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1、Review The SARS coronavirus nucleocapsid protein Forms and functions Chung-ke Chang a, Ming-Hon Houb, Chi-Fon Changc, Chwan-Deng Hsiaod, Tai-huang Huanga,c,e, aInstitute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan, ROC bDepartment of Life Science, National Chung Hsing University, T
2、aichung 40254, Taiwan, ROC cThe Genomics Research Center, Academia Sinica, Taipei 11529, Taiwan, ROC dInstitute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan, ROC eDepartment of Physics, National Taiwan Normal University, Taipei 11677, Taiwan, ROC a r t i c l ei n f o Article history:
3、Received 28 October 2013 Revised 8 December 2013 Accepted 20 December 2013 Available online 11 January 2014 Keywords: SARS Coronavirus Nucleocapsid protein Capsid packaging Intrinsic disorder RNP a b s t r a c t The nucleocapsid phosphoprotein of the severe acute respiratory syndrome coronavirus (SA
4、RS-CoV N protein) packages the viral genome into a helical ribonucleocapsid (RNP) and plays a fundamental role during viral self-assembly. It is a protein with multifarious activities. In this article we will review our current understanding of the N protein structure and its interaction with nuclei
5、c acid. Highlights of the progresses include uncovering the modular organization, determining the structures of the structural domains, realizing the roles of protein disorder in proteinprotein and proteinnucleic acid interactions, and visualizing the ribonucleoprotein (RNP) structure inside the vir
6、ions. It was also demonstrated that N- protein binds to nucleic acid at multiple sites with a coupled-allostery manner. We propose a SARS-CoV RNP model that conforms to existing data and bears resemblance to the existing RNP structures of RNA viruses. The model highlights the critical role of modula
7、r organization and intrinsic disorder of the N pro- tein in the formation and functions of the dynamic RNP capsid in RNA viruses. This paper forms part of a symposium in Antiviral Research on From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses. ? 2014 Elsevier B.V. All r
8、ights reserved. Contents 1.Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 40 2.Packaging of RNP inside the virus. . . . .
9、. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 40 3.Modular organization of the SARS-CoV N protein . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
10、. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 41 4.Structure of SARS-CoV N protein. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 42 4.1.Struc
11、ture of the N-terminal domain. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 42 4.2.Structure of the C-terminal structural domain . . . . . . . . . . . . . . . . . . . . . . . . . . .
12、. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 43 4.3.Comparison with N proteins of other coronaviruses. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 44 4.4.The CTD
13、 dimer interface suggests possible evolutional link between corona- and arteriviruses. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 44 5.Biophysical aspects of SARS-CoV N protein self-association . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
14、 . . . . . . . . . . . . . . . . . . . . . . . . . . 44 5.1.The CTD is a transient self-association site of the SARS-CoV N protein . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 44 5.2.Electrostatic screening and phosphorylation-mimicking mu
15、tation affect SARS-CoV N protein self-association. . . . . . . . . . . . . . . . . . . . . . 45 6.Proteinnucleic acid interaction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
16、. . . . . 46 6.1.SARS-CoV N protein binds to nucleic acids at multiple sites . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 46 6.2.Intrinsic disorder and coupled-allosteric binding of N to nucleic acids. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 46 7.Packaging of the SARS-CoV ribonucleocapsid. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
