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Histone variants at a glance
Eukaryotic nucleosomes organize chromatin by wrapping 147 bp of DNA around a histone core particle comprising two molecules each of histone H2A, H2B, H3 and H4. The DNA entering and exiting the particle may be bound by the linker histone H1. Whereas deposition of bulk histones is confined to S-phase...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Company of Biologists Ltd
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8015243/ https://www.ncbi.nlm.nih.gov/pubmed/33771851 http://dx.doi.org/10.1242/jcs.244749 |
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author | Talbert, Paul B. Henikoff, Steven |
author_facet | Talbert, Paul B. Henikoff, Steven |
author_sort | Talbert, Paul B. |
collection | PubMed |
description | Eukaryotic nucleosomes organize chromatin by wrapping 147 bp of DNA around a histone core particle comprising two molecules each of histone H2A, H2B, H3 and H4. The DNA entering and exiting the particle may be bound by the linker histone H1. Whereas deposition of bulk histones is confined to S-phase, paralogs of the common histones, known as histone variants, are available to carry out functions throughout the cell cycle and accumulate in post-mitotic cells. Histone variants confer different structural properties on nucleosomes by wrapping more or less DNA or by altering nucleosome stability. They carry out specialized functions in DNA repair, chromosome segregation and regulation of transcription initiation, or perform tissue-specific roles. In this Cell Science at a Glance article and the accompanying poster, we briefly examine new insights into histone origins and discuss variants from each of the histone families, focusing on how structural differences may alter their functions. |
format | Online Article Text |
id | pubmed-8015243 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | The Company of Biologists Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-80152432021-04-07 Histone variants at a glance Talbert, Paul B. Henikoff, Steven J Cell Sci Cell Science at A Glance Eukaryotic nucleosomes organize chromatin by wrapping 147 bp of DNA around a histone core particle comprising two molecules each of histone H2A, H2B, H3 and H4. The DNA entering and exiting the particle may be bound by the linker histone H1. Whereas deposition of bulk histones is confined to S-phase, paralogs of the common histones, known as histone variants, are available to carry out functions throughout the cell cycle and accumulate in post-mitotic cells. Histone variants confer different structural properties on nucleosomes by wrapping more or less DNA or by altering nucleosome stability. They carry out specialized functions in DNA repair, chromosome segregation and regulation of transcription initiation, or perform tissue-specific roles. In this Cell Science at a Glance article and the accompanying poster, we briefly examine new insights into histone origins and discuss variants from each of the histone families, focusing on how structural differences may alter their functions. The Company of Biologists Ltd 2021-03-26 /pmc/articles/PMC8015243/ /pubmed/33771851 http://dx.doi.org/10.1242/jcs.244749 Text en © 2021. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/4.0This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed. |
spellingShingle | Cell Science at A Glance Talbert, Paul B. Henikoff, Steven Histone variants at a glance |
title | Histone variants at a glance |
title_full | Histone variants at a glance |
title_fullStr | Histone variants at a glance |
title_full_unstemmed | Histone variants at a glance |
title_short | Histone variants at a glance |
title_sort | histone variants at a glance |
topic | Cell Science at A Glance |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8015243/ https://www.ncbi.nlm.nih.gov/pubmed/33771851 http://dx.doi.org/10.1242/jcs.244749 |
work_keys_str_mv | AT talbertpaulb histonevariantsataglance AT henikoffsteven histonevariantsataglance |