Identification of non-histone substrates for JMJD2A-C histone demethylases

被引：44

作者：

Ponnaluri, V. K. Chaithanya ^{[1
]}

Vavilala, Divya Teja ^{[1
]}

Putty, Sandeep ^{[1
]}

Gutheil, William G. ^{[1
]}

Mukherji, Mridul ^{[1
]}

机构：

[1] Univ Missouri, Div Pharmaceut Sci, Sch Pharm, Kansas City, MO 64108 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2009年 / 390卷 / 02期

关键词：

Epigenetics; Demethylase; Dioxygenase; Enzyme assay; Transcription regulation; Jumonji domain; HYPOXIA-INDUCIBLE FACTOR; ANDROGEN RECEPTOR; HYDROXYLATION; PROTEINS; LYSINE-9; DOMAIN; CTBP; LSD1; H3;

D O I：

10.1016/j.bbrc.2009.09.107

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recent studies have shown that some Jumonji domain containing proteins demethylate tri- and dimethylated histone lysines by catalyzing a dioxygenase reaction. Here we report the substrate specificity of Jumonji domain-2 family histone demethylases (JMJD2A-C). A candidate substrate-based approach demonstrated that in addition to its known substrate, tri-methylated histone H3-lysine-9, JMJD2A-C demethylate trimethylated lysine containing peptides from WIZ, CDYL1, CSB and G9a proteins, all constituents of transcription repression complexes. Our results are consistent with lax substrate specificities observed for the iron (11), 2-oxoglutarate-dependent dioxygenases, and shed new light on signaling pathways regulated by Jumonji domain-2 family histone demethylases during epigenetic transcriptional regulation. (C) 2009 Elsevier Inc. All rights reserved.

引用

页码：280 / 284

页数：5

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