编辑酶双链RNA腺苷脱氨酶的zalpha结构域可结合左旋Z-RNA以及Z-DNA。
The zalpha domain of the editing enzyme dsRNA adenosine deaminase binds left-handed Z-RNA as well as Z-DNA.
作者信息
Brown B A, Lowenhaupt K, Wilbert C M, Hanlon E B, Rich A
机构信息
Department of Biology and George R. Harrison Spectroscopy Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
出版信息
Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13532-6. doi: 10.1073/pnas.240464097.
Abstract
The Zalpha 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 Zalpha can also stabilize the left-handed Z-conformation in double-stranded RNA. Zalpha 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 Zalpha. The specific binding of Z-RNA by Zalpha may be involved in targeting double-stranded RNA adenosine deaminase 1 for a role in hypermutation of RNA viruses.
摘要
人双链RNA腺苷脱氨酶1的Zα结构域特异性结合左手Z-DNA并稳定Z构象。在此，我们报告的光谱和分析结果表明，Zα也能稳定双链RNA中的左手Z构象。Zα诱导双链r（CG）（6）从右手A构象缓慢转变为Z构象，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将双链RNA腺苷脱氨酶1靶向到RNA病毒高突变中发挥作用。
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