Premium
NMR study of hydrogen exchange during the B–Z transition of a DNA duplex induced by the Zα domains of yatapoxvirus E3L
Author(s) -
Lee Eun-Hae,
Seo Yeo-Jin,
Ahn Hee-Chul,
Kang Young-Min,
Kim Hee-Eun,
Lee Yeon-Mi,
Choi Byong-Seok,
Lee Joon-Hwa
Publication year - 2010
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.2010.10.003
Subject(s) - duplex (building) , transition (genetics) , chemistry , dna , biophysics , biochemistry , biology , gene
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 .