Cracking the histone code: one, two, three methyls, you're out!
In this issue of Molecular Cell, Zhang et al. report the structure of a ternary complex between the SET domain histone methyltransferase DIM-5, its cofactor, and a histone H3 peptide. The insight gained from analysis of a key amino acid provides an exciting opportunity to dissect the possible functional meaning of mono-, di-, and trimethylation of histone lysine residues in vivo that will complement existing approaches in the quest to crack the histone methylation code.
Dutnall
Robert N
RN
Section of Molecular Biology, Division of Biological Sciences, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.
D000595:Amino Acid Sequence / Q000235:genetics; D000818:Animals; D020134:Catalytic Domain / Q000235:genetics; D002467:Cell Nucleus / Q000235:genetics* / Q000378:metabolism; D005057:Eukaryotic Cells / Q000378:metabolism*; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000235:genetics / Q000378:metabolism*; D046911:Macromolecular Substances; D008745:Methylation; D008780:Methyltransferases / Q000235:genetics / Q000378:metabolism*; D011496:Protein Methyltransferases
D006657:Histones; D046911:Macromolecular Substances; D000076983:Histone Methyltransferases; D008780:Methyltransferases; D011496:Protein Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D008239:Lysine