The trithorax-group protein Lid is a histone H3 trimethyl-Lys4 demethylase Journal Article


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"
Altmetric
Citation Impact
BMJ Impact Analytics
MSK Authors
  1. Paul J Tempst
    324 Tempst