Analysis of Jmjd6 cellular localization and testing for its involvement in histone demethylation.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Schofield, Christopher J
AffiliationDepartment of Experimental Mouse Genetics, Helmholtz Centre for Infection Research, Braunschweig, Germany.
MetadataShow full item record
AbstractBACKGROUND: Methylation of residues in histone tails is part of a network that regulates gene expression. JmjC domain containing proteins catalyze the oxidative removal of methyl groups on histone lysine residues. Here, we report studies to test the involvement of Jumonji domain-containing protein 6 (Jmjd6) in histone lysine demethylation. Jmjd6 has recently been shown to hydroxylate RNA splicing factors and is known to be essential for the differentiation of multiple tissues and cells during embryogenesis. However, there have been conflicting reports as to whether Jmjd6 is a histone-modifying enzyme. METHODOLOGY/PRINCIPAL FINDINGS: Immunolocalization studies reveal that Jmjd6 is distributed throughout the nucleoplasm outside of regions containing heterochromatic DNA, with occasional localization in nucleoli. During mitosis, Jmjd6 is excluded from the nucleus and reappears in the telophase of the cell cycle. Western blot analyses confirmed that Jmjd6 forms homo-multimers of different molecular weights in the nucleus and cytoplasm. A comparison of mono-, di-, and tri-methylation states of H3K4, H3K9, H3K27, H3K36, and H4K20 histone residues in wildtype and Jmjd6-knockout cells indicate that Jmjd6 is not involved in the demethylation of these histone lysine residues. This is further supported by overexpression of enzymatically active and inactive forms of Jmjd6 and subsequent analysis of histone methylation patterns by immunocytochemistry and western blot analysis. Finally, treatment of cells with RNase A and DNase I indicate that Jmjd6 may preferentially associate with RNA/RNA complexes and less likely with chromatin. CONCLUSIONS/SIGNIFICANCE: Taken together, our results provide further evidence that Jmjd6 is unlikely to be involved in histone lysine demethylation. We confirmed that Jmjd6 forms multimers and showed that nuclear localization of the protein involves association with a nucleic acid matrix.
CitationAnalysis of Jmjd6 cellular localization and testing for its involvement in histone demethylation. 2010, 5 (10):e13769 PLoS ONE
The following license files are associated with this item:
- Lysyl 5-hydroxylation, a novel histone modification, by Jumonji domain containing 6 (JMJD6).
- Authors: Unoki M, Masuda A, Dohmae N, Arita K, Yoshimatsu M, Iwai Y, Fukui Y, Ueda K, Hamamoto R, Shirakawa M, Sasaki H, Nakamura Y
- Issue date: 2013 Mar 1
- The hydroxylation activity of Jmjd6 is required for its homo-oligomerization.
- Authors: Han G, Li J, Wang Y, Li X, Mao H, Liu Y, Chen CD
- Issue date: 2012 May
- Redistribution of demethylated RNA helicase A during foot-and-mouth disease virus infection: role of Jumonji C-domain containing protein 6 in RHA demethylation.
- Authors: Lawrence P, Conderino JS, Rieder E
- Issue date: 2014 Mar
- Control of histone H3 lysine 9 (H3K9) methylation state via cooperative two-step demethylation by Jumonji domain containing 1A (JMJD1A) homodimer.
- Authors: Goda S, Isagawa T, Chikaoka Y, Kawamura T, Aburatani H
- Issue date: 2013 Dec 27
- JMJD6 is a histone arginine demethylase.
- Authors: Chang B, Chen Y, Zhao Y, Bruick RK
- Issue date: 2007 Oct 19