity 'Coronavirus' named entity 'SR protein' named entity 'protein' named entity 'spectropolarimeter' named entity 'cytoplasm' named entity 'transiently transfected' named entity 'orthophosphate' named entity 'firefly luciferase' named entity 'recombinant' named entity 'arginine' named entity 'motif' named entity 'coronaviruses' named entity 'far-UV' named entity 'protein' named entity 'immunoblotting' named entity 'Phosphorylation' named entity 'coronaviruses' named entity 'nucleocapsid protein' named entity 'protein' named entity 'SDS' named entity 'virions' named entity 'positively charged' named entity 'protein' named entity 'HBV' named entity 'SRPK1' named entity 'stress granules' named entity 'N-terminal domain' named entity 'glycogen synthase kinase' named entity 'Transfection' named entity 'recombinant' named entity 'TBE buffer' named entity 'SARS-CoV' named entity 'serines' named entity 'NaCl' named entity 'phosphorylation site' named entity 'phosphorylated' named entity 'Fluorescein' named entity 'protein' named entity 'magnesium acetate' named entity 'serine' named entity 'hepatitis B virus' named entity 'SARS-CoV' named entity 'protein' named entity 'streptomycin' named entity 'EDTA' named entity 'sucrose' named entity 'serine' named entity 'oligomers' named entity 'nucleotide' named entity 'cytoplasm' named entity 'coronavirus' named entity 'assay' named entity 'Stratagene' named entity 'dose-dependent manner' named entity 'rhodamine' named entity 'NaCl' named entity 'glutathione S-transferase' named entity 'phosphorylated' named entity 'orthophosphate' named entity 'nucleocapsids' named entity 'motif' named entity 'motif' named entity 'motif' named entity 'phosphorylate' named entity 'titrated' named entity 'ATP' named entity 'infection' named entity 'cDNA' named entity 'protein' named entity 'protein' named entity 'luciferase' named entity 'protein' named entity 'phosphorylated' named entity 'motif' named entity 'mRNA'

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