ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression

@article{Shi2006ING2PD,
  title={ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression},
  author={Xiaobing Shi and T. Hong and Kay L. Walter and M. Ewalt and E. Michishita and T. Hung and Dylan Carney and P. Pe{\~n}a and F. Lan and M. Kaadige and N. Lacoste and Christelle Cayrou and F. Davrazou and Anjanabha Saha and B. Cairns and D. Ayer and T. Kutateladze and Yang Shi and J. C{\^o}t{\'e} and Katrin F Chua and O. Gozani},
  journal={Nature},
  year={2006},
  volume={442},
  pages={96-99}
}
Dynamic regulation of diverse nuclear processes is intimately linked to covalent modifications of chromatin. Much attention has focused on methylation at lysine 4 of histone H3 (H3K4), owing to its association with euchromatic genomic regions. H3K4 can be mono-, di- or tri-methylated. Trimethylated H3K4 (H3K4me3) is preferentially detected at active genes, and is proposed to promote gene expression through recognition by transcription-activating effector molecules. Here we identify a novel… Expand
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This work shows that a plant homeodomain (PHD) finger of nucleosome remodelling factor (NURF), an ISWI-containing ATP-dependent chromatin-remodelling complex, mediates a direct preferential association with H3K4me3 tails, and identifies a previously unknown function for the PHD finger as a highly specialized methyl-lysine-binding domain. Expand
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