Phase separation by the polyhomeotic sterile alpha motif compartmentalizes Polycomb Group proteins and enhances their activity
The conserved SAM motif of Polycomb Repressive Complex 1 subunit Ph has been shown to play an important role in chromatin organization. Here, the authors study the effect of Ph SAM on chromatin in vitro, showing that it induces the formation of concentrated, phase-separated condensates, which enhanc...
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2020-11-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-020-19435-z |
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doaj-f93773e13b25400184a9e8d15645342f2021-05-11T08:29:55ZengNature Publishing GroupNature Communications2041-17232020-11-0111111910.1038/s41467-020-19435-zPhase separation by the polyhomeotic sterile alpha motif compartmentalizes Polycomb Group proteins and enhances their activityElias Seif0Jin Joo Kang1Charles Sasseville2Olga Senkovich3Alexander Kaltashov4Elodie L. Boulier5Ibani Kapur6Chongwoo A. Kim7Nicole J. Francis8Institut de recherches cliniques de MontréalInstitut de recherches cliniques de MontréalInstitut de recherches cliniques de MontréalDepartment of Biochemistry and Molecular Genetics, Midwestern UniversityInstitut de recherches cliniques de MontréalInstitut de recherches cliniques de MontréalInstitut de recherches cliniques de MontréalDepartment of Biochemistry and Molecular Genetics, Midwestern UniversityInstitut de recherches cliniques de MontréalThe conserved SAM motif of Polycomb Repressive Complex 1 subunit Ph has been shown to play an important role in chromatin organization. Here, the authors study the effect of Ph SAM on chromatin in vitro, showing that it induces the formation of concentrated, phase-separated condensates, which enhance the ubiquitin ligase activity of PRC1.https://doi.org/10.1038/s41467-020-19435-z |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Elias Seif Jin Joo Kang Charles Sasseville Olga Senkovich Alexander Kaltashov Elodie L. Boulier Ibani Kapur Chongwoo A. Kim Nicole J. Francis |
spellingShingle |
Elias Seif Jin Joo Kang Charles Sasseville Olga Senkovich Alexander Kaltashov Elodie L. Boulier Ibani Kapur Chongwoo A. Kim Nicole J. Francis Phase separation by the polyhomeotic sterile alpha motif compartmentalizes Polycomb Group proteins and enhances their activity Nature Communications |
author_facet |
Elias Seif Jin Joo Kang Charles Sasseville Olga Senkovich Alexander Kaltashov Elodie L. Boulier Ibani Kapur Chongwoo A. Kim Nicole J. Francis |
author_sort |
Elias Seif |
title |
Phase separation by the polyhomeotic sterile alpha motif compartmentalizes Polycomb Group proteins and enhances their activity |
title_short |
Phase separation by the polyhomeotic sterile alpha motif compartmentalizes Polycomb Group proteins and enhances their activity |
title_full |
Phase separation by the polyhomeotic sterile alpha motif compartmentalizes Polycomb Group proteins and enhances their activity |
title_fullStr |
Phase separation by the polyhomeotic sterile alpha motif compartmentalizes Polycomb Group proteins and enhances their activity |
title_full_unstemmed |
Phase separation by the polyhomeotic sterile alpha motif compartmentalizes Polycomb Group proteins and enhances their activity |
title_sort |
phase separation by the polyhomeotic sterile alpha motif compartmentalizes polycomb group proteins and enhances their activity |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2020-11-01 |
description |
The conserved SAM motif of Polycomb Repressive Complex 1 subunit Ph has been shown to play an important role in chromatin organization. Here, the authors study the effect of Ph SAM on chromatin in vitro, showing that it induces the formation of concentrated, phase-separated condensates, which enhance the ubiquitin ligase activity of PRC1. |
url |
https://doi.org/10.1038/s41467-020-19435-z |
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