Evidence map›Paper›PMID 31442422›Full record

ArticleMolecular cell2019

The Gene-Silencing Protein MORC-1 Topologically Entraps DNA and Forms Multimeric Assemblies to Cause DNA Compaction.

HyeongJun Kim, Linda Yen, Somsakul P Wongpalee, Jessica A Kirshner, Nicita Mehta, Yan Xue, Jonathan B Johnston, Alma L Burlingame, John K Kim, Joseph J Loparo and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.8field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

44 citing papers in PubMed, 76 citations in OpenAlex.

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  18. ThemSphere · 2024
    Article
  19. AeLife · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 5 institutions in 2 countries.

HyeongJun KimDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; Department of Physics and Astronomy, University of Texas Rio Grande Valley, Edinburg, TX 78539, USA; Howard Hughes Medical Institute, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Linda YenDepartment of Molecular, Cell, and Developmental Biology, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Somsakul P WongpaleeDepartment of Molecular, Cell, and Developmental Biology, University of California, Los Angeles, Los Angeles, CA 90095, USA; Department of Microbiology, Faculty of Medicine, Chiang Mai University, Chiang Mai 50200, Thailand.
Jessica A KirshnerDepartment of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
Nicita MehtaDepartment of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
Yan XueDepartment of Molecular, Cell, and Developmental Biology, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Jonathan B JohnstonDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94158, USA; Howard Hughes Medical Institute, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Alma L BurlingameDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94158, USA.
John K KimDepartment of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
Joseph J LoparoDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: joseph_loparo@hms.harvard.edu.
Steve E JacobsenDepartment of Molecular, Cell, and Developmental Biology, University of California, Los Angeles, Los Angeles, CA 90095, USA; Howard Hughes Medical Institute, University of California, Los Angeles, Los Angeles, CA 90095, USA. Electronic address: jacobsen@ucla.edu.
Howard Hughes Medical Institute · USJohns Hopkins University · USUniversity of California, Los Angeles · USHarvard University · USUniversity of California, San Francisco · US

Funding

UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
CELLULAR AND MOLECULAR BIOLOGYT32GM007231 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI VAN DOREN, MARK B · 1985 to 2020
$18.4M
Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
Regulation of translesion synthesis by the bacterial replisomeR01GM114065 · NIGMS · HARVARD MEDICAL SCHOOL · PI LOPARO, JOSEPH J. · 2015 to 2024
$3.0M
Formation and Function of Glycolytic Bodies in HypoxiaR01GM129301 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI KIM, JOHN · 2018 to 2021
$1.9M
Epigenetic gene regulation in ArabidopsisR35GM130272 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI JACOBSEN, STEVEN E · 2019 to 2023
$1.6M
NIGMS NIH HHS P41 GM103481NIGMS NIH HHS R01 GM114065NIGMS NIH HHS R01 GM129301NIGMS NIH HHS R35 GM130272NIGMS NIH HHS T32 GM007185NIGMS NIH HHS T32 GM007231
6 · The paper itself

Abstract

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.

Indexed as

Nucleic Acid ConformationProtein MultimerizationAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsDNA, HelminthNuclear ProteinsNucleosomesCaenorhabditis elegans ProteinsDNA, HelminthMORC-1 protein, C elegansNuclear ProteinsNucleosomesDNA-binding proteinDNA compactiongenome organizationGHKL ATPasesMORC

Identifiers

PMID31442422
PMCPMC6814019
OpenAlexW2969461247

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.