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Characterization of histone acylations links chromatin modifications with metabolism
Journal article   Open access   Peer reviewed

Characterization of histone acylations links chromatin modifications with metabolism

Johayra Simithy, Simone Sidoli, Zuo-Fei Yuan, Mariel Coradin, Natarajan V Bhanu, Dylan M Marchione, Brianna J Klein, Gleb A Bazilevsky, Cheryl E McCullough, Robert S Magin, …
Nature communications, v 8(1), 1141
26 Oct 2017
PMID: 29070843
url
https://doi.org/10.1038/s41467-017-01384-9View
Published, Version of Record (VoR)CC BY V4.0 Open

Abstract

Over the last decade, numerous histone acyl post-translational modifications (acyl-PTMs) have been discovered, of which the functional significance is still under intense study. Here, we use high-resolution mass spectrometry to accurately quantify eight acyl-PTMs in vivo and after in vitro enzymatic assays. We assess the ability of seven histone acetyltransferases (HATs) to catalyze acylations on histones in vitro using short-chain acyl-CoA donors, proving that they are less efficient towards larger acyl-CoAs. We also observe that acyl-CoAs can acylate histones through non-enzymatic mechanisms. Using integrated metabolomic and proteomic approaches, we achieve high correlation (R  > 0.99) between the abundance of acyl-CoAs and their corresponding acyl-PTMs. Moreover, we observe a dose-dependent increase in histone acyl-PTM abundances in response to acyl-CoA supplementation in in nucleo reactions. This study represents a comprehensive profiling of scarcely investigated low-abundance histone marks, revealing that concentrations of acyl-CoAs affect histone acyl-PTM abundances by both enzymatic and non-enzymatic mechanisms.

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Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
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