SR-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization | |
Luo, HB; Ye, F; Chen, KX; Shen, X; Jiang, HL | |
刊名 | BIOCHEMISTRY |
2005-11-22 | |
卷号 | 44期号:46页码:15351-15358 |
ISSN号 | 0006-2960 |
DOI | 10.1021/bi051122c |
文献子类 | Article |
英文摘要 | The nucleocapsid (N) protein of SARS coronavirus (SARS-CoV) is reported to function in encapsidating the viral genomic RNA into helical nucleocapsid, and its self-association is believed to be vital in coating the viral genomic RNA. Characterization of SARS-CoV N multimerization may thereby help us better understand the coronavirus assembly. In the current work, using the yeast two-hybrid technique, an unexpected interaction between residues 1-210 and 211-290 (central region) of the SARS-CoV N protein was detected, and SPR results further revealed that the SR-rich motif (amino acids 183197) of SARS-CoV N protein is responsible for such an interaction. Chemical cross-linking and gel-filtration analyses indicated that the residues 283-422 of the SARS-CoV N protein have multimeric ability, although the full-length N protein is prone to exist predominantly as dimers. In addition, the multimeric ability of the C-terminal domain of SARS-CoV N protein could be weakened by the SR-rich motif interaction with the central region (amino acids 211-290). All of these data suggested that the SR-rich motif of the SARS-CoV N protein might play an import role in the transformation of the SARS-CoV N protein between the dimer and multimer during its binding to its central region for self-association or dissociation. This current paper will hopefully provide some new ideas in studying SARS-CoV N multimerization. |
WOS关键词 | ACUTE RESPIRATORY SYNDROME ; SEQUENCE-ANALYSIS ; SELF-ASSOCIATION ; GENOME SEQUENCE ; SYNDROME VIRUS ; DOMAIN ; AFFINITY ; STRAINS ; GENES ; RNA |
WOS研究方向 | Biochemistry & Molecular Biology |
语种 | 英语 |
出版者 | AMER CHEMICAL SOC |
WOS记录号 | WOS:000233453000028 |
内容类型 | 期刊论文 |
源URL | [http://119.78.100.183/handle/2S10ELR8/273770] |
专题 | 药理学第三研究室 药物发现与设计中心 |
通讯作者 | Shen, X |
作者单位 | 1.E China Univ Sci & Technol, Sch Pharm, Shanghai 200237, Peoples R China 2.Chinese Acad Sci, Shanghai Inst Biol Sci, Grad Sch,Shanghai Inst Mat Med, Drug Discovery & Design Ctr,State Key Lab Drug Re, Shanghai 201203, Peoples R China |
推荐引用方式 GB/T 7714 | Luo, HB,Ye, F,Chen, KX,et al. SR-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization[J]. BIOCHEMISTRY,2005,44(46):15351-15358. |
APA | Luo, HB,Ye, F,Chen, KX,Shen, X,&Jiang, HL.(2005).SR-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization.BIOCHEMISTRY,44(46),15351-15358. |
MLA | Luo, HB,et al."SR-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization".BIOCHEMISTRY 44.46(2005):15351-15358. |
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