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Conversion of Cysteine into Dehydroalanine Enables Access to Synthetic Histones Bearing Diverse Post-Translational Modifications†
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The authors thank the Rhodes Trust, US NSF (J.M.C.); Cancer Research UK, EPSRC (L.L.); the Commonwealth Scholarship Commission, the Wellcome Trust (N.R.R.); Wellcome Trust, EU, BBSRC (C.J.S.); BBSRC, EPSRC (B.G.D.). B.G.D. is a recipient of a Royal Society Wolfson Research Merit Award. We thank Dr. Rob Klose (Biochemistry, Oxford) for H3-encoding plasmids.
Abstract
Six for the price of one: From a single precursor, dehydroalanine, six distinct post-translational modifications can be site-selectively installed on histone proteins (see figure), including the first site-selective phosphorylation and glycosylation of histones. Direct observation of histone deacetylase activity on a full-length modified histone as well as its interactions with both chromatin reader and writer/eraser proteins are reported.