NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Zα domains of yatapoxvirus E3L

Eun Hae Lee; Yeo Jin Seo; Hee Chul Ahn; Young Min Kang; Hee Eun Kim; Yeon Mi Lee; Byong Seok Choi; Joon Hwa Lee

doi:10.1016/j.febslet.2010.10.003

NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Zα domains of yatapoxvirus E3L

Eun Hae Lee, Yeo Jin Seo, Hee Chul Ahn, Young Min Kang, Hee Eun Kim, Yeon Mi Lee, Byong Seok Choi, Joon Hwa Lee

Department of Pharmacy

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

19 Scopus citations

Abstract

The Yaba-like disease viruses (YLDV) are members of the Yatapoxvirus family and have double-stranded DNA genomes. The E3L protein, which is essential for pathogenesis in the vaccinia virus, consists of two domains: an N-terminal Z-DNA binding domain and a C-terminal RNA binding domain. The crystal structure of the E3L orthologue of YLDV (yabZα_E3L) bound to Z-DNA revealed that the overall structure of yabZα_E3L and its interaction with Z-DNA are very similar to those of hZα_ADAR1. Here we have performed NMR hydrogen exchange experiments on the complexes between yabZα_E3L and d(CGCGCG)₂ with a variety of protein-to-DNA molar ratios. This study revealed that yabZα_E3L could efficiently change the B-form helix of the d(CGCGCG)₂ to left-handed Z-DNA via the active-mono B-Z transition pathway like hZα_ADAR1.

Original language	English
Pages (from-to)	4453-4457
Number of pages	5
Journal	FEBS Letters
Volume	584
Issue number	21
DOIs	https://doi.org/10.1016/j.febslet.2010.10.003
State	Published - 5 Nov 2010

Keywords

E3L
Hydrogen exchange
NMR
Poxvirus
Z-DNA
Z-DNA binding protein

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.febslet.2010.10.003

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title = "NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Zα domains of yatapoxvirus E3L",

abstract = "The Yaba-like disease viruses (YLDV) are members of the Yatapoxvirus family and have double-stranded DNA genomes. The E3L protein, which is essential for pathogenesis in the vaccinia virus, consists of two domains: an N-terminal Z-DNA binding domain and a C-terminal RNA binding domain. The crystal structure of the E3L orthologue of YLDV (yabZαE3L) bound to Z-DNA revealed that the overall structure of yabZαE3L and its interaction with Z-DNA are very similar to those of hZαADAR1. Here we have performed NMR hydrogen exchange experiments on the complexes between yabZαE3L and d(CGCGCG)2 with a variety of protein-to-DNA molar ratios. This study revealed that yabZαE3L could efficiently change the B-form helix of the d(CGCGCG)2 to left-handed Z-DNA via the active-mono B-Z transition pathway like hZαADAR1.",

keywords = "E3L, Hydrogen exchange, NMR, Poxvirus, Z-DNA, Z-DNA binding protein",

author = "Lee, {Eun Hae} and Seo, {Yeo Jin} and Ahn, {Hee Chul} and Kang, {Young Min} and Kim, {Hee Eun} and Lee, {Yeon Mi} and Choi, {Byong Seok} and Lee, {Joon Hwa}",

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doi = "10.1016/j.febslet.2010.10.003",

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T1 - NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Zα domains of yatapoxvirus E3L

AU - Lee, Eun Hae

AU - Seo, Yeo Jin

AU - Ahn, Hee Chul

AU - Kang, Young Min

AU - Kim, Hee Eun

AU - Lee, Yeon Mi

AU - Choi, Byong Seok

AU - Lee, Joon Hwa

PY - 2010/11/5

Y1 - 2010/11/5

N2 - The Yaba-like disease viruses (YLDV) are members of the Yatapoxvirus family and have double-stranded DNA genomes. The E3L protein, which is essential for pathogenesis in the vaccinia virus, consists of two domains: an N-terminal Z-DNA binding domain and a C-terminal RNA binding domain. The crystal structure of the E3L orthologue of YLDV (yabZαE3L) bound to Z-DNA revealed that the overall structure of yabZαE3L and its interaction with Z-DNA are very similar to those of hZαADAR1. Here we have performed NMR hydrogen exchange experiments on the complexes between yabZαE3L and d(CGCGCG)2 with a variety of protein-to-DNA molar ratios. This study revealed that yabZαE3L could efficiently change the B-form helix of the d(CGCGCG)2 to left-handed Z-DNA via the active-mono B-Z transition pathway like hZαADAR1.

AB - The Yaba-like disease viruses (YLDV) are members of the Yatapoxvirus family and have double-stranded DNA genomes. The E3L protein, which is essential for pathogenesis in the vaccinia virus, consists of two domains: an N-terminal Z-DNA binding domain and a C-terminal RNA binding domain. The crystal structure of the E3L orthologue of YLDV (yabZαE3L) bound to Z-DNA revealed that the overall structure of yabZαE3L and its interaction with Z-DNA are very similar to those of hZαADAR1. Here we have performed NMR hydrogen exchange experiments on the complexes between yabZαE3L and d(CGCGCG)2 with a variety of protein-to-DNA molar ratios. This study revealed that yabZαE3L could efficiently change the B-form helix of the d(CGCGCG)2 to left-handed Z-DNA via the active-mono B-Z transition pathway like hZαADAR1.

KW - E3L

KW - Hydrogen exchange

KW - NMR

KW - Poxvirus

KW - Z-DNA

KW - Z-DNA binding protein

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JF - FEBS Letters

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NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Zα domains of yatapoxvirus E3L

Abstract

Keywords

UN SDGs

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