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- Title
The Zβ domain of human DAI binds to Z-DNA via a novel B–Z transition pathway
- Authors
Kim, Hee-Eun; Ahn, Hee-Chul; Lee, Yeon-Mi; Lee, Eun-Hae; Seo, Yeo-Jin; Kim, Yang-Gyun; Kim, Kyeong Kyu; Choi, Byong-Seok; Lee, Joon-Hwa
- Abstract
Abstract: The human DNA-dependent activator of IFN-regulatory factor (DAI) protein, which activates the innate immune response in response to DNA, contains two tandem Z-DNA binding domains (Zα and Zβ) at the NH2 terminus. The hZβDAI structure is similar to other Z-DNA binding proteins, although it demonstrates an unusual Z-DNA recognition. We performed NMR experiments on complexes of hZβDAI with DNA duplex, d(CGCGCG)2, at a variety of protein-to-DNA molar ratios. The results suggest that hZβDAI binds to Z-DNA via an active-di B–Z transition mechanism, where two hZβDAI proteins bind to B-DNA to form the hZβDAI–B-DNA complex; the B-DNA is subsequently converted to left-handed Z-DNA. This novel mechanism of DNA binding and B–Z conversion is distinct from Z-DNA binding of the human ADAR1 protein.
- Subjects
DNA-binding proteins; CARRIER proteins; INTERFERONS; NATURAL immunity; IMMUNE response; NUCLEAR magnetic resonance
- Publication
FEBS Letters, 2011, Vol 585, Issue 5, p772
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2011.01.043