Abstract
The histone H3 lysine 4 demethylase RBP2 contains a DNA binding domain, the AT-rich interaction domain (ARID). We solved the structure of ARID by NMR, identified its DNA binding motif (CCGCCC) and characterized the binding contacts. Immunofluorescence and luciferase assays indicated that ARID is required for RBP2 demethylase activity in cells and that DNA recognition is essential to regulate transcription.
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Acknowledgements
We thank B. Lamarche and H.-M. Shih for useful discussion, W. Hong at the Institute of Molecular and Cell Biology, Singapore, for providing RBP2 plasmids, and W.G. Kaelin, Jr. at Harvard Medical School, Boston, for BRD2 promoter construct and the RBP2 antibody. NMR was performed at Campus Chemical Instrument Center of Ohio State University and the National Research Program for Genomic Medicine (Taiwan) NMR Core. This work was supported by funding from the Genomics Research Center (to L.-J.J. and M.-D.T.), and research grant DOH96-TD-G-111-003 from National Research Program for Genomic Medicine of Taiwan (to L.-J.J.) and CA69472 from US National Institutes of Health (to M.-D.T.).
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S.T., Y.-T.W., L.-J.J. and M.-D.T. designed the research; S.T., Y.-C.T., C.Y., M.-Y.C., A.-N.C. and P.-H.L. performed the research; S.T., L.-J.J. and M.-D.T. analyzed the data and wrote the paper.
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Supplementary figures 1–6, Tables 1–3 and Methods (PDF 1120 kb)
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Tu, S., Teng, YC., Yuan, C. et al. The ARID domain of the H3K4 demethylase RBP2 binds to a DNA CCGCCC motif. Nat Struct Mol Biol 15, 419–421 (2008). https://doi.org/10.1038/nsmb.1400
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DOI: https://doi.org/10.1038/nsmb.1400
