The nucleocapsid protein of SARS coronavirus has a high binding affinity to the human cellular heterogeneous nuclear ribonucleoprotein A1
文献类型：期刊论文
| 作者 | Luo, HB; Chen, Q; Chen, J ; Chen, KX; Shen, X; Jiang, HL
|
| 刊名 | FEBS LETTERS
 |
| 出版日期 | 2005-05-09 |
| 卷号 | 579期号:12页码:2623-2628 |
| 关键词 | SARS coronavirus nucleocapsid protein heterogeneous nuclear ribonucleoprotein A1 GST pull-down surface plasmon resonance yeast two-hybrid |
| ISSN号 | 0014-5793 |
| DOI | 10.1016/j.febslet.2005.03.080 |
| 文献子类 | Article |
| 英文摘要 | The nucleocapsid (N) protein of SARS coronavirus (SARS_CoV) is a major structural component of virions, which appears to be a multifunctional protein involved in viral RNA replication and translation. Heterogeneous nuclear ribonucleoprotein At (hnRNP A1) is related to the pre-mRNA splicing in the nucleus and translation regulation in the cytoplasm. In this report, based on the relevant biophysical and biochemical assays, the nucleocapsid protein of SARS_CoV (SARS_N) was discovered to exhibit high binding affinity to human hnRNP A1. GST pull-down results clearly demonstrated that SARS_N protein could directly and specifically bind to human hnRNP A I in vitro. Yeast two-hybrid assays further indicated in vivo that such binding relates to the fragment (aa 161-210) of SARS_N and the Gly-rich domain (aa 203-320) of hnRNP A1. Moreover, kinetic analyses by surface plasmon resonance (SPR) technology revealed that SARS_N protein has a specific binding affinity against human hnRNP At with K-D at 0.35 ± 0.02 μ M (k(on) = 5.83 ± 0.42 x 10(3) M-1 s(-1) and k(off) = 2.06 ± 0.12 x 10(-3) s(-1)). It is suggested that both SARS_N and hnRNP At proteins are possibly within the SARS_CoV replication/transcription complex and SARS_N/human hnRNP At interaction might function in the regulation of SARS_CoV RNA synthesis. In addition, the determined results showed that SARS_N protein has only one binding domain for interacting with human hnRNP At, which is different from the mouse hepatitis virus (MHV) binding case where the nucleocapsid protein of MHV (MHV_N) was found to have two binding domains involved in the MHV_N/hnRNP At interaction, thereby suggesting that SARS_N protein might carry out a different binding mode to bind to human hnRNP At for its further function performance in comparison with MHV_N. © 2005 Federal ion of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
| WOS关键词 | ACUTE RESPIRATORY SYNDROME ; IN-VITRO ; RNA ; DOMAIN ; VIRUS ; INTERACTS ; SEQUENCE |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics ; Cell Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000229051600014 |
| 出版者 | ELSEVIER SCIENCE BV |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/273873]  |
| 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, X |
| 作者单位 | 1.E China Univ Sci & Technol, Sch Pharm, Shanghai 200237, Peoples R China 2.Chinese Acad Sci, Grad Sch, Shanghai Inst Biol Sci,Drug Discovery & Design Ct, Shanghai Inst Mat Med,State Key Lab Drug Res, Shanghai 201203, Peoples R China |
| 推荐引用方式 GB/T 7714 | Luo, HB,Chen, Q,Chen, J,et al. The nucleocapsid protein of SARS coronavirus has a high binding affinity to the human cellular heterogeneous nuclear ribonucleoprotein A1[J]. FEBS LETTERS,2005,579(12):2623-2628. |
| APA | Luo, HB,Chen, Q,Chen, J,Chen, KX,Shen, X,&Jiang, HL.(2005).The nucleocapsid protein of SARS coronavirus has a high binding affinity to the human cellular heterogeneous nuclear ribonucleoprotein A1.FEBS LETTERS,579(12),2623-2628. |
| MLA | Luo, HB,et al."The nucleocapsid protein of SARS coronavirus has a high binding affinity to the human cellular heterogeneous nuclear ribonucleoprotein A1".FEBS LETTERS 579.12(2005):2623-2628. |
入库方式： OAI收割
来源：上海药物研究所
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