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Drosophila insulator proteins exhibit in vivo liquid–liquid phase separation properties
Mounting evidence implicates liquid–liquid phase separation (LLPS), the condensation of biomolecules into liquid-like droplets in the formation and dissolution of membraneless intracellular organelles (MLOs). Cells use MLOs or condensates for various biological processes, including emergency signali...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Life Science Alliance LLC
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9297610/ https://www.ncbi.nlm.nih.gov/pubmed/35853678 http://dx.doi.org/10.26508/lsa.202201536 |
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author | Amankwaa, Bright Schoborg, Todd Labrador, Mariano |
author_facet | Amankwaa, Bright Schoborg, Todd Labrador, Mariano |
author_sort | Amankwaa, Bright |
collection | PubMed |
description | Mounting evidence implicates liquid–liquid phase separation (LLPS), the condensation of biomolecules into liquid-like droplets in the formation and dissolution of membraneless intracellular organelles (MLOs). Cells use MLOs or condensates for various biological processes, including emergency signaling and spatiotemporal control over steady-state biochemical reactions and heterochromatin formation. Insulator proteins are architectural elements involved in establishing independent domains of transcriptional activity within eukaryotic genomes. In Drosophila, insulator proteins form nuclear foci known as insulator bodies in response to osmotic stress. However, the mechanism through which insulator proteins assemble into bodies is yet to be investigated. Here, we identify signatures of LLPS by insulator bodies, including high disorder tendency in insulator proteins, scaffold–client–dependent assembly, extensive fusion behavior, sphericity, and sensitivity to 1,6-hexanediol. We also show that the cohesin subunit Rad21 is a component of insulator bodies, adding to the known insulator protein constituents and γH2Av. Our data suggest a concerted role of cohesin and insulator proteins in insulator body formation and under physiological conditions. We propose a mechanism whereby these architectural proteins modulate 3D genome organization through LLPS. |
format | Online Article Text |
id | pubmed-9297610 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Life Science Alliance LLC |
record_format | MEDLINE/PubMed |
spelling | pubmed-92976102022-08-04 Drosophila insulator proteins exhibit in vivo liquid–liquid phase separation properties Amankwaa, Bright Schoborg, Todd Labrador, Mariano Life Sci Alliance Research Articles Mounting evidence implicates liquid–liquid phase separation (LLPS), the condensation of biomolecules into liquid-like droplets in the formation and dissolution of membraneless intracellular organelles (MLOs). Cells use MLOs or condensates for various biological processes, including emergency signaling and spatiotemporal control over steady-state biochemical reactions and heterochromatin formation. Insulator proteins are architectural elements involved in establishing independent domains of transcriptional activity within eukaryotic genomes. In Drosophila, insulator proteins form nuclear foci known as insulator bodies in response to osmotic stress. However, the mechanism through which insulator proteins assemble into bodies is yet to be investigated. Here, we identify signatures of LLPS by insulator bodies, including high disorder tendency in insulator proteins, scaffold–client–dependent assembly, extensive fusion behavior, sphericity, and sensitivity to 1,6-hexanediol. We also show that the cohesin subunit Rad21 is a component of insulator bodies, adding to the known insulator protein constituents and γH2Av. Our data suggest a concerted role of cohesin and insulator proteins in insulator body formation and under physiological conditions. We propose a mechanism whereby these architectural proteins modulate 3D genome organization through LLPS. Life Science Alliance LLC 2022-07-19 /pmc/articles/PMC9297610/ /pubmed/35853678 http://dx.doi.org/10.26508/lsa.202201536 Text en © 2022 Amankwaa et al. https://creativecommons.org/licenses/by/4.0/This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Research Articles Amankwaa, Bright Schoborg, Todd Labrador, Mariano Drosophila insulator proteins exhibit in vivo liquid–liquid phase separation properties |
title | Drosophila insulator proteins exhibit in vivo liquid–liquid phase separation properties |
title_full | Drosophila insulator proteins exhibit in vivo liquid–liquid phase separation properties |
title_fullStr | Drosophila insulator proteins exhibit in vivo liquid–liquid phase separation properties |
title_full_unstemmed | Drosophila insulator proteins exhibit in vivo liquid–liquid phase separation properties |
title_short | Drosophila insulator proteins exhibit in vivo liquid–liquid phase separation properties |
title_sort | drosophila insulator proteins exhibit in vivo liquid–liquid phase separation properties |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9297610/ https://www.ncbi.nlm.nih.gov/pubmed/35853678 http://dx.doi.org/10.26508/lsa.202201536 |
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