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

Hee Eun Kim; Hee Chul Ahn; Yeon Mi Lee; Eun Hae Lee; Yeo Jin Seo; Yang Gyun Kim; Kyeong Kyu Kim; Byong Seok Choi; Joon Hwa Lee

doi:10.1016/j.febslet.2011.01.043

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

Hee Eun Kim, Hee Chul Ahn, Yeon Mi Lee, Eun Hae Lee, Yeo Jin Seo, Yang Gyun Kim, Kyeong Kyu Kim, Byong Seok Choi, Joon Hwa Lee

Department of Pharmacy

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

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 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.

Original language	English
Pages (from-to)	772-778
Number of pages	7
Journal	FEBS Letters
Volume	585
Issue number	5
DOIs	https://doi.org/10.1016/j.febslet.2011.01.043
State	Published - 9 Mar 2011

Keywords

B-Z transition
DNA-protein interaction
Hydrogen exchange
NMR
Z-DNA
Z-DNA binding protein

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10.1016/j.febslet.2011.01.043

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title = "The Zβ domain of human DAI binds to Z-DNA via a novel B-Z transition pathway",

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.",

keywords = "B-Z transition, DNA-protein interaction, Hydrogen exchange, NMR, Z-DNA, Z-DNA binding protein",

author = "Kim, {Hee Eun} and Ahn, {Hee Chul} and Lee, {Yeon Mi} and Lee, {Eun Hae} and Seo, {Yeo Jin} and Kim, {Yang Gyun} and Kim, {Kyeong Kyu} and Choi, {Byong Seok} and Lee, {Joon Hwa}",

year = "2011",

month = mar,

day = "9",

doi = "10.1016/j.febslet.2011.01.043",

language = "English",

volume = "585",

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T1 - The Zβ domain of human DAI binds to Z-DNA via a novel B-Z transition pathway

AU - Kim, Hee Eun

AU - Ahn, Hee Chul

AU - Lee, Yeon Mi

AU - Lee, Eun Hae

AU - Seo, Yeo Jin

AU - Kim, Yang Gyun

AU - Kim, Kyeong Kyu

AU - Choi, Byong Seok

AU - Lee, Joon Hwa

PY - 2011/3/9

Y1 - 2011/3/9

N2 - 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.

AB - 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.

KW - B-Z transition

KW - DNA-protein interaction

KW - Hydrogen exchange

KW - NMR

KW - Z-DNA

KW - Z-DNA binding protein

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SN - 0014-5793

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EP - 778

JO - FEBS Letters

JF - FEBS Letters

IS - 5

ER -

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

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Keywords

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