Disulfide-directed histone ubiquitylation reveals plasticity in hDot1L activation

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.


Published in:
Nature chemical biology, 6, 4, 267-9
Year:
2010
ISSN:
1552-4469
Laboratories:




 Record created 2012-10-15, last modified 2018-09-13


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