Restraining and unleashing chromatin remodelers - structural information guides chromatin plasticity.


Journal

Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784

Informations de publication

Date de publication:
12 2020
Historique:
received: 27 03 2020
revised: 06 06 2020
accepted: 16 06 2020
pubmed: 22 7 2020
medline: 16 10 2021
entrez: 22 7 2020
Statut: ppublish

Résumé

Chromatin remodeling enzymes are large molecular machines that guard the genome by reorganizing chromatin structure. They can reposition, space and evict nucleosomes and thus control gene expression, DNA replication and repair. Recent cryo-electron microscopy (cryo-EM) analyses have captured snapshots of various chromatin remodelers as they interact with nucleosomes. In this review, we summarize and discuss the advances made in our understanding of the regulation of chromatin remodelers, the mode of DNA translocation, as well as the influence of associated protein domains and remodeler subunits on the specific functions of chromatin remodeling complexes. The emerging structural information will help our understanding of disease mechanisms and guide our knowledge toward innovative therapeutic interventions.

Identifiants

pubmed: 32693313
pii: S0959-440X(20)30108-1
doi: 10.1016/j.sbi.2020.06.008
pii:
doi:

Substances chimiques

Chromatin 0
Nucleosomes 0
Transcription Factors 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

130-138

Informations de copyright

Copyright © 2020 Elsevier Ltd. All rights reserved.

Auteurs

Charlotte Blessing (C)

Department of Physiological Chemistry, Biomedical Center (BMC), Faculty of Medicine, LMU Munich, 82152 Planegg-Martinsried, Germany; International Max Planck Research School for Molecular Life Sciences, Am Klopferspitz 18, 82152 Planegg-Martinsried, Germany.

Gunnar Knobloch (G)

Eisbach Bio GmbH, Am Klopferspitz 19, 82152, Planegg-Martinsried, Germany.

Andreas G Ladurner (AG)

Department of Physiological Chemistry, Biomedical Center (BMC), Faculty of Medicine, LMU Munich, 82152 Planegg-Martinsried, Germany; International Max Planck Research School for Molecular Life Sciences, Am Klopferspitz 18, 82152 Planegg-Martinsried, Germany; Eisbach Bio GmbH, Am Klopferspitz 19, 82152, Planegg-Martinsried, Germany. Electronic address: andreas.ladurner@bmc.med.lmu.de.

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Classifications MeSH