Carboxyl terminus of severe acute respiratory syndrome coronavirus nucleocapsid protein: Self-association analysis and nucleic acid binding characterization | |
Luo, Haibin; Chen, Jing![]() ![]() ![]() ![]() | |
刊名 | BIOCHEMISTRY
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2006-10-03 | |
卷号 | 45期号:39页码:11827-11835 |
ISSN号 | 0006-2960 |
DOI | 10.1021/bi0609319 |
文献子类 | Article |
英文摘要 | Coronavirus nucleocapsid (N) protein envelops the genomic RNA to form long helical nucleocapsid during virion assembly. Since N protein oligomerization is usually a crucial step in this process, characterization of such an oligomerization will help in the understanding of the possible mechanisms for nucleocapsid formation. The N protein of severe acute respiratory syndrome coronavirus (SARS-CoV) was recently discovered to self-associate by its carboxyl terminus. In this study, to further address the detailed understanding of the association feature of this C-terminus, its oligomerization was systematically investigated by size exclusion chromatography and chemical cross-linking assays. Our results clearly indicated that the C-terminal domain of SARS-CoV N protein could form not only dimers but also trimers, tetramers, and hexamers. Further analyses against six deletion mutants showed that residues 343-402 were necessary and sufficient for this C-terminus oligomerization. Although this segment contains many charged residues, differences in ionic strength have no effects on its oligomerization, indicating the absence of electrostatic force in SARS-CoV N protein C-terminus self-association. Gel shift assay results revealed that the SARS-CoV N protein C-terminus is also able to associate with nucleic acids and residues 363-382 are the responsible interaction partner, demonstrating that this fragment might involve genomic RNA binding sites. The fact that nucleic acid binding could promote the SARS-CoV N protein C-terminus to form high-order oligomers implies that the oligomeric SARS-CoV N protein probably combines with the viral genomic RNA in triggering long nucleocapsid formation. |
WOS关键词 | SARS-ASSOCIATED CORONAVIRUS ; SYNDROME VIRUS ; MEMBRANE-PROTEIN ; GENOME SEQUENCE ; N PROTEIN ; DOMAIN ; MULTIMERIZATION ; PROGRESSION ; INFECTION ; CELLS |
WOS研究方向 | Biochemistry & Molecular Biology |
语种 | 英语 |
出版者 | AMER CHEMICAL SOC |
WOS记录号 | WOS:000240752400012 |
内容类型 | 期刊论文 |
源URL | [http://119.78.100.183/handle/2S10ELR8/273472] ![]() |
专题 | 药理学第三研究室 中科院受体结构与功能重点实验室 新药研究国家重点实验室 药物发现与设计中心 |
通讯作者 | Shen, Xu |
作者单位 | 1.E China Univ Sci & Technol, Sch Pharm, Shanghai 200237, Peoples R China 2.Chinese Acad Sci, Drug Discovery & Design Ctr, State Key Lab Drug Res, Shanghai Inst Mat Med, Shanghai 210203, Peoples R China |
推荐引用方式 GB/T 7714 | Luo, Haibin,Chen, Jing,Chen, Kaixian,et al. Carboxyl terminus of severe acute respiratory syndrome coronavirus nucleocapsid protein: Self-association analysis and nucleic acid binding characterization[J]. BIOCHEMISTRY,2006,45(39):11827-11835. |
APA | Luo, Haibin,Chen, Jing,Chen, Kaixian,Shen, Xu,&Jiang, Hualiang.(2006).Carboxyl terminus of severe acute respiratory syndrome coronavirus nucleocapsid protein: Self-association analysis and nucleic acid binding characterization.BIOCHEMISTRY,45(39),11827-11835. |
MLA | Luo, Haibin,et al."Carboxyl terminus of severe acute respiratory syndrome coronavirus nucleocapsid protein: Self-association analysis and nucleic acid binding characterization".BIOCHEMISTRY 45.39(2006):11827-11835. |
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