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The Histone Chaperone Network Is Highly Conserved in Physarum polycephalum
The nucleosome is composed of histones and DNA. Prior to their deposition on chromatin, histones are shielded by specialized and diverse proteins known as histone chaperones. They escort histones during their entire cellular life and ensure their proper incorporation in chromatin. Physarum polycepha...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9864664/ https://www.ncbi.nlm.nih.gov/pubmed/36674565 http://dx.doi.org/10.3390/ijms24021051 |
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author | Poulet, Axel Rousselot, Ellyn Téletchéa, Stéphane Noirot, Céline Jacob, Yannick van Wolfswinkel, Josien Thiriet, Christophe Duc, Céline |
author_facet | Poulet, Axel Rousselot, Ellyn Téletchéa, Stéphane Noirot, Céline Jacob, Yannick van Wolfswinkel, Josien Thiriet, Christophe Duc, Céline |
author_sort | Poulet, Axel |
collection | PubMed |
description | The nucleosome is composed of histones and DNA. Prior to their deposition on chromatin, histones are shielded by specialized and diverse proteins known as histone chaperones. They escort histones during their entire cellular life and ensure their proper incorporation in chromatin. Physarum polycephalum is a Mycetozoan, a clade located at the crown of the eukaryotic tree. We previously found that histones, which are highly conserved between plants and animals, are also highly conserved in Physarum. However, histone chaperones differ significantly between animal and plant kingdoms, and this thus probed us to further study the conservation of histone chaperones in Physarum and their evolution relative to animal and plants. Most of the known histone chaperones and their functional domains are conserved as well as key residues required for histone and chaperone interactions. Physarum is divergent from yeast, plants and animals, but PpHIRA, PpCABIN1 and PpSPT6 are similar in structure to plant orthologues. PpFACT is closely related to the yeast complex, and the Physarum genome encodes the animal-specific APFL chaperone. Furthermore, we performed RNA sequencing to monitor chaperone expression during the cell cycle and uncovered two distinct patterns during S-phase. In summary, our study demonstrates the conserved role of histone chaperones in handling histones in an early-branching eukaryote. |
format | Online Article Text |
id | pubmed-9864664 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-98646642023-01-22 The Histone Chaperone Network Is Highly Conserved in Physarum polycephalum Poulet, Axel Rousselot, Ellyn Téletchéa, Stéphane Noirot, Céline Jacob, Yannick van Wolfswinkel, Josien Thiriet, Christophe Duc, Céline Int J Mol Sci Article The nucleosome is composed of histones and DNA. Prior to their deposition on chromatin, histones are shielded by specialized and diverse proteins known as histone chaperones. They escort histones during their entire cellular life and ensure their proper incorporation in chromatin. Physarum polycephalum is a Mycetozoan, a clade located at the crown of the eukaryotic tree. We previously found that histones, which are highly conserved between plants and animals, are also highly conserved in Physarum. However, histone chaperones differ significantly between animal and plant kingdoms, and this thus probed us to further study the conservation of histone chaperones in Physarum and their evolution relative to animal and plants. Most of the known histone chaperones and their functional domains are conserved as well as key residues required for histone and chaperone interactions. Physarum is divergent from yeast, plants and animals, but PpHIRA, PpCABIN1 and PpSPT6 are similar in structure to plant orthologues. PpFACT is closely related to the yeast complex, and the Physarum genome encodes the animal-specific APFL chaperone. Furthermore, we performed RNA sequencing to monitor chaperone expression during the cell cycle and uncovered two distinct patterns during S-phase. In summary, our study demonstrates the conserved role of histone chaperones in handling histones in an early-branching eukaryote. MDPI 2023-01-05 /pmc/articles/PMC9864664/ /pubmed/36674565 http://dx.doi.org/10.3390/ijms24021051 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Poulet, Axel Rousselot, Ellyn Téletchéa, Stéphane Noirot, Céline Jacob, Yannick van Wolfswinkel, Josien Thiriet, Christophe Duc, Céline The Histone Chaperone Network Is Highly Conserved in Physarum polycephalum |
title | The Histone Chaperone Network Is Highly Conserved in Physarum polycephalum |
title_full | The Histone Chaperone Network Is Highly Conserved in Physarum polycephalum |
title_fullStr | The Histone Chaperone Network Is Highly Conserved in Physarum polycephalum |
title_full_unstemmed | The Histone Chaperone Network Is Highly Conserved in Physarum polycephalum |
title_short | The Histone Chaperone Network Is Highly Conserved in Physarum polycephalum |
title_sort | histone chaperone network is highly conserved in physarum polycephalum |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9864664/ https://www.ncbi.nlm.nih.gov/pubmed/36674565 http://dx.doi.org/10.3390/ijms24021051 |
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