Diverse ways to be specific: a novel Zn-binding domain confers substrate specificity to UTX/KDM6A histone H3 Lys 27 demethylase
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.
- Publisher
- Cold Spring Harbor Lab Press
- Issue Date
- 2011-11
- Language
- English
- Article Type
- Article
- Keywords
METHYLTRANSFERASE COMPLEX; METHYLATION; JMJD2A; RECOGNITION; UTX
- Citation
GENES & DEVELOPMENT, v.25, no.21, pp.2223 - 2226
- ISSN
- 0890-9369
- Appears in Collection
- BS-Journal Papers(저널논문)
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