Author: Zeng, Yingchun; Ye, Linbai; Zhu, Shengli; Zheng, Hong; Zhao, Peng; Cai, Weijia; Su, Liya; She, Yinglong; Wu, Zhenghui
Title: The nucleocapsid protein of SARS-associated coronavirus inhibits B23 phosphorylation Cord-id: cwt7dswz Document date: 2008_5_2
ID: cwt7dswz
Snippet: 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
Document: 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.
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