Mouse heterochromatin adopts digital compaction states without showing hallmarks of HP1-driven liquid-liquid phase separation

Research output: Contribution to journal › Article › peer-review

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Mouse heterochromatin adopts digital compaction states without showing hallmarks of HP1-driven liquid-liquid phase separation. / Erdel, Fabian; Rademacher, Anne; Vlijm, Rifka; Tünnermann, Jana; Frank, Lukas; Weinmann, Robin; Schweigert, Elisabeth; Yserentant, Klaus; Hummert, Johan; Bauer, Caroline; Schumacher, Sabrina; Al Alwash, Ahmad; Normand, Christophe; Herten, Dirk-peter; Engelhardt, Johann; Rippe, Karsten.

In: Molecular Cell, Vol. 78, No. 2, 16.04.2020, p. 236-249.e7.

Research output: Contribution to journal › Article › peer-review

Harvard

Erdel, F, Rademacher, A, Vlijm, R, Tünnermann, J, Frank, L, Weinmann, R, Schweigert, E, Yserentant, K, Hummert, J, Bauer, C, Schumacher, S, Al Alwash, A, Normand, C, Herten, D, Engelhardt, J & Rippe, K 2020, 'Mouse heterochromatin adopts digital compaction states without showing hallmarks of HP1-driven liquid-liquid phase separation', Molecular Cell, vol. 78, no. 2, pp. 236-249.e7. https://doi.org/10.1016/j.molcel.2020.02.005

APA

Erdel, F., Rademacher, A., Vlijm, R., Tünnermann, J., Frank, L., Weinmann, R., Schweigert, E., Yserentant, K., Hummert, J., Bauer, C., Schumacher, S., Al Alwash, A., Normand, C., Herten, D., Engelhardt, J., & Rippe, K. (2020). Mouse heterochromatin adopts digital compaction states without showing hallmarks of HP1-driven liquid-liquid phase separation. Molecular Cell, 78(2), 236-249.e7. https://doi.org/10.1016/j.molcel.2020.02.005

Vancouver

Erdel F, Rademacher A, Vlijm R, Tünnermann J, Frank L, Weinmann R et al. Mouse heterochromatin adopts digital compaction states without showing hallmarks of HP1-driven liquid-liquid phase separation. Molecular Cell. 2020 Apr 16;78(2):236-249.e7. https://doi.org/10.1016/j.molcel.2020.02.005

Author

Erdel, Fabian ; Rademacher, Anne ; Vlijm, Rifka ; Tünnermann, Jana ; Frank, Lukas ; Weinmann, Robin ; Schweigert, Elisabeth ; Yserentant, Klaus ; Hummert, Johan ; Bauer, Caroline ; Schumacher, Sabrina ; Al Alwash, Ahmad ; Normand, Christophe ; Herten, Dirk-peter ; Engelhardt, Johann ; Rippe, Karsten. / Mouse heterochromatin adopts digital compaction states without showing hallmarks of HP1-driven liquid-liquid phase separation. In: Molecular Cell. 2020 ; Vol. 78, No. 2. pp. 236-249.e7.

