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The Zα Domain of the Editing Enzyme dsRNA Adenosine Deaminase Binds Left-Handed Z-RNA as Well as Z-DNA
Bernard A. Brown II, Ky Lowenhaupt, Christina M. Wilbert, Eugene B. Hanlon and Alexander Rich
Proceedings of the National Academy of Sciences of the United States of America
Vol. 97, No. 25 (Dec. 5, 2000), pp. 13532-13536
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/2666404
Page Count: 5
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The Zα 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 Zα can also stabilize the left-handed Z-conformation in double-stranded RNA. Zα 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 Zα. The specific binding of Z-RNA by Zα may be involved in targeting double-stranded RNA adenosine deaminase 1 for a role in hypermutation of RNA viruses.
Proceedings of the National Academy of Sciences of the United States of America © 2000 National Academy of Sciences