来自耐辐射球菌的 RecQ 解旋酶的 N 端最 HRDC1 结构域的 NMR 结构。
NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans.
机构信息
State Key Laboratory of Bio-organic and Natural Product Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 345 Lingling Road, Shanghai 200032, China.
出版信息
FEBS Lett. 2013 Aug 19;587(16):2635-42. doi: 10.1016/j.febslet.2013.06.048. Epub 2013 Jul 4.
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 μM to all DNA substrates without any specificity. Biochemical assays suggested that HRDC1 cooperates with other domains to enhance full-length DrRecQ interactions with DNA.
耐辐射球菌（Deinococcus radiodurans）的 RecQ 解旋酶（DrRecQ）与其他解旋酶的不同之处在于，它利用其三个“解旋酶和 RNaseD C 端”结构域（HRDC1、HRDC2 和 HRDC3）来调节其活性。这些 HRDC 结构域对 DrRecQ 的生化功能有不同的影响。目前，仅报道了 HRDC3 的结构。在这里，我们确定了 HRDC1 最 N 端的 NMR 结构，揭示了一个潜在的 DNA 结合域。荧光各向异性测定表明，HRDC1 与所有 DNA 底物的结合亲和力均弱于 70 μM，且无任何特异性。生化测定表明，HRDC1 与其他结构域合作，增强全长 DrRecQ 与 DNA 的相互作用。
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