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Nitsch, S. ; Zorro Shahidian, L. ; Schneider, R.

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

EMBO Rep. 22:e52774 (2021)
Verlagsversion 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.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Schlagwörter Acylation ; Chromatin ; Histones ; Metabolism ; Microdomains; Gene-expression; Lysine 2-hydroxyisobutyrylation; Phase-separation; Acetyl-coenzyme; Lateral Surface; In-vivo; Crotonylation; Transcription; Succinylation; Proteins
Sprache englisch
Veröffentlichungsjahr 2021
HGF-Berichtsjahr 2021
ISSN (print) / ISBN 1469-221X
e-ISSN 1469-3178
Zeitschrift EMBO Reports
Quellenangaben Band: 22, Heft: 7, Seiten: , Artikelnummer: e52774 Supplement: ,
Verlag EMBO Press
Verlagsort 111 River St, Hoboken 07030-5774, Nj Usa
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Functional Epigenetics (IFE)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Helmholtz Diabetes Center
PSP-Element(e) G-502800-001
Förderungen Helmholtz Gesellschaft
AMPro
DOI 10.15252/embr.202152774
WOS ID WOS:000664460300001
Scopus ID 85108364703
PubMed ID 34159701
Erfassungsdatum 2021-07-02
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