The nucleocapsid protein of SARS-associated coronavirus inhibits B23 phosphorylation.
Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is responsible for SARS infection. Nucleocapsid (N) protein of SARS-CoV encapsidates the viral RNA and plays an important role in virus particle assembly and release. In this study, the N protein of SARS-CoV was found to associate with B23, a phosphoprotein in nucleolus, in ... vitro and in vivo. Mapping studies localized the critical N sequences for this interaction to amino acid residues 175-210, which included a serine/arginine (SR)-rich domain. In vitro phosphorylation assay showed that the N protein inhibited the B23 phosphorylation at Thr199.
Mesh Terms:
Binding Sites, HeLa Cells, Humans, Nuclear Proteins, Nucleocapsid Proteins, Phosphorylation, Protein Binding, SARS Virus
Binding Sites, HeLa Cells, Humans, Nuclear Proteins, Nucleocapsid Proteins, Phosphorylation, Protein Binding, SARS Virus
Biochem. Biophys. Res. Commun.
Date: May. 02, 2008
PubMed ID: 18243139
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