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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
F1000 Research Limited
2020
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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. |
format | Online Article Text |
id | pubmed-7445562 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | F1000 Research Limited |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT sundaramoorthyramasubramian chromatinremodellingcomesintofocus AT owenhughestom chromatinremodellingcomesintofocus |