Brief Communication abstract
Nature Structural & Molecular Biology 14, 240 - 242 (2007)
Published online: 18 February 2007 | doi:10.1038/nsmb1200
Demethylation of trimethylated histone H3 Lys4
in vivo by JARID1 JmjC proteins
David J Seward1, Gabrielle Cubberley1, Soojin Kim1, Matt Schonewald1, Lian Zhang1, Brian Tripet1 & David L Bentley1
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.
- Department of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, University of Colorado Health Sciences Center, MS8101, P.O. Box 6511, Aurora, Colorado 80045, USA.
Correspondence to: David L Bentley1 e-mail: david.bentley@uchsc.edu
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
The expanding world of histone lysine demethylasesNature Structural & Molecular Biology News and Views (01 Apr 2007)
RESEARCH
Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylaseNature Structural & Molecular Biology Article (01 Aug 2007)
See all 20 matches for Research
