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Status |
Public on Dec 01, 2019 |
Title |
The nuclear matrix protein SAFB maintains heterochromatin architecture through RNA-dependent phase separation [HiChIP] |
Organism |
Mus musculus |
Experiment type |
Other
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Summary |
Eukaryotic chromosomes fold into topologically associating domains (TADs), which further gather in active (A) or inactive (B) genomic compartments. Here we show that Scaffold Attachment Factor B (SAFB), a nuclear matrix-associated protein with RNA binding functions, modulates global chromatin condensation in a dosage-dependent manner. Upon the depletion of SAFB, the genome coverage of Lamina-associated-domains (LADs) decreases from 53.33% to 45.93%, and both inter- and intra-TAD chromatin-chromatin interactions in compartment B decrease significantly. In the nucleus, SAFB favorably co-localizes with H3K9me3, a marker of heterochromatin, and the disruption of SAFB leads to a collapse of H3K9me3 foci. Furthermore, we show that SAFB proteins can form liquid-liquid phase separation in the cell and in vitro. Intriguingly, SAFB interacts with RNAs from repetitive elements enriched in heterochromatin (e.g., Major Satellites and LINE1), which can promote SAFB-mediated phase separation, depending on the density of SAFB recognizing motifs in the RNAs.
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Overall design |
H3K9me3 HiChIP data in Ctrl and Safb KD AML12 cells.
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Citation(s) |
31677973 |
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Submission date |
Nov 27, 2019 |
Last update date |
Mar 01, 2020 |
Contact name |
Luzhang Ji |
E-mail(s) |
jiluzhang@tongji.edu.cn
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Organization name |
Tongji University
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Street address |
1239 Siping Rd.
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City |
Shanghai |
ZIP/Postal code |
200092 |
Country |
China |
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Platforms (1) |
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Samples (8)
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This SubSeries is part of SuperSeries: |
GSE125037 |
The Nuclear Matrix Protein SAFB Cooperates with Major Satellite RNAs to Stabilize Heterochromatin Architecture Partially through Phase Separation |
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Relations |
BioProject |
PRJNA592152 |
SRA |
SRP233493 |