Lysyl 5-hydroxylation, a novel histone modification, by jumonji domain containing 6 (JMJD6)

Motoko Unoki, Akiko Masuda, Naoshi Dohmae, Kyohei Arita, Masanori Yoshimatsu, Yukiko Iwai, Yoshinori Fukui, Koji Ueda, Ryuji Hamamoto, Masahiro Shirakawa, Hiroyuki Sasaki, Yusuke Nakamura

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107 Citations (Scopus)


JMJD6 is reported to hydroxylate lysyl residues of a splicing factor, U2AF65. In this study, we found that JMJD6 hydroxylates histone lysyl residues. In vitro experiments showed that JMJD6 has a binding affinity to histone proteins and hydroxylates multiple lysyl residues of histone H3 and H4 tails. Using JMJD6 knock-out mouse embryos, we revealed that JMJD6 hydroxylates lysyl residues of histones H2A/H2B and H3/H4 in vivo by amino acid composition analysis. 5-Hydroxylysine was detected at the highest level in histones purified from murine testis, which expressed JMJD6 at a significantly high level among various tissues examined, and JMJD6 overexpression increased the amount of 5-hydroxylysine in histones in human embryonic kidney 293 cells. These results indicate that histones are additional substrates of JMJD6 in vivo. Because 5-hydroxylation of lysyl residues inhibited N-acetylation and N-methylation by an acetyltransferase and a methyltransferase, respectively, in vitro, histone 5-hydroxylation may have important roles in epigenetic regulation of gene transcription or chromosomal rearrangement.

Original languageEnglish
Pages (from-to)6053-6062
Number of pages10
JournalJournal of Biological Chemistry
Issue number9
Publication statusPublished - Mar 1 2013

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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