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

doi:10.1002/anie.201106432

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 journal › Article › peer-review

177 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 language	English
Pages (from-to)	1835-1839
Number of pages	5
Journal	Angewandte Chemie-International Edition
Volume	51
Issue number	8
DOIs	https://doi.org/10.1002/anie.201106432
Publication status	Published - 20 Feb 2012

Keywords

chromatin
enzymes
histone
phosphorylation
protein modifications
synthetic biology

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10.1002/anie.201106432

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

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Keywords

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