Diverse ways to be specific: A novel zn-binding domain confers substrate specificity to UTX/KDM6a histone H3 lys 27 demethylase

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Abstract

Histone methylations are highly regulated by site-specific histone methyltransferases and demethylases. In this issue of Genes & Development, Sengoku and Yokoyama (pp. 2266-2277) demonstrate that a novel Zn-binding domain and the Jumonji domain of UTX/KDM6A (Lys demethylase 6A) recognize histone H3 and together function as a substrate specificity determinant for H3K27 demethylation. This study demonstrates the mechanism of site-specific demethylation by UTX/KDM6A and implicates that histone demethylases use diverse methods to accomplish target specificity.

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Kim, E., & Song, J. J. (2011). Diverse ways to be specific: A novel zn-binding domain confers substrate specificity to UTX/KDM6a histone H3 lys 27 demethylase. Genes and Development, 25(21), 223–2226. https://doi.org/10.1101/gad.179473.111

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