Conversion of Cysteine into Dehydroalanine Enables Access to Synthetic Histones Bearing Diverse Post-Translational Modifications

Justin Chalker, Lukas Lercher, Nathan Rose, Christopher Schofield, Benjamin Davis

    Research output: Contribution to journalArticlepeer-review

    127 Citations (Scopus)

    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.

    Original languageEnglish
    Pages (from-to)1835-1839
    Number of pages5
    JournalAngewandte Chemie-International Edition
    Volume51
    Issue number8
    DOIs
    Publication statusPublished - 20 Feb 2012

    Keywords

    • chromatin
    • enzymes
    • histone
    • phosphorylation
    • protein modifications
    • synthetic biology

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