A left-handed RNA double helix bound by the Zα domain of the RNA-editing enzyme ADAR1
A left-handed RNA double helix bound by the Zα domain of the RNA-editing enzyme ADAR1
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DOI：
10.1016/j.str.2007.03.001
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发表时间：
2007-04-01
期刊：
影响因子：
5.7
通讯作者：
Athanasiadis, Alekos
中科院分区：
文献类型：
--
作者：
Placido, Diana;Brown, Bernard A., II;Athanasiadis, Alekos
A型RNA双螺旋可以转化为左手螺旋，称为Z-RNA。目前，对Z-RNA的详细结构特征或其参与细胞过程知之甚少。某些干扰素反应蛋白具有能够稳定Z-RNA和Z-DNA的结构域的发现为Z-RNA的研究开辟了道路。在这里，我们展示了RNA编辑酶ADAR 1（双链RNA腺苷脱氨酶）与dUr（CG）（3）双链RNA复合的Z α结构域的2.25埃晶体结构。Z-RNA螺旋与一种独特的溶剂模式相关联，这种溶剂模式将其与Z-DNA的其他相似构象区分开来。基于结构，我们提出了一个模型，表明溶剂化的差异如何导致两种类型的Z-RNA结构。Z alpha与Z-RNA的相互作用证明了干扰素诱导的ADAR 1亚型如何靶向含有嘌呤-嘧啶重复序列的选定dsRNA，可能是病毒来源。
The A form RNA double helix can be transformed to a left-handed helix, called Z-RNA. Currently, little is known about the detailed structural features of Z-RNA or its involvement in cellular processes. The discovery that certain interferon-response proteins have domains that can stabilize Z-RNA as well as Z-DNA opens the way for the study of Z-RNA. Here, we present the 2.25 angstrom crystal structure of the Z alpha domain of the RNA-editing enzyme ADAR1 (double-stranded RNA adenosine deaminase) complexed to a dUr(CG)(3) duplex RNA. The Z-RNA helix is associated with a unique solvent pattern that distinguishes it from the otherwise similar conformation of Z-DNA. Based on the structure, we propose a model suggesting how differences in solvation lead to two types of Z-RNA structures. The interaction of Z alpha with Z-RNA demonstrates how the interferon-induced isoform of ADAR1 could be targeted toward selected dsRNAs containing purine-pyrimidine repeats, possibly of viral origin.