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- 저자 : Lowenhaupt, Ky (검색결과 1 건)
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A peptide with alternating lysines can act as a highly specific Z-DNA binding domain
Kim, Yang-Gyun,Park, Hyun-Ju,Kim, Kyeong Kyu,Lowenhaupt, Ky,Rich, Alexander Oxford University Press 2006 Nucleic acids research Vol.34 No.17
<P>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) <I>FEBS Lett</I>., <B>279</B>, 253–255 and H. Takeuchi, N. Hanamura and I. Harada (1994) <I>J. Mol. Biol</I>., <B>236</B>, 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 <I>in vitro</I> and <I>in vivo</I>.</P>
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