Kaiso uses all three zinc fingers and adjacent sequence motifs for high affinity binding to sequence-specific and methyl-CpG DNA targets.
Kaiso uses all three zinc fingers and adjacent sequence motifs for high affinity binding to sequence-specific and methyl-CpG DNA targets.
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DOI：
10.1016/j.febslet.2012.01.045
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发表时间：
2012-03-23
期刊：
影响因子：
3.5
通讯作者：
Wright PE
中科院分区：
文献类型：
--
作者：
Buck-Koehntop BA;Martinez-Yamout MA;Dyson HJ;Wright PE
Kaiso是一种Cys 2 His 2锌指蛋白，介导甲基CpG依赖性和序列特异性转录抑制。作为阐明识别这些不同DNA序列的结构和分子基础的第一步，Kaiso的最小结合区域被鉴定，并表征了高亲和力相互作用的最佳DNA序列。与以前的研究结果相反，Kaiso需要所有三个锌指加上相邻的蛋白质区域进行DNA识别。N-末端延伸有助于结构稳定性，而延伸的C-末端区域增强DNA结合。优化的Kaiso构建体和两个DNA序列之间形成的复合物适合于未来的结构评估。
Kaiso is a Cys2His2 zinc finger protein that mediates methyl-CpG -dependent and sequence-specific transcriptional repression. As a first step towards elucidating the structural and molecular basis for recognition of these disparate DNA sequences, the minimal binding region of Kaiso was identified and optimal DNA sequences for high-affinity interactions were characterized. Contrary to previous findings, Kaiso requires all three zinc fingers plus adjacent protein regions for DNA recognition. An N-terminal extension contributes to structural stability, while an extended C-terminal region augments DNA binding. Complexes formed between the optimized Kaiso construct and both DNA sequences are suitable for future structural evaluation.
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