Skip Navigation



Nucleic Acids Research Advance Access published online on November 5, 2007
Nucleic Acids Research, doi:10.1093/nar/gkm748
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (4079K) Freely available
Right arrow Screen PDF (586K) Freely available
Right arrow Supplementary Material
Right arrow Supplementary Data
Right arrowOA All Versions of this Article:
35/22/7714    most recent
gkm748v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Quyen, D. V.
Right arrow Articles by Kim, Y.-G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Quyen, D. V.
Right arrow Articles by Kim, Y.-G.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 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 ß-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 ß-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.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 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.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.