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. 2010 Apr;6(4):267-9.
doi: 10.1038/nchembio.315. Epub 2010 Mar 7.

Disulfide-directed histone ubiquitylation reveals plasticity in hDot1L activation

Champak Chatterjee  1 , Robert K McGinty, Beat Fierz, Tom W Muir
Affiliations

Disulfide-directed histone ubiquitylation reveals plasticity in hDot1L activation

Champak Chatterjee et al. Nat Chem Biol. 2010 Apr.

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.

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