Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Talbert, Paul B., Henikoff, Steven
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Company of Biologists Ltd 2021
Materias:
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
_version_ 1783673642100457472
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