Abstract
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) |
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Pages (from-to) | 267-269 |
Number of pages | 3 |
Journal | Nature Chemical Biology |
Volume | 6 |
Issue number | 4 |
DOIs | |
State | Published - Apr 2010 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology