| First Author | Liu Y | Year | 2014 |
| Journal | Nucleic Acids Res | Volume | 42 |
| Issue | 8 | Pages | 4859-67 |
| PubMed ID | 24520114 | Mgi Jnum | J:212988 |
| Mgi Id | MGI:5582663 | Doi | 10.1093/nar/gku134 |
| Citation | Liu Y, et al. (2014) Structural basis for Klf4 recognition of methylated DNA. Nucleic Acids Res 42(8):4859-67 |
| abstractText | Transcription factor Kruppel-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 Kruppel-like zinc fingers (ZnFs) of mouse Klf4, in complex with fully methylated DNA, was determined at 1.85 A 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. |
