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Histone demethylation by a family of JmjC domain-containing proteins

Author

Listed:
  • Yu-ichi Tsukada

    (Howard Hughes Medical Institute
    University of North Carolina at Chapel Hill)

  • Jia Fang

    (Howard Hughes Medical Institute
    University of North Carolina at Chapel Hill)

  • Hediye Erdjument-Bromage

    (Memorial Sloan Kettering Cancer Center)

  • Maria E. Warren

    (University of North Carolina at Chapel Hill)

  • Christoph H. Borchers

    (University of North Carolina at Chapel Hill)

  • Paul Tempst

    (Memorial Sloan Kettering Cancer Center)

  • Yi Zhang

    (Howard Hughes Medical Institute
    University of North Carolina at Chapel Hill)

Abstract

Covalent modification of histones has an important role in regulating chromatin dynamics and transcription. Whereas most covalent histone modifications are reversible, until recently it was unknown whether methyl groups could be actively removed from histones. Using a biochemical assay coupled with chromatography, we have purified a novel JmjC domain-containing protein, JHDM1 (JmjC domain-containing histone demethylase 1), that specifically demethylates histone H3 at lysine 36 (H3-K36). In the presence of Fe(ii) and α-ketoglutarate, JHDM1 demethylates H3-methyl-K36 and generates formaldehyde and succinate. Overexpression of JHDM1 reduced the level of dimethyl-H3-K36 (H3K36me2) in vivo. The demethylase activity of the JmjC domain-containing proteins is conserved, as a JHDM1 homologue in Saccharomyces cerevisiae also has H3-K36 demethylase activity. Thus, we identify the JmjC domain as a novel demethylase signature motif and uncover a protein demethylation mechanism that is conserved from yeast to human.

Suggested Citation

  • Yu-ichi Tsukada & Jia Fang & Hediye Erdjument-Bromage & Maria E. Warren & Christoph H. Borchers & Paul Tempst & Yi Zhang, 2006. "Histone demethylation by a family of JmjC domain-containing proteins," Nature, Nature, vol. 439(7078), pages 811-816, February.
    • Handle: RePEc:nat:nature:v:439:y:2006:i:7078:d:10.1038_nature04433
    DOI: 10.1038/nature04433
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    Cited by:

    1. Lily L. Wong & Christina G. Bruxvoort & Nicholas I. Cejda & Matthew R. Delaney & Jannette Rodriguez Otero & David J. Forsthoefel, 2022. "Intestine-enriched apolipoprotein b orthologs are required for stem cell progeny differentiation and regeneration in planarians," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
    2. Fei Li & Yizhe Wang & Inah Hwang & Ja-Young Jang & Libo Xu & Zhong Deng & Eun Young Yu & Yiming Cai & Caizhi Wu & Zhenbo Han & Yu-Han Huang & Xiangao Huang & Ling Zhang & Jun Yao & Neal F. Lue & Paul , 2023. "Histone demethylase KDM2A is a selective vulnerability of cancers relying on alternative telomere maintenance," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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