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Targets of histone H3 lysine 9 methyltransferases
Histone H3 lysine 9 di- and trimethylation are well-established marks of constitutively silenced heterochromatin domains found at repetitive DNA elements including pericentromeres, telomeres, and transposons. Loss of heterochromatin at these sites causes genomic instability in the form of aberrant D...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9768651/ https://www.ncbi.nlm.nih.gov/pubmed/36568972 http://dx.doi.org/10.3389/fcell.2022.1026406 |
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author | Levinsky, Aidan J. McEdwards, Gregor Sethna, Nasha Currie, Mark A. |
author_facet | Levinsky, Aidan J. McEdwards, Gregor Sethna, Nasha Currie, Mark A. |
author_sort | Levinsky, Aidan J. |
collection | PubMed |
description | Histone H3 lysine 9 di- and trimethylation are well-established marks of constitutively silenced heterochromatin domains found at repetitive DNA elements including pericentromeres, telomeres, and transposons. Loss of heterochromatin at these sites causes genomic instability in the form of aberrant DNA repair, chromosome segregation defects, replication stress, and transposition. H3K9 di- and trimethylation also regulate cell type-specific gene expression during development and form a barrier to cellular reprogramming. However, the role of H3K9 methyltransferases extends beyond histone methylation. There is a growing list of non-histone targets of H3K9 methyltransferases including transcription factors, steroid hormone receptors, histone modifying enzymes, and other chromatin regulatory proteins. Additionally, two classes of H3K9 methyltransferases modulate their own function through automethylation. Here we summarize the structure and function of mammalian H3K9 methyltransferases, their roles in genome regulation and constitutive heterochromatin, as well as the current repertoire of non-histone methylation targets including cases of automethylation. |
format | Online Article Text |
id | pubmed-9768651 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-97686512022-12-22 Targets of histone H3 lysine 9 methyltransferases Levinsky, Aidan J. McEdwards, Gregor Sethna, Nasha Currie, Mark A. Front Cell Dev Biol Cell and Developmental Biology Histone H3 lysine 9 di- and trimethylation are well-established marks of constitutively silenced heterochromatin domains found at repetitive DNA elements including pericentromeres, telomeres, and transposons. Loss of heterochromatin at these sites causes genomic instability in the form of aberrant DNA repair, chromosome segregation defects, replication stress, and transposition. H3K9 di- and trimethylation also regulate cell type-specific gene expression during development and form a barrier to cellular reprogramming. However, the role of H3K9 methyltransferases extends beyond histone methylation. There is a growing list of non-histone targets of H3K9 methyltransferases including transcription factors, steroid hormone receptors, histone modifying enzymes, and other chromatin regulatory proteins. Additionally, two classes of H3K9 methyltransferases modulate their own function through automethylation. Here we summarize the structure and function of mammalian H3K9 methyltransferases, their roles in genome regulation and constitutive heterochromatin, as well as the current repertoire of non-histone methylation targets including cases of automethylation. Frontiers Media S.A. 2022-12-06 /pmc/articles/PMC9768651/ /pubmed/36568972 http://dx.doi.org/10.3389/fcell.2022.1026406 Text en Copyright © 2022 Levinsky, McEdwards, Sethna and Currie. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Cell and Developmental Biology Levinsky, Aidan J. McEdwards, Gregor Sethna, Nasha Currie, Mark A. Targets of histone H3 lysine 9 methyltransferases |
title | Targets of histone H3 lysine 9 methyltransferases |
title_full | Targets of histone H3 lysine 9 methyltransferases |
title_fullStr | Targets of histone H3 lysine 9 methyltransferases |
title_full_unstemmed | Targets of histone H3 lysine 9 methyltransferases |
title_short | Targets of histone H3 lysine 9 methyltransferases |
title_sort | targets of histone h3 lysine 9 methyltransferases |
topic | Cell and Developmental Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9768651/ https://www.ncbi.nlm.nih.gov/pubmed/36568972 http://dx.doi.org/10.3389/fcell.2022.1026406 |
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