Disulfide-directed histone ubiquitylation reveals plasticity in hDot1L activation

Champak Chatterjee, Robert K. McGinty, Beat Fierz, Tom W. Muir

Research output: Contribution to journalArticlepeer-review

215 Scopus citations


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 languageEnglish (US)
Pages (from-to)267-269
Number of pages3
JournalNature Chemical Biology
Issue number4
StatePublished - Apr 2010
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology


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