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Nucleic Acids Research Advance Access originally published online on November 5, 2007
Nucleic Acids Research 2007 35(22):7714-7720; doi:10.1093/nar/gkm748
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Nucleic Acids Research, 2007, Vol. 35, No. 22 7714-7720
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

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

Dong Van Quyen1, Sung Chul Ha1, Ky Lowenhaupt2, Alexander Rich2, Kyeong Kyu Kim1,* and Yang-Gyun Kim3,*

1Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea, 2Department of Biology, Massachusetts Institute of technology, Cambridge, MA 02139, USA and 3Department of Chemistry, School of Natural Sciences, Sungkyunkwan University, Suwon 440-746, Korea

*To whom correspondence should be addressed. Tel: +82 31 299 4563; Fax: +82 31 299 4575; Email: ygkimmit{at}skku.edu Correspondence may also be addressed to Kyeong Kyu Kim. Tel: 82 31 299 6136; Fax: 82 31 299 6159; Email: kkim{at}med.skku.ac.kr

Received July 5, 2007. Revised September 9, 2007. Accepted September 10, 2007.

The E3L gene is essential for pathogenesis in vaccinia virus. The E3L gene product consists of an N-terminal Z{alpha} domain and a C-terminal double-stranded RNA (dsRNA) binding domain; the left-handed Z-DNA-binding activity of the Z{alpha} 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 Z{alpha} domains play similar roles. To better understand the biological function of E3L proteins, we have investigated the Z-DNA-binding behavior of five representative Z{alpha} domains from poxviruses. Using surface plasmon resonance (SPR), we have demonstrated that these viral Z{alpha} domains bind Z-DNA tightly. Ability of Z{alpha}E3L converting B-DNA to Z-DNA was measured by circular dichroism (CD). The extents to which these Z{alpha}s 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 Z{alpha} 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 Z{alpha} proteins.


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 Proc. Natl. Acad. Sci. USAHome page
S. C. Ha, D. Kim, H.-Y. Hwang, A. Rich, Y.-G. Kim, and K. K. Kim
The crystal structure of the second Z-DNA binding domain of human DAI (ZBP1) in complex with Z-DNA reveals an unusual binding mode to Z-DNA
PNAS, December 30, 2008; 105(52): 20671 - 20676.
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