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Angew Chem Int Ed Engl. 2016 Mar 14;55(12):4083-6. doi: 10.1002/anie.201511750. Epub 2016 Feb 23.

Dual Genetic Encoding of Acetyl-lysine and Non-deacetylatable Thioacetyl-lysine Mediated by Flexizyme.

Author information

1
Department of Molecular Biophysics and Biochemistry, Yale University, Whitney Avenue 266, New Haven, CT, 06511, USA.
2
Yale Center for Molecular Discovery, Yale University, West Haven, CT, 06516, USA.
3
Department of Chemistry, Yale University, 225 Prospect Street, New Haven, CT, 06511, USA.
4
Department of Molecular Biophysics and Biochemistry, Yale University, Whitney Avenue 266, New Haven, CT, 06511, USA. dieter.soll@yale.edu.
5
Department of Chemistry, Yale University, 225 Prospect Street, New Haven, CT, 06511, USA. dieter.soll@yale.edu.

Abstract

Acetylation of lysine residues is an important post-translational protein modification. Lysine acetylation in histones and its crosstalk with other post-translational modifications in histone and non-histone proteins are crucial to DNA replication, DNA repair, and transcriptional regulation. We incorporated acetyl-lysine (AcK) and the non-hydrolyzable thioacetyl-lysine (ThioAcK) into full-length proteins in vitro, mediated by flexizyme. ThioAcK and AcK were site-specifically incorporated at different lysine positions into human histone H3, either individually or in pairs. We demonstrate that the thioacetyl group in histone H3 could not be removed by the histone deacetylase sirtuin type 1. This method provides a powerful tool to study protein acetylation and its role in crosstalk between post-translational modifications.

KEYWORDS:

flexizyme; histone; lysine acetylation; post-translational modifications; thioacetyl-lysine

PMID:
26914285
PMCID:
PMC4789153
DOI:
10.1002/anie.201511750
[Indexed for MEDLINE]
Free PMC Article

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