Reader domain specificity and lysine demethylase-4 family function

@inproceedings{Su2016ReaderDS,
  title={Reader domain specificity and lysine demethylase-4 family function},
  author={Zhangli Su and Fengbin Wang and Jin-Hee Lee and Kimberly E Stephens and Romeo Papazyan and Ekaterina Voronina and Kimberly A. Krautkramer and Ana Raman and Jeremy J Thorpe and Melissa D Boersma and Vyacheslav I. Kuznetsov and Mitchell D Miller and Sean D. Taverna and George N. Phillips and John M Denu},
  booktitle={Nature communications},
  year={2016}
}
The KDM4 histone demethylases are conserved epigenetic regulators linked to development, spermatogenesis and tumorigenesis. However, how the KDM4 family targets specific chromatin regions is largely unknown. Here, an extensive histone peptide microarray analysis uncovers trimethyl-lysine histone-binding preferences among the closely related KDM4 double tudor domains (DTDs). KDM4A/B DTDs bind strongly to H3K23me3, a poorly understood histone modification recently shown to be enriched in meiotic… CONTINUE READING
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