解螺旋酶DrRecQ功能结构域HRDC1的结构和功能研究

摘要：

　　The RecQ helicase from Deinococcus radiodurans (DrRecQ) is unusual from other DNA helicases in that it utilizes its three ‘Helicase and RNaseD C-terminal” (HRDC1,2 and 3) domains to regulate its activity.Except its most C-terminal HRDC3 motif,the structures of other HRDC domains were never reported.In this study,we determined the solution structure of the separated and the most N-terminal DrRecQ HRDC1 domain,revealing a globular fold that resembles known DNA binding domains.We thus characterized its DNA-binding activities by fluorescence anisotropy assay,indicating that HRDC 1 does not preferentially bind to any DNA substrate,and it is just an auxiliary DNA binding domain of RecQ_Ct domain with weak binding affinities (KD > ~10 μM).

作者: 刘珊珊 张雯 明倩倩 高增强 侯海峰 蓝文贤 董宇辉 曹春阳

作者单位: 中国科学院上海有机化学研究所生命有机国家重点实验室,上海200032 中国科学院高能物理研究所,北京同步辐射光源,北京100049

会议类型: 国内会议

会议名称: 第十七届全国波谱学学术会议

会议地点: 厦门

会议语种:中文

页码: 217-218

在线出版日期: 2012-10-01（万方平台首次上网日期，不代表论文的发表时间）