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.
Zeng
Yingchun
Y
State Key Laboratory of Virology, College of Life Science, Wuhan University, Wuhan 430072, PR China.
Ye
Linbai
L
Zhu
Shengli
S
Zheng
Hong
H
Zhao
Peng
P
Cai
Weijia
W
Su
Liya
L
She
Yinglong
Y
Wu
Zhenghui
Z
D001665:Binding Sites; D006367:HeLa Cells; D006801:Humans; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism*; D019590:Nucleocapsid Proteins / Q000737:chemistry* / Q000378:metabolism*; D010766:Phosphorylation; D011485:Protein Binding; D045473:Severe acute respiratory syndrome-related coronavirus / Q000737:chemistry* / Q000378:metabolism*
D009687:Nuclear Proteins; D019590:Nucleocapsid Proteins