NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans
文献类型：期刊论文
| 作者 | Liu, SS; Zhang, W; Gao ZQ(高增强) ; Gao, ZQ; Ming, QQ; Hou, HF; Lan, WX; Wu, HM; Cao, CY; Dong, YH;
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| 刊名 | FEBS LETTERS
 |
| 出版日期 | 2013 |
| 卷号 | 587期号:16页码:2635-2642 |
| 关键词 | DrRecQ HRDC1 NMR Structure DNA |
| 英文摘要 | The RecQ helicase from Deinococcus radiodurans (DrRecQ) distinguishes from other helicases in that it utilizes its three 'helicase and RNaseD C-terminal' domains (HRDC1, HRDC2 and HRDC3) to regulate its activity. These HRDC domains have different influence on the biochemical functions of DrRecQ. Currently, only the structure of HRDC3 was reported. Here, we determined the NMR structure of the N-terminal-most HRDC1, revealing a potential DNA binding domain. Fluorescence anisotropy assay indicates that HRDC1 has binding affinity weaker than 70 mu M to all DNA substrates without any specificity. Biochemical assays suggested that HRDC1 cooperates with other domains to enhance full-length DrRecQ interactions with DNA. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| 收录类别 | SCI |
| WOS记录号 | WOS:000323458400024 |
| 公开日期 | 2016-05-03 |
| 源URL | [http://ir.ihep.ac.cn/handle/311005/224210]  |
| 专题 | 高能物理研究所_多学科研究中心 |
| 推荐引用方式 GB/T 7714 | Liu, SS,Zhang, W,Gao ZQ,et al. NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans[J]. FEBS LETTERS,2013,587(16):2635-2642. |
| APA | Liu, SS.,Zhang, W.,高增强.,Gao, ZQ.,Ming, QQ.,...&董宇辉.(2013).NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans.FEBS LETTERS,587(16),2635-2642. |
| MLA | Liu, SS,et al."NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans".FEBS LETTERS 587.16(2013):2635-2642. |
入库方式： OAI收割
来源：高能物理研究所
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