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Conversion of Cysteine into Dehydroalanine Enables Access to Synthetic Histones Bearing Diverse Post‐Translational Modifications
Author(s) -
Chalker Justin M.,
Lercher Lukas,
Rose Nathan R.,
Schofield Christopher J.,
Davis Benjamin G.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201106432
Subject(s) - dehydroalanine , histone , chemistry , posttranslational modification , histone deacetylase , glycosylation , microbiology and biotechnology , histone modifying enzymes , chromatin , biochemistry , histone h2a , biology , dna , enzyme , peptide
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.