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Zorro Shahidian, L. ; Haas, M.* ; Le Gras, S.* ; Nitsch, S. ; Mourao, A. ; Geerlof, A. ; Margueron, R.* ; Michaelis, J.* ; Daujat, S.* ; Schneider, R.

Succinylation of H3K122 destabilizes nucleosomes and enhances transcription.

EMBO Rep. 22:e51009 (2021)
Publ. Version/Full Text DOI
Open Access Gold (Paid Option)
Creative Commons Lizenzvertrag
Histone post-translational modifications (PTMs) are key players in chromatin regulation. The identification of novel histone acylations raises important questions regarding their role in transcription. In this study, we characterize the role of an acylation on the lateral surface of the histone octamer, H3K122 succinylation (H3K122succ), in chromatin function and transcription. Using chromatin succinylated at H3K122 in in vitro transcription assays, we show that the presence of H3K122succ is sufficient to stimulate transcription. In line with this, we found in our ChIP assays H3K122succ enriched on promoters of active genes and H3K122succ enrichment scaling with gene expression levels. Furthermore, we show that the co-activators p300/CBP can succinylate H3K122 and identify sirtuin 5 (SIRT5) as a new desuccinylase. By applying single molecule FRET assays, we demonstrate a direct effect of H3K122succ on nucleosome stability, indicating an important role for histone succinylation in modulating chromatin dynamics. Together, these data provide the first insights into the mechanisms underlying transcriptional regulation by H3K122succ.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Acylation ; Histones ; Succinylation
ISSN (print) / ISBN 1469-221X
e-ISSN 1469-3178
Journal EMBO Reports
Quellenangaben Volume: 22, Issue: 3, Pages: , Article Number: e51009 Supplement: ,
Publisher EMBO Press
Publishing Place 111 River St, Hoboken 07030-5774, Nj Usa
Reviewing status Peer reviewed
Grants Helmholtz Gesellschaft
Ampro Program
Epitrio Consortium
Deutsche Forschungsgemeinschaft