Histone demethylation by a family of JmjC domain-containing proteins

Yu-ichi Tsukada, Jia Fang, Hediye Erdjument-Bromage, Maria E. Warren, Christoph H. Borchers, Paul Tempst and Yi Zhang ()
Additional contact information
Yu-ichi Tsukada: Howard Hughes Medical Institute
Jia Fang: Howard Hughes Medical Institute
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

Nature, 2006, vol. 439, issue 7078, 811-816

Abstract: 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.

Date: 2006
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/nature04433 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:439:y:2006:i:7078:d:10.1038_nature04433

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature04433

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().