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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,...

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Autores principales: Gill, Jasmita, Kumar, Anuj, Sharma, Amit
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2022
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.
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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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