Premium
The Zβ domain of human DAI binds to Z‐DNA via a novel B–Z transition pathway
Author(s) -
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
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.01.043
Subject(s) - z dna , dna , hmg box , microbiology and biotechnology , dna binding site , protein–dna interaction , dna binding domain , dna clamp , binding domain , biology , dna binding protein , chemistry , binding site , biochemistry , gene , transcription factor , rna , gene expression , promoter , reverse transcriptase
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 NH 2 terminus. The hZβ 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 hZβ DAI with DNA duplex, d(CGCGCG) 2 , at a variety of protein‐to‐DNA molar ratios. The results suggest that hZβ DAI binds to Z‐DNA via an active‐di B–Z transition mechanism, where two hZβ DAI proteins bind to B‐DNA to form the hZβ 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.