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  4. Characterization of DNA-binding activity of Zα domains from poxviruses and the importance of the β-wing regions in converting B-DNA to Z-DNA

Characterization of DNA-binding activity of Zα domains from poxviruses and the importance of the β-wing regions in converting B-DNA to Z-DNA

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Author(s)
Quyen, Dong Van
•
Ha, Sung Chul
•
Kim, Kyeong Kyu
•
Kim, Yang-Gyun
•
Lowenhaupt, Ky
•
Rich, Alexander
Date Issued
November 2007
Journal
Nucleic Acids Research
Publisher
Oxford University Press (OUP)
Citation
Van Quyen, D. et al. “Characterization of DNA-binding Activity of Z  Domains from Poxviruses and the Importance of the -wing Regions in Converting B-DNA to Z-DNA.” Nucleic Acids Research 35.22 (2007): 7714–7720. Web. 1 June 2012.
Version
Final published version
Abstract
The E3L gene is essential for pathogenesis in vaccinia virus. The E3L gene product consists of an N-terminal Zα domain and a C-terminal double-stranded RNA (dsRNA) binding domain; the left-handed Z-DNA-binding activity of the Zα domain of E3L is required for viral pathogenicity in mice. E3L is highly conserved among poxviruses, including the smallpox virus, and it is likely that the orthologous Zα domains play similar roles. To better understand the biological function of E3L proteins, we have investigated the Z-DNA-binding behavior of five representative Zα domains from poxviruses. Using surface plasmon resonance (SPR), we have demonstrated that these viral Zα domains bind Z-DNA tightly. Ability of Zα[subscript E3L] converting B-DNA to Z-DNA was measured by circular dichroism (CD). The extents to which these Zαs can stabilize Z-DNA vary considerably. Mutational studies demonstrate that residues in the loop of the β-wing play an important role in this stabilization. Notably the Zα domain of vaccinia E3L acquires ability to convert B-DNA to Z-DNA by mutating amino acid residues in this region. Differences in the host cells of the various poxviruses may require different abilities to stabilize Z-DNA; this may be reflected in the observed differences in behavior in these Zα proteins.
MIT Department
Massachusetts Institute of Technology. Department of Biology
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Creative Commons Attribution Non-Commercial
http://creativecommons.org/licenses/by-nc/2.5
Persistent DSpace Link
http://hdl.handle.net/1721.1/70997
DOI of Published Version
https://doi.org/10.1093/nar/gkm748
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