PuSH - Publication Server of Helmholtz Zentrum München

Histone acylations and chromatin dynamics: Concepts, challenges, and links to metabolism.

EMBO Rep. 22:e52774 (2021)
Publ. Version/Full Text DOI PMC
Open Access Hybrid
Creative Commons Lizenzvertrag
In eukaryotic cells, DNA is tightly packed with the help of histone proteins into chromatin. Chromatin architecture can be modified by various post-translational modifications of histone proteins. For almost 60 years now, studies on histone lysine acetylation have unraveled the contribution of this acylation to an open chromatin state with increased DNA accessibility, permissive for gene expression. Additional complexity emerged from the discovery of other types of histone lysine acylations. The acyl group donors are products of cellular metabolism, and distinct histone acylations can link the metabolic state of a cell with chromatin architecture and contribute to cellular adaptation through changes in gene expression. Currently, various technical challenges limit our full understanding of the actual impact of most histone acylations on chromatin dynamics and of their biological relevance. In this review, we summarize the state of the art and provide an overview of approaches to overcome these challenges. We further discuss the concept of subnuclear metabolic niches that could regulate local CoA availability and thus couple cellular metabolisms with the epigenome.
Impact Factor
Scopus SNIP
Web of Science
Times Cited
Scopus
Cited By
Altmetric
8.807
1.577
4
31
Tags
Annotations
Special Publikation
Hide on homepage

Edit extra information
Edit own tags
Private
Edit own annotation
Private
Hide on publication lists
on hompage
Mark as special
publikation
Publication type Article: Journal article
Document type Review
Keywords Acylation ; Chromatin ; Histones ; Metabolism ; Microdomains; Gene-expression; Lysine 2-hydroxyisobutyrylation; Phase-separation; Acetyl-coenzyme; Lateral Surface; In-vivo; Crotonylation; Transcription; Succinylation; Proteins
Language english
Publication Year 2021
HGF-reported in Year 2021
ISSN (print) / ISBN 1469-221X
e-ISSN 1469-3178
Journal EMBO Reports
Quellenangaben Volume: 22, Issue: 7, Pages: , Article Number: e52774 Supplement: ,
Publisher EMBO Press
Publishing Place 111 River St, Hoboken 07030-5774, Nj Usa
Reviewing status Peer reviewed
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Helmholtz Diabetes Center
PSP Element(s) G-502800-001
Grants Helmholtz Gesellschaft
AMPro
Scopus ID 85108364703
PubMed ID 34159701
Erfassungsdatum 2021-07-02