Carboxyl terminus of severe acute respiratory syndrome coronavirus nucleocapsid protein: Self-association analysis and nucleic acid binding characterization

doi:10.1021/bi0609319

CORC > 上海药物研究所 > 中国科学院上海药物研究所 > 药理学第三研究室

	Carboxyl terminus of severe acute respiratory syndrome coronavirus nucleocapsid protein: Self-association analysis and nucleic acid binding characterization
	Luo, Haibin ; Chen, Jing; Chen, Kaixian; Shen, Xu; Jiang, Hualiang
刊名	BIOCHEMISTRY
	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.