Authors: | Lee, N.; Zhang, J.; Klose, R. J.; Erdjument-Bromage, H.; Tempst, P.; Jones, R. S.; Zhang, Y. |
Article Title: | The trithorax-group protein Lid is a histone H3 trimethyl-Lys4 demethylase |
Abstract: | Recent studies have demonstrated that histone methylation can be dynamically regulated through active demethylation. However, no demethylase specific to histone H3 trimethyl-Lys4 (H3K4me3) has been identified. Here we report that the Drosophila melanogaster protein 'little imaginal discs' (Lid), a JmjC domain-containing trithorax group protein, can demethylate H3K4me3. Consistent with its genetic classification, Lid positively regulates Hox gene expression in S2 cells. © 2007 Nature Publishing Group. |
Keywords: | protein expression; methylation; dna-binding proteins; nonhuman; genetic analysis; protein domain; phenotype; animals; gene expression; transcription factors; histone-lysine n-methyltransferase; histone h3; substrate specificity; protein transport; gene control; protein structure, tertiary; drosophila melanogaster; mutant proteins; drosophila proteins; rna polymerase ii; histones; lysine; larva; transferase |
Journal Title: | Nature Structural and Molecular Biology |
Volume: | 14 |
Issue: | 4 |
ISSN: | 1545-9993 |
Publisher: | Nature Publishing Group |
Date Published: | 2007-04-01 |
Start Page: | 341 |
End Page: | 343 |
Language: | English |
DOI: | 10.1038/nsmb1216 |
PUBMED: | 17351631 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | --- - "Cited By (since 1996): 41" - "Export Date: 17 November 2011" - "CODEN: NSMBC" - "Source: Scopus" |