ArticleNucleic acids research2006
A peptide with alternating lysines can act as a highly specific Z-DNA binding domain.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Z-DNA Hunter tool for straightforward detection of Z-DNA forming regions and a case study inNAR genomics and bioinformatics · 2025Article
- Variola virus E3L Zα domain, but not its Z-DNA binding activity, is required for PKR inhibition.RNA (New York, N.Y.) · 2014Article
- Coupled folding and specific binding: fishing for amphiphilicity.International journal of molecular sciences · 2011Review
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Authors and funding
5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Many nucleic acid binding proteins use short peptide sequences to provide specificity in recognizing their targets, which may be either a specific sequence or a conformation. Peptides containing alternating lysine have been shown to bind to poly(dG-d5meC) in the Z conformation, and stabilize the higher energy form [H. Takeuchi, N. Hanamura, H. Hayasaka and I. Harada (1991) FEBS Lett., 279, 253-255 and H. Takeuchi, N. Hanamura and I. Harada (1994) J. Mol. Biol., 236, 610-617.]. Here we report the construction of a Z-DNA specific binding protein, with the peptide KGKGKGK as a functional domain and a leucine zipper as a dimerization domain. The resultant protein, KGZIP, induces the Z conformation in poly(dG-d5meC) and binds to Z-DNA stabilized by bromination with high affinity and specificity. The binding of KGZIP is sufficient to convert poly(dG-d5meC) from the B to the Z form, as shown by circular dichroism. The sequence KGKGKGK is found in many proteins, although no functional role has been established. KGZIP also has potential for engineering other Z-DNA specific proteins for future studies of Z-DNA in vitro and in vivo.
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