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[PRION(+)] States Are Associated with Specific Histone H3 Post-Translational Modification Changes
Prions are proteins able to take on alternative conformations and propagate them in a self-templating process. In Saccharomyces cerevisiae, prions enable heritable responses to environmental conditions through bet-hedging mechanisms. Hence, [PRION(+)] states may serve as an atypical form of epigenet...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9786042/ https://www.ncbi.nlm.nih.gov/pubmed/36558770 http://dx.doi.org/10.3390/pathogens11121436 |
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author | Cobos, Samantha N. Janani, Chaim Cruz, Gabriel Rana, Navin Son, Elizaveta Frederic, Rania Paredes Casado, Jailene Khan, Maliha Bennett, Seth A. Torrente, Mariana P. |
author_facet | Cobos, Samantha N. Janani, Chaim Cruz, Gabriel Rana, Navin Son, Elizaveta Frederic, Rania Paredes Casado, Jailene Khan, Maliha Bennett, Seth A. Torrente, Mariana P. |
author_sort | Cobos, Samantha N. |
collection | PubMed |
description | Prions are proteins able to take on alternative conformations and propagate them in a self-templating process. In Saccharomyces cerevisiae, prions enable heritable responses to environmental conditions through bet-hedging mechanisms. Hence, [PRION(+)] states may serve as an atypical form of epigenetic control, producing heritable phenotypic change via protein folding. However, the connections between prion states and the epigenome remain unknown. Do [PRION(+)] states link to canonical epigenetic channels, such as histone post-translational modifications? Here, we map out the histone H3 modification landscape in the context of the [SWI(+)] and [PIN(+)] prion states. [SWI(+)] is propagated by Swi1, a subunit of the SWI/SNF chromatin remodeling complex, while [PIN(+)] is propagated by Rnq1, a protein of unknown function. We find [SWI(+)] yeast display decreases in the levels of H3K36me2 and H3K56ac compared to [swi(−)] yeast. In contrast, decreases in H3K4me3, H3K36me2, H3K36me3 and H3K79me3 are connected to the [PIN(+)] state. Curing of the prion state by treatment with guanidine hydrochloride restored histone PTM to [prion(−)] state levels. We find histone PTMs in the [PRION(+)] state do not match those in loss-of-function models. Our findings shed light into the link between prion states and histone modifications, revealing novel insight into prion function in yeast. |
format | Online Article Text |
id | pubmed-9786042 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-97860422022-12-24 [PRION(+)] States Are Associated with Specific Histone H3 Post-Translational Modification Changes Cobos, Samantha N. Janani, Chaim Cruz, Gabriel Rana, Navin Son, Elizaveta Frederic, Rania Paredes Casado, Jailene Khan, Maliha Bennett, Seth A. Torrente, Mariana P. Pathogens Article Prions are proteins able to take on alternative conformations and propagate them in a self-templating process. In Saccharomyces cerevisiae, prions enable heritable responses to environmental conditions through bet-hedging mechanisms. Hence, [PRION(+)] states may serve as an atypical form of epigenetic control, producing heritable phenotypic change via protein folding. However, the connections between prion states and the epigenome remain unknown. Do [PRION(+)] states link to canonical epigenetic channels, such as histone post-translational modifications? Here, we map out the histone H3 modification landscape in the context of the [SWI(+)] and [PIN(+)] prion states. [SWI(+)] is propagated by Swi1, a subunit of the SWI/SNF chromatin remodeling complex, while [PIN(+)] is propagated by Rnq1, a protein of unknown function. We find [SWI(+)] yeast display decreases in the levels of H3K36me2 and H3K56ac compared to [swi(−)] yeast. In contrast, decreases in H3K4me3, H3K36me2, H3K36me3 and H3K79me3 are connected to the [PIN(+)] state. Curing of the prion state by treatment with guanidine hydrochloride restored histone PTM to [prion(−)] state levels. We find histone PTMs in the [PRION(+)] state do not match those in loss-of-function models. Our findings shed light into the link between prion states and histone modifications, revealing novel insight into prion function in yeast. MDPI 2022-11-29 /pmc/articles/PMC9786042/ /pubmed/36558770 http://dx.doi.org/10.3390/pathogens11121436 Text en © 2022 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 Cobos, Samantha N. Janani, Chaim Cruz, Gabriel Rana, Navin Son, Elizaveta Frederic, Rania Paredes Casado, Jailene Khan, Maliha Bennett, Seth A. Torrente, Mariana P. [PRION(+)] States Are Associated with Specific Histone H3 Post-Translational Modification Changes |
title | [PRION(+)] States Are Associated with Specific Histone H3 Post-Translational Modification Changes |
title_full | [PRION(+)] States Are Associated with Specific Histone H3 Post-Translational Modification Changes |
title_fullStr | [PRION(+)] States Are Associated with Specific Histone H3 Post-Translational Modification Changes |
title_full_unstemmed | [PRION(+)] States Are Associated with Specific Histone H3 Post-Translational Modification Changes |
title_short | [PRION(+)] States Are Associated with Specific Histone H3 Post-Translational Modification Changes |
title_sort | [prion(+)] states are associated with specific histone h3 post-translational modification changes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9786042/ https://www.ncbi.nlm.nih.gov/pubmed/36558770 http://dx.doi.org/10.3390/pathogens11121436 |
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