Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome
ATP-dependent chromatin remodelling proteins represent a diverse family of proteins that share ATPase domains that are adapted to regulate protein–DNA interactions. Here, we present structures of the Saccharomyces cerevisiae Chd1 protein engaged with nucleosomes in the presence of the transition sta...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6118821/ https://www.ncbi.nlm.nih.gov/pubmed/30079888 http://dx.doi.org/10.7554/eLife.35720 |
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author | Sundaramoorthy, Ramasubramanian Hughes, Amanda L El-Mkami, Hassane Norman, David G Ferreira, Helder Owen-Hughes, Tom |
author_facet | Sundaramoorthy, Ramasubramanian Hughes, Amanda L El-Mkami, Hassane Norman, David G Ferreira, Helder Owen-Hughes, Tom |
author_sort | Sundaramoorthy, Ramasubramanian |
collection | PubMed |
description | ATP-dependent chromatin remodelling proteins represent a diverse family of proteins that share ATPase domains that are adapted to regulate protein–DNA interactions. Here, we present structures of the Saccharomyces cerevisiae Chd1 protein engaged with nucleosomes in the presence of the transition state mimic ADP-beryllium fluoride. The path of DNA strands through the ATPase domains indicates the presence of contacts conserved with single strand translocases and additional contacts with both strands that are unique to Snf2 related proteins. The structure provides connectivity between rearrangement of ATPase lobes to a closed, nucleotide bound state and the sensing of linker DNA. Two turns of linker DNA are prised off the surface of the histone octamer as a result of Chd1 binding, and both the histone H3 tail and ubiquitin conjugated to lysine 120 are re-orientated towards the unravelled DNA. This indicates how changes to nucleosome structure can alter the way in which histone epitopes are presented. |
format | Online Article Text |
id | pubmed-6118821 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-61188212018-09-05 Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome Sundaramoorthy, Ramasubramanian Hughes, Amanda L El-Mkami, Hassane Norman, David G Ferreira, Helder Owen-Hughes, Tom eLife Chromosomes and Gene Expression ATP-dependent chromatin remodelling proteins represent a diverse family of proteins that share ATPase domains that are adapted to regulate protein–DNA interactions. Here, we present structures of the Saccharomyces cerevisiae Chd1 protein engaged with nucleosomes in the presence of the transition state mimic ADP-beryllium fluoride. The path of DNA strands through the ATPase domains indicates the presence of contacts conserved with single strand translocases and additional contacts with both strands that are unique to Snf2 related proteins. The structure provides connectivity between rearrangement of ATPase lobes to a closed, nucleotide bound state and the sensing of linker DNA. Two turns of linker DNA are prised off the surface of the histone octamer as a result of Chd1 binding, and both the histone H3 tail and ubiquitin conjugated to lysine 120 are re-orientated towards the unravelled DNA. This indicates how changes to nucleosome structure can alter the way in which histone epitopes are presented. eLife Sciences Publications, Ltd 2018-08-06 /pmc/articles/PMC6118821/ /pubmed/30079888 http://dx.doi.org/10.7554/eLife.35720 Text en © 2018, Sundaramoorthy et al http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Chromosomes and Gene Expression Sundaramoorthy, Ramasubramanian Hughes, Amanda L El-Mkami, Hassane Norman, David G Ferreira, Helder Owen-Hughes, Tom Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome |
title | Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome |
title_full | Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome |
title_fullStr | Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome |
title_full_unstemmed | Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome |
title_short | Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome |
title_sort | structure of the chromatin remodelling enzyme chd1 bound to a ubiquitinylated nucleosome |
topic | Chromosomes and Gene Expression |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6118821/ https://www.ncbi.nlm.nih.gov/pubmed/30079888 http://dx.doi.org/10.7554/eLife.35720 |
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