The Z beta domain of human DAI binds to Z-DNA via a novel B-Z transition pathway

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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 (Z alpha and Z beta) at the NH(2) terminus. The hZ beta(DAI) structure is similar to other Z-DNA binding proteins, although it demonstrates an unusual Z-DNA recognition. We performed NMR experiments on complexes of hZ beta(DAI) with DNA duplex, d(CGCGCG)(2), at a variety of protein-to-DNA molar ratios. The results suggest that hZ beta(DAI) binds to Z-DNA via an active-di B-Z transition mechanism, where two hZ beta(DAI) proteins bind to B-DNA to form the hZ beta(DAI)-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. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publisher
ELSEVIER SCIENCE BV
Issue Date
2011-03
Language
English
Article Type
Article
Keywords

Z-ALPHA DOMAIN; HANDED Z-DNA; CRYSTAL-STRUCTURE; PROTON-EXCHANGE; HUMAN ADAR1; KINETICS; DUPLEXES; COMPLEX; ZBP1; THERMODYNAMICS

Citation

FEBS LETTERS, v.585, no.5, pp.772 - 778

ISSN
0014-5793
DOI
10.1016/j.febslet.2011.01.043
URI
http://hdl.handle.net/10203/98552
Appears in Collection
CH-Journal Papers(저널논문)
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