The hydroxylation activity of Jmjd6 is required for its homo-oligomerization

	The hydroxylation activity of Jmjd6 is required for its homo-oligomerization
	Han, G; Li, JJ; Wang, YQ; Li, X; Mao, HL; Liu, YF; Chen, CD
刊名	JOURNAL OF CELLULAR BIOCHEMISTRY
	2012
卷号	113 期号:5 页码:1663-1670
关键词	Jmjd6 ARGININE DEMETHYLATION HYDROXYLATION HOMO-OLIGOMERIZATION
通讯作者	Chen, CD (reprint author), 320 Yueyang Rd, Shanghai 200031, Peoples R China.,cdchen@sibs.ac.cn
英文摘要	Jumonji C-terminal (JmjC) domain-containing proteins are protein hydroxylases and histone demethylases that control gene expression. Jumonji domain-containing protein 6 (Jmjd6) is indispensable for embryonic development and has both histone arginine demethylase and lysyl-hydroxylase activities. The protein undergoes post-translational homo-oligomerization, but the underlying mechanism remains unknown. In this study, we examined the enzymatic activity of Jmjd6 and uncovered the mechanism underlying its homo-oligomerization. An in vitro enzymatic assay monitored by matrix-assisted laser desorption-ionization time-of-flight (MALDI-TOF) mass spectrometry indicates that Jmjd6 is unable to remove the methyl group from histone arginine residues but can hydroxylate the histone H4 tail at lysine residues in a 2-oxoglutarate (2-OG)- and Fe (II)-dependent manner. A mutational analysis reveals that the homo-oligomerization of Jmjd6 requires its enzymatic activity and the N- and C-termini. Using an in vitro enzymatic assay, we further demonstrate that Jmjd6 can hydroxylate its N-terminus but not its C-terminus. In summary, we did not detect arginine demethylase activity for Jmjd6, but we did confirm that it could catalyze the lysyl-hydroxylation of histone peptides. In addition, we demonstrated that the homo-oligomerization of Jmjd6 requires its own enzymatic activity and the N- and C-termini. We propose that Jmjd6 forms intermolecular covalent bonds between its N- and C-termini via autohydroxylation. J. Cell. Biochem. 113: 16631670, 2012. (C) 2011 Wiley Periodicals, Inc.
学科主题	Biochemistry & Molecular Biology; Cell Biology
类目[WOS]	Biochemistry & Molecular Biology ; Cell Biology
关键词[WOS]	DOMAIN-CONTAINING PROTEINS ; PHOSPHATIDYLSERINE RECEPTOR ; HISTONE DEMETHYLATION ; ARGININE METHYLATION ; APOPTOTIC CELLS ; COLLAGENS ; CLEARANCE ; ENZYMES ; DISEASE ; OXIDASE
收录类别	SCI
语种	英语
WOS记录号	WOS:000301524900022
内容类型	期刊论文
版本	出版稿
源URL	[http://202.127.25.143/handle/331003/602]
专题	上海生化细胞研究所_上海生科院生化细胞研究所
推荐引用方式 GB/T 7714	Han, G,Li, JJ,Wang, YQ,et al. The hydroxylation activity of Jmjd6 is required for its homo-oligomerization[J]. JOURNAL OF CELLULAR BIOCHEMISTRY,2012,113(5):1663-1670.
APA	Han, G.,Li, JJ.,Wang, YQ.,Li, X.,Mao, HL.,...&Chen, CD.(2012).The hydroxylation activity of Jmjd6 is required for its homo-oligomerization.JOURNAL OF CELLULAR BIOCHEMISTRY,113(5),1663-1670.
MLA	Han, G,et al."The hydroxylation activity of Jmjd6 is required for its homo-oligomerization".JOURNAL OF CELLULAR BIOCHEMISTRY 113.5(2012):1663-1670.