The Zα domain of the editing enzyme dsRNA adenosine deaminase binds left-handed Z-RNA as well as Z-DNA
The Zα domain of the editing enzyme dsRNA adenosine deaminase binds left-handed Z-RNA as well as Z-DNA
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DOI：
10.1073/pnas.240464097
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发表时间：
2000-12-05
影响因子：
11.1
通讯作者：
Rich, A
中科院分区：
文献类型：
--
作者：
Brown, BA;Lowenhaupt, K;Rich, A
人双链RNA腺苷脱氨酶1的Z α结构域特异性结合左旋Z-DNA并稳定Z构象。在这里，我们报告的光谱和分析结果表明，Z α也可以稳定的左手Z-构象的双链RNA。Z α诱导双链体r（CG）（6）从右旋A-构象缓慢转变为Z-构象，活化能为38 kcal mol（-1）。我们的结论是，Z-RNA以及Z-DNA可以容纳在定制的结合位点的Z α。Z-RNA与Z α的特异性结合可能涉及靶向双链RNA腺苷脱氨酶1，以在RNA病毒的超突变中发挥作用。
The Z alpha domain of human double-stranded RNA adenosine deaminase 1 binds specifically to left-handed Z-DNA and stabilizes the Z-conformation. Here we report spectroscopic and analytical results that demonstrate that Z alpha can also stabilize the left-handed Z-conformation in double-stranded RNA. Z alpha induces a slow transition from the right-handed A-conformation to the Z-form in duplex r(CG)(6), with an activation energy of 38 kcal mol(-1). We conclude that Z-RNA as well as Z-DNA can be accommodated in the tailored binding site of Z alpha. The specific binding of Z-RNA by Z alpha may be involved in targeting double-stranded RNA adenosine deaminase 1 for a role in hypermutation of RNA viruses.