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Structural Paradigms in the Recognition of the Nucleosome Core Particle by Histone Lysine Methyltransferases
Post-translational modifications (PTMs) of histone proteins play essential functions in shaping chromatin environment. Alone or in combination, these PTMs create templates recognized by dedicated proteins or change the chemistry of chromatin, enabling a myriad of nuclear processes to occur. Referred...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7412744/ https://www.ncbi.nlm.nih.gov/pubmed/32850785 http://dx.doi.org/10.3389/fcell.2020.00600 |
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author | Janna, Ashley Davarinejad, Hossein Joshi, Monika Couture, Jean-Francois |
author_facet | Janna, Ashley Davarinejad, Hossein Joshi, Monika Couture, Jean-Francois |
author_sort | Janna, Ashley |
collection | PubMed |
description | Post-translational modifications (PTMs) of histone proteins play essential functions in shaping chromatin environment. Alone or in combination, these PTMs create templates recognized by dedicated proteins or change the chemistry of chromatin, enabling a myriad of nuclear processes to occur. Referred to as cross-talk, the positive or negative impact of a PTM on another PTM has rapidly emerged as a mechanism controlling nuclear transactions. One of those includes the stimulatory functions of histone H2B ubiquitylation on the methylation of histone H3 on K79 and K4 by Dot1L and COMPASS, respectively. While these findings were established early on, the structural determinants underlying the positive impact of H2B ubiquitylation on H3K79 and H3K4 methylation were resolved only recently. We will also review the molecular features controlling these cross-talks and the impact of H3K27 tri-methylation on EZH2 activity when embedded in the PRC2 complex. |
format | Online Article Text |
id | pubmed-7412744 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-74127442020-08-25 Structural Paradigms in the Recognition of the Nucleosome Core Particle by Histone Lysine Methyltransferases Janna, Ashley Davarinejad, Hossein Joshi, Monika Couture, Jean-Francois Front Cell Dev Biol Cell and Developmental Biology Post-translational modifications (PTMs) of histone proteins play essential functions in shaping chromatin environment. Alone or in combination, these PTMs create templates recognized by dedicated proteins or change the chemistry of chromatin, enabling a myriad of nuclear processes to occur. Referred to as cross-talk, the positive or negative impact of a PTM on another PTM has rapidly emerged as a mechanism controlling nuclear transactions. One of those includes the stimulatory functions of histone H2B ubiquitylation on the methylation of histone H3 on K79 and K4 by Dot1L and COMPASS, respectively. While these findings were established early on, the structural determinants underlying the positive impact of H2B ubiquitylation on H3K79 and H3K4 methylation were resolved only recently. We will also review the molecular features controlling these cross-talks and the impact of H3K27 tri-methylation on EZH2 activity when embedded in the PRC2 complex. Frontiers Media S.A. 2020-07-31 /pmc/articles/PMC7412744/ /pubmed/32850785 http://dx.doi.org/10.3389/fcell.2020.00600 Text en Copyright © 2020 Janna, Davarinejad, Joshi and Couture. http://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 Janna, Ashley Davarinejad, Hossein Joshi, Monika Couture, Jean-Francois Structural Paradigms in the Recognition of the Nucleosome Core Particle by Histone Lysine Methyltransferases |
title | Structural Paradigms in the Recognition of the Nucleosome Core Particle by Histone Lysine Methyltransferases |
title_full | Structural Paradigms in the Recognition of the Nucleosome Core Particle by Histone Lysine Methyltransferases |
title_fullStr | Structural Paradigms in the Recognition of the Nucleosome Core Particle by Histone Lysine Methyltransferases |
title_full_unstemmed | Structural Paradigms in the Recognition of the Nucleosome Core Particle by Histone Lysine Methyltransferases |
title_short | Structural Paradigms in the Recognition of the Nucleosome Core Particle by Histone Lysine Methyltransferases |
title_sort | structural paradigms in the recognition of the nucleosome core particle by histone lysine methyltransferases |
topic | Cell and Developmental Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7412744/ https://www.ncbi.nlm.nih.gov/pubmed/32850785 http://dx.doi.org/10.3389/fcell.2020.00600 |
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