We have developed a readily accessible disulfide-directed methodology for the site-specific modification of histones by ubiquitin and ubiquitin-like proteins. The disulfide-linked analog of mono-ubiquitylated H2B stimulated the H3K79 methyltransferase activity of hDot1L to a similar extent as the native isopeptide linkage. This permitted structure-activity studies of ubiquitylated mononucleosomes that revealed plasticity in the mechanism of hDot1L stimulation and identified surfaces of ubiquitin important for activation.
|Original language||English (US)|
|Number of pages||3|
|Journal||Nature Chemical Biology|
|State||Published - Apr 2010|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology