Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases.

Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases. Research Abstract Details 

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Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases. Abstract Text:

Sunhwa Hong,Young-Wook Cho,Li-Rong Yu,Hong Yu,Timothy D Veenstra,Kai Ge,Sunhwa Hong,Young-Wook Cho,Li-Rong Yu,Hong Yu,Timothy D Veenstra,Kai Ge,

Covalent modifications of histones, such as acetylation and methylation, play important roles in the regulation of gene expression. Histone lysine methylation has been implicated in both gene activation and repression, depending on the specific lysine (K) residue that becomes methylated and the state of methylation (mono-, di-, or trimethylation). Methylation on K4, K9, and K36 of histone H3 has been shown to be reversible and can be removed by site-specific demethylases. However, the enzymes that antagonize methylation on K27 of histone H3 (H3K27), an epigenetic mark important for embryonic stem cell maintenance, Polycomb-mediated gene silencing, and X chromosome inactivation have been elusive. Here we show the JmjC domain-containing protein UTX (ubiquitously transcribed tetratricopeptide repeat, X chromosome), as well as the related JMJD3 (jumonji domain containing 3), specifically removes methyl marks on H3K27 in vitro. Further, the demethylase activity of UTX requires a catalytically active JmjC domain. Finally, overexpression of UTX and JMJD3 leads to reduced di- and trimethylation on H3K27 in cells, suggesting that UTX and JMJD3 may function as H3K27 demethylases in vivo. The identification of UTX and JMJD3 as H3K27-specific demethylases provides direct evidence to indicate that similar to methylation on K4, K9, and K36 of histone H3, methylation on H3K27 is also reversible and can be dynamically regulated by site-specific histone methyltransferases and demethylases.

Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases. Publishing Authors By Initials

S Hong,YW Cho,LR Yu,H Yu,TD Veenstra,K Ge,S Hong,YW Cho,LR Yu,H Yu,TD Veenstra,K Ge,

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Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Intr

Journal: Proceedings of the National Academy of Sciences of

VOLUME: 104

Page Numbers: 18439-44

Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.

ISSN: 1091-6490

DAY: 14

MONTH: 11

YEAR: 2007

Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases. Information

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LANGUAGE: eng

NlmUniqueID: 7505876

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Grant and Affiliation Information for Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases.

AFFILIATION: Nuclear Receptor Biology Section, Clinical Endocrinology Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Country: United States

AGENCY: United States NCI

GRANT: N01-CO-12400

ACRONYM: CO

MEDLINETA: Proc Natl Acad Sci U S A

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