Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 38, Issue 4, Pages 177-183Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2012.12.005
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Funding
- US National Institutes of Health [GM049245-19]
- National Science Foundation [MCB-0964728]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0964728] Funding Source: National Science Foundation
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Much is known about vertebrate DNA methylation, however it is not known how methylated CpG within particular sequences is recognized. Two recent structures of C2H2 zinc finger (ZnF) proteins in complex with methylated DNA reveal a common recognition mode for 5-methylcytosine (5mC) that involves a 5mC-Arg-G triad. In the two ZnF proteins, an arginine that precedes the first Zn-binding histidine (RH motif) can interact with a 5mCpG or TpG dinucleotide. Among a family of >300 human Kruppel-associated box (KRAB) domain containing ZnF proteins examined, two-thirds contained at least one ZnF that included an RH motif. We propose that the RH-ZnF motifs provide specificity for 5mCpG, whereas the neighboring Zn fingers recognize the surrounding DNA sequence context.
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