Structural basis for Klf4 recognition of methylated DNA.

Structural basis for Klf4 recognition of methylated DNA.
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DOI:
10.1093/nar/gku134
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发表时间:
2014-04
影响因子:
14.9
通讯作者:
Cheng X
Cheng X
中科院分区:
生物学2区
文献类型:
--
作者:
Liu Y;Olanrewaju YO;Zheng Y;Hashimoto H;Blumenthal RM;Zhang X;Cheng X

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Transcription factor Krüppel-like factor 4 (Klf4), one of the factors directing cellular reprogramming, recognizes the CpG dinucleotide (whether methylated or unmodified) within a specific G/C-rich sequence. The binding affinity of the mouse Klf4 DNA-binding domain for methylated DNA is only slightly stronger than that for an unmodified oligonucleotide. The structure of the C-terminal three Krüppel-like zinc fingers (ZnFs) of mouse Klf4, in complex with fully methylated DNA, was determined at 1.85 Å resolution. An arginine and a glutamate interact with the methyl group. By comparison with two other recently characterized structures of ZnF protein complexes with methylated DNA, we propose a common principle of recognition of methylated CpG by C2H2 ZnF proteins, which involves a spatially conserved Arg–Glu pair.
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