Identification of a specific inhibitor of the histone methyltransferase SU(VAR)3-9.
Histone methylation plays a key role in establishing and maintaining stable gene expression patterns during cellular differentiation and embryonic development. Here, we report the characterization of the fungal metabolite chaetocin as the first inhibitor of a lysine-specific histone methyltransferase. Chaetocin is specific for the methyltransferase SU(VAR)3-9 both in vitro and in vivo and may therefore be used to study heterochromatin-mediated gene repression.
Greiner
Dorothea
D
Adolf Butenandt Institute, Department of Molecular Biology, Histone Modifications Group, Ludwig-Maximillians University of Munich, Schillerstr. 44, 80336 Munich, Germany.
Bonaldi
Tiziana
T
Eskeland
Ragnhild
R
Roemer
Ernst
E
Imhof
Axel
A
D000818:Animals; D029721:Drosophila Proteins / Q000037:antagonists & inhibitors / Q000235:genetics; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase / Q000037:antagonists & inhibitors* / Q000145:classification; D008780:Methyltransferases / Q000037:antagonists & inhibitors*; D015394:Molecular Structure; D009183:Mycotoxins / Q000494:pharmacology*; D010879:Piperazines / Q000494:pharmacology; D011042:Poisons / Q000494:pharmacology*; D011496:Protein Methyltransferases; D011994:Recombinant Proteins / Q000037:antagonists & inhibitors / Q000235:genetics; D013379:Substrate Specificity
D029721:Drosophila Proteins; D009183:Mycotoxins; D010879:Piperazines; D011042:Poisons; D011994:Recombinant Proteins; C002511:chaetocin; D000076983:Histone Methyltransferases; D008780:Methyltransferases; D011496:Protein Methyltransferases; C445404:SU(VAR)3-9; D011495:Histone-Lysine N-Methyltransferase