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Phase separation of Dri1 contributes to heterochromatin formation in Schizosaccharomyces pombe
The RNA binding protein Dri1 facilitates heterochromatin assembly via the RNAi pathway and histone deacetylases (HDAC). Dri1 contains an intrinsically disordered region (IDR) and three zinc fingers at its C-terminus, which are important for its role in heterochromatin silencing. Both IDR and zinc fi...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Caltech Library
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9019594/ https://www.ncbi.nlm.nih.gov/pubmed/35622527 http://dx.doi.org/10.17912/micropub.biology.000559 |
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author | Ban, Hyoju Sun, Wenqi Chen, Yong Li, Fei |
author_facet | Ban, Hyoju Sun, Wenqi Chen, Yong Li, Fei |
author_sort | Ban, Hyoju |
collection | PubMed |
description | The RNA binding protein Dri1 facilitates heterochromatin assembly via the RNAi pathway and histone deacetylases (HDAC). Dri1 contains an intrinsically disordered region (IDR) and three zinc fingers at its C-terminus, which are important for its role in heterochromatin silencing. Both IDR and zinc fingers have been implicated in mediating liquid-liquid phase separation (LLPS). In this study, we investigated the phase separation properties of Dri1. We observed that Dri1 undergoes phase separation in vitro . Dri1 also exhibits liquid-like behavior in vivo . Combined with our previous findings, our data support a model in which the phase-separated condensates formed by Dri1 may help recruit RNAi components and HDAC to mediate heterochromatin assembly. |
format | Online Article Text |
id | pubmed-9019594 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Caltech Library |
record_format | MEDLINE/PubMed |
spelling | pubmed-90195942022-04-21 Phase separation of Dri1 contributes to heterochromatin formation in Schizosaccharomyces pombe Ban, Hyoju Sun, Wenqi Chen, Yong Li, Fei MicroPubl Biol New Finding The RNA binding protein Dri1 facilitates heterochromatin assembly via the RNAi pathway and histone deacetylases (HDAC). Dri1 contains an intrinsically disordered region (IDR) and three zinc fingers at its C-terminus, which are important for its role in heterochromatin silencing. Both IDR and zinc fingers have been implicated in mediating liquid-liquid phase separation (LLPS). In this study, we investigated the phase separation properties of Dri1. We observed that Dri1 undergoes phase separation in vitro . Dri1 also exhibits liquid-like behavior in vivo . Combined with our previous findings, our data support a model in which the phase-separated condensates formed by Dri1 may help recruit RNAi components and HDAC to mediate heterochromatin assembly. Caltech Library 2022-04-19 /pmc/articles/PMC9019594/ /pubmed/35622527 http://dx.doi.org/10.17912/micropub.biology.000559 Text en Copyright: © 2022 by the authors https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | New Finding Ban, Hyoju Sun, Wenqi Chen, Yong Li, Fei Phase separation of Dri1 contributes to heterochromatin formation in Schizosaccharomyces pombe |
title |
Phase separation of Dri1 contributes to heterochromatin formation in
Schizosaccharomyces pombe
|
title_full |
Phase separation of Dri1 contributes to heterochromatin formation in
Schizosaccharomyces pombe
|
title_fullStr |
Phase separation of Dri1 contributes to heterochromatin formation in
Schizosaccharomyces pombe
|
title_full_unstemmed |
Phase separation of Dri1 contributes to heterochromatin formation in
Schizosaccharomyces pombe
|
title_short |
Phase separation of Dri1 contributes to heterochromatin formation in
Schizosaccharomyces pombe
|
title_sort | phase separation of dri1 contributes to heterochromatin formation in
schizosaccharomyces pombe |
topic | New Finding |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9019594/ https://www.ncbi.nlm.nih.gov/pubmed/35622527 http://dx.doi.org/10.17912/micropub.biology.000559 |
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