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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@article{93b4e41abf0442ba9e370b048c4f65fc,

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\}",

year = "2010",

month = nov,

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

language = "English",

volume = "584",

pages = "4453--4457",

journal = "FEBS Letters",

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publisher = "John Wiley and Sons Inc",

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TY - JOUR

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

UR - https://www.scopus.com/pages/publications/78049290009

U2 - 10.1016/j.febslet.2010.10.003

DO - 10.1016/j.febslet.2010.10.003

M3 - Article

C2 - 20937275

AN - SCOPUS:78049290009

SN - 0014-5793

VL - 584

SP - 4453

EP - 4457

JO - FEBS Letters

JF - FEBS Letters

IS - 21

ER -

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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