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Structural comparisons reveal diverse binding modes between nucleosome assembly proteins and histones
Nucleosome assembly proteins (NAPs) are histone chaperones that play a central role in facilitating chromatin assembly/disassembly which is of fundamental importance for DNA replication, gene expression regulation, and progression through the cell cycle. In vitro, NAPs bind to the core histones H2A,...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9128123/ https://www.ncbi.nlm.nih.gov/pubmed/35606827 http://dx.doi.org/10.1186/s13072-022-00452-9 |
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author | Gill, Jasmita Kumar, Anuj Sharma, Amit |
author_facet | Gill, Jasmita Kumar, Anuj Sharma, Amit |
author_sort | Gill, Jasmita |
collection | PubMed |
description | Nucleosome assembly proteins (NAPs) are histone chaperones that play a central role in facilitating chromatin assembly/disassembly which is of fundamental importance for DNA replication, gene expression regulation, and progression through the cell cycle. In vitro, NAPs bind to the core histones H2A, H2B, H3, H4 and possibly to H1. The NAP family contains well-characterized and dedicated histone chaperone domain called the NAP domain, and the NAP–histone interactions are key to deciphering chromatin assembly. Our comparative structural analysis of the three three-dimensional structures of NAPs from S. cerevisiae, C. elegans, and A. thaliana in complex with the histone H2A–H2B dimer reveals distinct and diverse binding of NAPs with histones. The three NAPs employ distinct surfaces for recognizing the H2A–H2B dimer and vice versa. Though histones are highly conserved across species they display diverse footprints on NAPs. Our analysis indicates that understanding of NAPs and their interaction with histone H2A–H2B remains sparse. Due to divergent knowledge from the current structures analyzed here, investigations into the dynamic nature of NAP–histone interactions are warranted. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13072-022-00452-9. |
format | Online Article Text |
id | pubmed-9128123 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-91281232022-05-25 Structural comparisons reveal diverse binding modes between nucleosome assembly proteins and histones Gill, Jasmita Kumar, Anuj Sharma, Amit Epigenetics Chromatin Review Nucleosome assembly proteins (NAPs) are histone chaperones that play a central role in facilitating chromatin assembly/disassembly which is of fundamental importance for DNA replication, gene expression regulation, and progression through the cell cycle. In vitro, NAPs bind to the core histones H2A, H2B, H3, H4 and possibly to H1. The NAP family contains well-characterized and dedicated histone chaperone domain called the NAP domain, and the NAP–histone interactions are key to deciphering chromatin assembly. Our comparative structural analysis of the three three-dimensional structures of NAPs from S. cerevisiae, C. elegans, and A. thaliana in complex with the histone H2A–H2B dimer reveals distinct and diverse binding of NAPs with histones. The three NAPs employ distinct surfaces for recognizing the H2A–H2B dimer and vice versa. Though histones are highly conserved across species they display diverse footprints on NAPs. Our analysis indicates that understanding of NAPs and their interaction with histone H2A–H2B remains sparse. Due to divergent knowledge from the current structures analyzed here, investigations into the dynamic nature of NAP–histone interactions are warranted. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13072-022-00452-9. BioMed Central 2022-05-24 /pmc/articles/PMC9128123/ /pubmed/35606827 http://dx.doi.org/10.1186/s13072-022-00452-9 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Review Gill, Jasmita Kumar, Anuj Sharma, Amit Structural comparisons reveal diverse binding modes between nucleosome assembly proteins and histones |
title | Structural comparisons reveal diverse binding modes between nucleosome assembly proteins and histones |
title_full | Structural comparisons reveal diverse binding modes between nucleosome assembly proteins and histones |
title_fullStr | Structural comparisons reveal diverse binding modes between nucleosome assembly proteins and histones |
title_full_unstemmed | Structural comparisons reveal diverse binding modes between nucleosome assembly proteins and histones |
title_short | Structural comparisons reveal diverse binding modes between nucleosome assembly proteins and histones |
title_sort | structural comparisons reveal diverse binding modes between nucleosome assembly proteins and histones |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9128123/ https://www.ncbi.nlm.nih.gov/pubmed/35606827 http://dx.doi.org/10.1186/s13072-022-00452-9 |
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