Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC proteins (original) (raw)
- Brief Communication
- Published: 18 February 2007
- Gabrielle Cubberley1,
- Soojin Kim1,
- Matt Schonewald1,
- Lian Zhang1,
- Brian Tripet1 &
- …
- David L Bentley1
Nature Structural & Molecular Biology volume 14, pages 240–242 (2007)Cite this article
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Abstract
Histone H3 Lys4 trimethylation (H3-K4me3) is a conserved mark of actively transcribed chromatin. Using a conditional mutant of the yeast H3-K4 methyltransferase, Set1p, we demonstrate rapid turnover of H3-K4me3 and H3-K4me2 in vivo and show this process requires Yjr119Cp, of the JARID1 family of JmjC proteins. Ectopic overexpression of mouse Jarid1B, a Yjr119Cp homolog, greatly diminished H3-K4me3 and H3-K4me2 in HeLa cells, suggesting these proteins function as K4 demethylases in vivo.
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Acknowledgements
We thank M. Cleary (University of Iowa), D. Turner (University of Michigan) and A. Varshavsky (California Institute of Technology) for reagents, D. Gottschling, N. Fong, K. Glover and B. Erickson for discussion and technical help, and the Cancer Center sequencing facility of the University of Colorado Health Sciences Center. This work was supported by US National Institutes of Health grants R01GM063873 and T32-GM08730 to D.L.B. and D.J.S. D.J.S. is a member of the Medical Scientist Training Program.
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Authors and Affiliations
- Department of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, University of Colorado Health Sciences Center, MS8101, P.O. Box 6511, Aurora, 80045, Colorado, USA
David J Seward, Gabrielle Cubberley, Soojin Kim, Matt Schonewald, Lian Zhang, Brian Tripet & David L Bentley
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Correspondence toDavid L Bentley.
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Seward, D., Cubberley, G., Kim, S. et al. Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC proteins.Nat Struct Mol Biol 14, 240–242 (2007). https://doi.org/10.1038/nsmb1200
- Received: 29 November 2006
- Accepted: 10 January 2007
- Published: 18 February 2007
- Issue Date: March 2007
- DOI: https://doi.org/10.1038/nsmb1200