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Chromatin remodelling comes into focus

ATP-dependent chromatin remodelling enzymes are molecular machines that act to reconfigure the structure of nucleosomes. Until recently, little was known about the structure of these enzymes. Recent progress has revealed that their interaction with chromatin is dominated by ATPase domains that conta...

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Detalles Bibliográficos
Autores principales: Sundaramoorthy, Ramasubramian, Owen-Hughes, Tom
Formato: Online Artículo Texto
Lenguaje:English
Publicado: F1000 Research Limited 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7445562/
https://www.ncbi.nlm.nih.gov/pubmed/32864100
http://dx.doi.org/10.12688/f1000research.21933.1
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author Sundaramoorthy, Ramasubramian
Owen-Hughes, Tom
author_facet Sundaramoorthy, Ramasubramian
Owen-Hughes, Tom
author_sort Sundaramoorthy, Ramasubramian
collection PubMed
description ATP-dependent chromatin remodelling enzymes are molecular machines that act to reconfigure the structure of nucleosomes. Until recently, little was known about the structure of these enzymes. Recent progress has revealed that their interaction with chromatin is dominated by ATPase domains that contact DNA at favoured locations on the nucleosome surface. Contacts with histones are limited but play important roles in modulating activity. The ATPase domains do not act in isolation but are flanked by diverse accessory domains and subunits. New structures indicate how these subunits are arranged in multi-subunit complexes providing a framework from which to understand how a common motor is applied to distinct functions.
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spelling pubmed-74455622020-08-27 Chromatin remodelling comes into focus Sundaramoorthy, Ramasubramian Owen-Hughes, Tom F1000Res Review ATP-dependent chromatin remodelling enzymes are molecular machines that act to reconfigure the structure of nucleosomes. Until recently, little was known about the structure of these enzymes. Recent progress has revealed that their interaction with chromatin is dominated by ATPase domains that contact DNA at favoured locations on the nucleosome surface. Contacts with histones are limited but play important roles in modulating activity. The ATPase domains do not act in isolation but are flanked by diverse accessory domains and subunits. New structures indicate how these subunits are arranged in multi-subunit complexes providing a framework from which to understand how a common motor is applied to distinct functions. F1000 Research Limited 2020-08-20 /pmc/articles/PMC7445562/ /pubmed/32864100 http://dx.doi.org/10.12688/f1000research.21933.1 Text en Copyright: © 2020 Sundaramoorthy R and Owen-Hughes T http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Sundaramoorthy, Ramasubramian
Owen-Hughes, Tom
Chromatin remodelling comes into focus
title Chromatin remodelling comes into focus
title_full Chromatin remodelling comes into focus
title_fullStr Chromatin remodelling comes into focus
title_full_unstemmed Chromatin remodelling comes into focus
title_short Chromatin remodelling comes into focus
title_sort chromatin remodelling comes into focus
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7445562/
https://www.ncbi.nlm.nih.gov/pubmed/32864100
http://dx.doi.org/10.12688/f1000research.21933.1
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