The structures of non-CG-repeat Z-DNAs co-crystallized with the Z-DNA-binding domain, hZαADAR1
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Ha-2009-The structures of non-CG-repeat Z-DNAs.pdf
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Author(s) • • • • •
Ha, Sung Chul
Choi, Jongkeun
Hwang, Hye-Yeon
Rich, Alexander
Kim, Yang-Gyun
Kim, Kyeong Kyu
Date Issued
December 2008
Journal
Nucleic Acids Research
Publisher
Oxford University Press
Citation
Ha, S. C. et al. “The Structures of non-CG-repeat Z-DNAs Co-crystallized with the Z-DNA-binding Domain, hZ[alpha]ADAR1.” Nucleic Acids Research 37.2 (2008): 629–637. Web.
Version
Final published version
Abstract
The Z-DNA conformation preferentially occurs at alternating purine-pyrimidine repeats, and is specifically recognized by Zα domains identified in several Z-DNA-binding proteins. The binding of Zα to foreign or chromosomal DNA in various sequence contexts is known to influence various biological functions, including the DNA-mediated innate immune response and transcriptional modulation of gene expression. For these reasons, understanding its binding mode and the conformational diversity of Zα bound Z-DNAs is of considerable importance. However, structural studies of Zα bound Z-DNA have been mostly limited to standard CG-repeat DNAs. Here, we have solved the crystal structures of three representative non-CG repeat DNAs, d(CACGTG)2, d(CGTACG)2 and d(CGGCCG)2 complexed to hZαADAR1 and compared those structures with that of hZαADAR1/d(CGCGCG)2 and the Zα-free Z-DNAs. hZαADAR1 bound to each of the three Z-DNAs showed a well conserved binding mode with very limited structural deviation irrespective of the DNA sequence, although varying numbers of residues were in contact with Z-DNA. Z-DNAs display less structural alterations in the Zα-bound state than in their free form, thereby suggesting that conformational diversities of Z-DNAs are restrained by the binding pocket of Zα. These data suggest that Z-DNAs are recognized by Zα through common conformational features regardless of the sequence and structural alterations.
MIT Department
Massachusetts Institute of Technology. Department of Biology
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DOI of Published Version
https://doi.org/10.1093/nar/gkn976