Journal
MOLECULAR CELL
Volume 75, Issue 4, Pages 700-+Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2019.07.032
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Funding
- W.M. Keck Foundation
- John and Virginia Kaneb Fellowship
- University of Texas System's Rising STARs Award
- NIH [R01 GM129301, 1R35GM130272, P41GM103481, R01 GM114054]
- University of California, San Francisco, Research Resource Program (RRP) Shared Equipment Award
- Ruth L. Kirschstein National Research Service Award [GM007185]
- University of Texas Rio Grande Valley Start-up Grant
- University of California, Los Angeles, Dissertation Year Fellowship
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Microrchidia (MORC) ATPases are critical for gene silencing and chromatin compaction in multiple eukaryotic systems, but the mechanisms by which MORC proteins act are poorly understood. Here, we apply a series of biochemical, single-molecule, and cell-based imaging approaches to better understand the function of the Caenorhabditis elegans MORC-1 protein. We find that MORC-1 binds to DNA in a length-dependent but sequence non-specific manner and compacts DNA by forming DNA loops. MORC-1 molecules diffuse along DNA but become static as they grow into foci that are topologically entrapped on DNA. Consistent with the observed MORC-1 multimeric assemblies, MORC-1 forms nuclear puncta in cells and can also form phase-separated droplets in vitro. We also demonstrate that MORC-1 compacts nucleosome templates. These results suggest that MORCs affect genome structure and gene silencing by forming multimeric assemblages to topologically entrap and progressively loop and compact chromatin.
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