Studies on substrate specificity of Jmjd2a-c histone demethylases

被引：10

作者：

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

Vavilala, Divya Teja ^{[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 | 2011年 / 405卷 / 04期

关键词：

Epigenetics; Demethylase; Dioxygenase; Enzyme assay; Transcription regulation; Jumonji domain; PHYTANOYL-COA; 2-HYDROXYLASE; HYPOXIA-INDUCIBLE FACTOR; LYSINE METHYLTRANSFERASE; KAPPA-B; DOMAIN; METHYLATION; PROTEIN; H3; HYDROXYLATION; RECOGNITION;

D O I：

10.1016/j.bbrc.2011.01.073

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：

Jumonji domain containing iron (II), 2-oxoglutarate (2OG)-dependent dioxygenases from Jmjd2 family demethylate trimethylated histone3-lysine 9 (H3-K9me3), and also H3-K9me2 and H3-K36me3, albeit at lower rates. Recently, we have identified the first non-histone substrates of JmjD2 demethylases. Here, we studied the substrate specificity of Jmjd2a-c demethylases using site-directed mutagenesis and novel non-histone substrates. We identified preference of Arg at -1 position and a smaller amino acid at -2 position using both singly and doubly mutated peptide substrates by Jmjd2a-c demethylases. Our results also identified similarities in substrate selectivity by H3-K9 methyltransferase, G9a and Jmjd2 demethylases despite their distinct reaction mechanisms. Published by Elsevier Inc.

引用

页码：588 / 592

页数：5

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