Bibtex

@article{b7f806b45a124e3a855c04b6d0dce981,
title = "Mouse heterochromatin adopts digital compaction states without showing hallmarks of HP1-driven liquid-liquid phase separation",
abstract = "The formation of silenced and condensed heterochromatin foci involves enrichment of heterochromatin protein 1 (HP1). HP1 can bridge chromatin segments and form liquid droplets, but the biophysical principles underlying heterochromatin compartmentalization in the cell nucleus are elusive. Here, we assess mechanistically relevant features of pericentric heterochromatin compaction in mouse fibroblasts. We find that (1) HP1 has only a weak capacity to form liquid droplets in living cells; (2) the size, global accessibility, and compaction of heterochromatin foci are independent of HP1; (3) heterochromatin foci lack a separated liquid HP1 pool; and (4) heterochromatin compaction can toggle between two {"}digital{"} states depending on the presence of a strong transcriptional activator. These findings indicate that heterochromatin foci resemble collapsed polymer globules that are percolated with the same nucleoplasmic liquid as the surrounding euchromatin, which has implications for our understanding of chromatin compartmentalization and its functional consequences.",
keywords = "Heterochromatin protein 1, chromatin accessibility, chromatin compartmentalization, epigenetic editing, intracellular viscosity, liquid- liquid phase separation, nuclear organization, optodroplets, polarization-dependent fluorescence correlation spectroscopy, polymer collapse",
author = "Fabian Erdel and Anne Rademacher and Rifka Vlijm and Jana T{\"u}nnermann and Lukas Frank and Robin Weinmann and Elisabeth Schweigert and Klaus Yserentant and Johan Hummert and Caroline Bauer and Sabrina Schumacher and {Al Alwash}, Ahmad and Christophe Normand and Dirk-peter Herten and Johann Engelhardt and Karsten Rippe",
year = "2020",
month = apr,
day = "16",
doi = "10.1016/j.molcel.2020.02.005",
language = "English",
volume = "78",
pages = "236--249.e7",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Mouse heterochromatin adopts digital compaction states without showing hallmarks of HP1-driven liquid-liquid phase separation

AU - Erdel, Fabian

AU - Rademacher, Anne

AU - Vlijm, Rifka

AU - Tünnermann, Jana

AU - Frank, Lukas

AU - Weinmann, Robin

AU - Schweigert, Elisabeth

AU - Yserentant, Klaus

AU - Hummert, Johan

AU - Bauer, Caroline

AU - Schumacher, Sabrina

AU - Al Alwash, Ahmad

AU - Normand, Christophe

AU - Herten, Dirk-peter

AU - Engelhardt, Johann

AU - Rippe, Karsten

PY - 2020/4/16

Y1 - 2020/4/16

N2 - The formation of silenced and condensed heterochromatin foci involves enrichment of heterochromatin protein 1 (HP1). HP1 can bridge chromatin segments and form liquid droplets, but the biophysical principles underlying heterochromatin compartmentalization in the cell nucleus are elusive. Here, we assess mechanistically relevant features of pericentric heterochromatin compaction in mouse fibroblasts. We find that (1) HP1 has only a weak capacity to form liquid droplets in living cells; (2) the size, global accessibility, and compaction of heterochromatin foci are independent of HP1; (3) heterochromatin foci lack a separated liquid HP1 pool; and (4) heterochromatin compaction can toggle between two "digital" states depending on the presence of a strong transcriptional activator. These findings indicate that heterochromatin foci resemble collapsed polymer globules that are percolated with the same nucleoplasmic liquid as the surrounding euchromatin, which has implications for our understanding of chromatin compartmentalization and its functional consequences.

AB - The formation of silenced and condensed heterochromatin foci involves enrichment of heterochromatin protein 1 (HP1). HP1 can bridge chromatin segments and form liquid droplets, but the biophysical principles underlying heterochromatin compartmentalization in the cell nucleus are elusive. Here, we assess mechanistically relevant features of pericentric heterochromatin compaction in mouse fibroblasts. We find that (1) HP1 has only a weak capacity to form liquid droplets in living cells; (2) the size, global accessibility, and compaction of heterochromatin foci are independent of HP1; (3) heterochromatin foci lack a separated liquid HP1 pool; and (4) heterochromatin compaction can toggle between two "digital" states depending on the presence of a strong transcriptional activator. These findings indicate that heterochromatin foci resemble collapsed polymer globules that are percolated with the same nucleoplasmic liquid as the surrounding euchromatin, which has implications for our understanding of chromatin compartmentalization and its functional consequences.

KW - Heterochromatin protein 1

KW - chromatin accessibility

KW - chromatin compartmentalization

KW - epigenetic editing

KW - intracellular viscosity

KW - liquid- liquid phase separation

KW - nuclear organization

KW - optodroplets

KW - polarization-dependent fluorescence correlation spectroscopy

KW - polymer collapse

UR - http://www.scopus.com/inward/record.url?scp=85083012976&partnerID=8YFLogxK

U2 - 10.1016/j.molcel.2020.02.005

DO - 10.1016/j.molcel.2020.02.005

M3 - Article

C2 - 32101700

VL - 78

SP - 236-249.e7

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 2

ER -