Exploring the Histone Acylome through Incorporation of γ-Thialysine on Histone Tails

Giordano Proietti, Giorgio Rainone, Jordi C J Hintzen, Jasmin Mecinović*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

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Abstract

Histone lysine acetyltransferases (KATs) catalyze the transfer of the acetyl group from acetyl Coenzyme A to lysine residues in histones and nonhistone proteins. Here, we report biomolecular studies on epigenetic acetylation and related acylation reactions of lysine and γ-thialysine, a cysteine-derived lysine mimic, which can be site-specifically introduced to histone peptides and histone proteins. Enzyme assays demonstrate that human KATs catalyze an efficient acetylation and propionylation of histone peptides that possess lysine and γ-thialysine. Enzyme kinetics analyses reveal that lysine- and γ-thialysine-containing histone peptides exhibit indistinguishable Km values, whereas small differences in kcat values were observed. This work highlights that γ-thialysine may act as a representative and easily accessible lysine mimic for chemical and biochemical examinations of post-translationally modified histones.

Original languageEnglish
JournalBioconjugate Chemistry
Volume31
Issue number3
Pages (from-to)844-851
ISSN1043-1802
DOIs
Publication statusPublished - 18. Mar 2020

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