한빛사 논문
Abstract
Eunji Kim and Ji-Joon Song1
Department of Biological Sciences, Graduate School of Nanoscience and Technology (WCU), KAIST, Daejeon 305-701, South Korea
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.
Keywords
epigenetics, UTX/KDM6A, histone demethylase, jumonji domain, crystal structure, H3K27 methylation
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1Corrresponding author
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