期刊
NUCLEIC ACIDS RESEARCH
卷 42, 期 8, 页码 4859-4867出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gku134
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资金
- National Institutes of Health (NIH) [GM049245-20]
- Emory University School of Medicine
- U.S. Department of Energy, Office of Science
- Georgia Research Alliance Eminent Scholar
- Oxford University
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 angstrom 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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