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ATAC-seq profiling of MORC2 knock-out HEK293T cells

GSE274771 Homo sapiens Genome binding/occupancy profiling by high throughput sequencing 4 samples Submitted 2025/05/05 Platform GPL30173
Summary
We report an in vitro reconstitution of full-length MORC2, the most commonly mutated MORC member, linked to various cancers and neurological disorders. MORC2 possesses multiple DNA binding sites that undergo structural rearrangement upon DNA binding. MORC2 locks onto the DNA using its C-terminal domain (CTD) and acts as a sliding clamp. A conserved phosphate-interacting motif within the CTD was found to regulate ATP hydrolysis and cooperative DNA binding. Importantly, MORC2 mediates chromatin remodelling via ATP hydrolysis-dependent DNA compaction, regulated by the phosphorylation state of its CTD.
Published in
MORC2 is a phosphorylation-dependent DNA compaction machine
Tan W, Park J, Venugopal H et al. · Nature communications 2025 · PMID 40593625 · doi:10.1038/s41467-025-60751-z
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Also filed as BioProject PRJNA1147785 and SRA study SRP526166. Searching any of these in the dataset finder brings you back here.

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