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http://purl.uniprot.org/citations/22189873http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22189873http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22189873http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.org/dc/terms/identifier"doi:10.1002/jcb.24035"xsd:string
http://purl.uniprot.org/citations/22189873http://purl.org/dc/terms/identifier"doi:10.1002/jcb.24035"xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/author"Han G."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/author"Han G."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/author"Liu Y."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/author"Liu Y."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/author"Li J."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/author"Li J."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/author"Li X."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/author"Li X."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/author"Mao H."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/author"Mao H."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/author"Wang Y."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/author"Wang Y."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/author"Chen C.D."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/author"Chen C.D."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/name"J. Cell. Biochem."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/name"J. Cell. Biochem."xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/pages"1663-1670"xsd:string
http://purl.uniprot.org/citations/22189873http://purl.uniprot.org/core/pages"1663-1670"xsd:string