Evidence map›Paper›PMID 30445475›Full record

ArticleNucleic acids research2019

Single and double box HMGB proteins differentially destabilize nucleosomes.

Micah J McCauley, Ran Huo, Nicole Becker, Molly Nelson Holte, Uma M Muthurajan, Ioulia Rouzina, Karolin Luger, L James Maher, Nathan E Israeloff, Mark C Williams

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 45 citations in OpenAlex.

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  12. Simultaneous mass spectrometry analysis of cisplatin with oligonucleotide-peptide mixtures: implications for the mechanism of action.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Article
  13. Micropipette-based biomechanical nanotools on living cells.European biophysics journal : EBJ · 2022
    Review
  14. Review
  15. Effects of forces on chromatin.APL bioengineering · 2021
    Review
  16. Article
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  19. Review
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

10 authors at 5 institutions in 1 country.

Micah J McCauleyDepartment of Physics, Northeastern University, Boston, MA, USA.
Ran HuoDepartment of Physics, Northeastern University, Boston, MA, USA.
Nicole BeckerDepartment of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine and Science, Rochester, MN, USA.
Molly Nelson HolteDepartment of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine and Science, Rochester, MN, USA.
Uma M MuthurajanDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, CO, USA.
Ioulia RouzinaDepartment of Chemistry and Biochemistry, Ohio State University, Columbus, OH, USA.
Karolin LugerDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, CO, USA.
L James MaherDepartment of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine and Science, Rochester, MN, USA.
Nathan E IsraeloffDepartment of Physics, Northeastern University, Boston, MA, USA.
Mark C WilliamsDepartment of Physics, Northeastern University, Boston, MA, USA.
Northeastern University · USMayo Clinic · USHoward Hughes Medical Institute · USThe Ohio State University · USUniversity of Colorado Boulder · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleosome disruption plays a key role in many nuclear processes including transcription, DNA repair and recombination. Here we combine atomic force microscopy (AFM) and optical tweezers (OT) experiments to show that high mobility group B (HMGB) proteins strongly disrupt nucleosomes, revealing a new mechanism for regulation of chromatin accessibility. We find that both the double box yeast Hmo1 and the single box yeast Nhp6A display strong binding preferences for nucleosomes over linker DNA, and both HMGB proteins destabilize and unwind DNA from the H2A-H2B dimers. However, unlike Nhp6A, Hmo1 also releases half of the DNA held by the (H3-H4)2 tetramer. This difference in nucleosome destabilization may explain why Nhp6A and Hmo1 function at different genomic sites. Hmo1 is enriched at highly transcribed ribosomal genes, known to be depleted of histones. In contrast, Nhp6A is found across euchromatin, pointing to a significant difference in cellular function.

Indexed as

High Mobility Group ProteinsHMGN ProteinsMicroscopy, Atomic ForceNucleosomesOptical TweezersSaccharomyces cerevisiae ProteinsHigh Mobility Group ProteinsHMGN ProteinsHMO1 protein, S cerevisiaeNHP6A protein, S cerevisiaeNucleosomesSaccharomyces cerevisiae Proteins

Identifiers

PMID30445475
PMCPMC6344895
OpenAlexW2904102299

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.