Recognition of Histone H3 Lysine-4 Methylation by the Double Tudor Domain of JMJD2A

@article{Huang2006RecognitionOH,
  title={Recognition of Histone H3 Lysine-4 Methylation by the Double Tudor Domain of JMJD2A},
  author={Ying Huang and Jia Fang and Mark T. Bedford and Yi Zhang and Rui-Ming Xu},
  journal={Science},
  year={2006},
  volume={312},
  pages={748 - 751}
}
Biological responses to histone methylation critically depend on the faithful readout and transduction of the methyl-lysine signal by “effector” proteins, yet our understanding of methyl-lysine recognition has so far been limited to the study of histone binding by chromodomain and WD40-repeat proteins. The double tudor domain of JMJD2A, a Jmjc domain–containing histone demethylase, binds methylated histone H3-K4 and H4-K20. We found that the double tudor domain has an interdigitated structure… 
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TLDR
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TLDR
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TLDR
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TLDR
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Tudor domain of histone demethylase KDM4B is a reader of H4K20me3.
TLDR
The results showed that both HTD alone and the combination of HTD and PHD were able to specifically bind to H3K4me3 and H4K20me3, which is essential for KDM4B's rapid recruitment to DNA damage site.
Molecular recognition of histone H3 by the WD40 protein WDR5
TLDR
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