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The Zα domain of the editing enzyme dsRNA adenosine deaminase binds left-handed Z-RNA as well as Z-DNA

机译:编辑酶dsRNA腺苷脱氨酶的Zα结构域与左手Z-RNA以及Z-DNA结合

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The Zα domain of human double-stranded RNA adenosine deami- nase 1 binds specifically to left-handed Z-DNA and stabilizes the Z-conformation. Here we report spectroscopic and analytical re- sults that demonstrate that Zα can also stabilize the left-handed Z-conformation in double-stranded RNA. Zα induces a slow tran- sition 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 Zα. The specific binding of Z-RNA by Zα may be involved in targeting double-stranded RNA adenosine deami- nase 1 for a role in hypermutation of RNA viruses.
机译:人双链RNA腺苷脱氨酶1的Zα结构域与左手Z-DNA特异性结合,并稳定Z构象。在这里,我们报告了光谱和分析结果,这些结果表明Zα还可以稳定双链RNA中的左手Z构象。 Zα在双链体r(CG)_6中诱导从右旋A构型缓慢转变为Z形,活化能为38 kcal mol〜-1。我们得出结论,Z-RNA以及Z-DNA都可以容纳在Zα的定制结合位点中。 Zα对Z-RNA的特异性结合可能参与靶向双链RNA腺苷脱氨酶1,从而在RNA病毒的超突变中起作用。

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