The nucleocapsid protein of SARS-associated coronavirus inhibits B23 phosphorylation

被引:27
|
作者
Zeng, Yingchun [1 ]
Ye, Linbai [1 ]
Zhu, Shengli [1 ]
Zheng, Hong [1 ]
Zhao, Peng [1 ]
Cai, Weijia [1 ]
Su, Liya [1 ]
She, Yinglong [1 ]
Wu, Zhenghui [1 ]
机构
[1] Wuhan Univ, Coll Life Sci, State Key Lab Virol, Wuhan 430072, Peoples R China
关键词
SARS coronavirus; nucleocapsid protein; B23; protein-protein interaction; serine/arginine-rich domain; phosphorylation;
D O I
10.1016/j.bbrc.2008.01.096
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 P4 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. (c) 2008 Published by Elsevier Inc.
引用
收藏
页码:287 / 291
页数:5
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