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.
journal_name
Mol Celljournal_title
Molecular cellauthors
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 DP,Engelhardt J,Rippe Kdoi
10.1016/j.molcel.2020.02.005subject
Has Abstractpub_date
2020-04-16 00:00:00pages
236-249.e7issue
2eissn
1097-2765issn
1097-4164pii
S1097-2765(20)30075-7journal_volume
78pub_type
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