Evidence map›Paper›PMID 40412388›Full record

ArticleMolecular cell2025

FACT weakens the nucleosomal barrier to transcription and preserves its integrity by forming a hexasome-like intermediate.

Francesca Burgos-Bravo, Alexander B Tong, Chen Li, César Díaz-Celis, Craig D Kaplan, Gary LeRoy, Danny Reinberg, Carlos Bustamante

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Review
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  3. Article
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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

8 authors.

Francesca Burgos-BravoJason Choy Laboratory of Single Molecule Biophysics, University of California, Berkeley, Berkeley, CA 94704, USA; Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94704, USA; California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA 94720, USA.
Alexander B TongJason Choy Laboratory of Single Molecule Biophysics, University of California, Berkeley, Berkeley, CA 94704, USA; California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA 94720, USA; Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA.
Chen LiJason Choy Laboratory of Single Molecule Biophysics, University of California, Berkeley, Berkeley, CA 94704, USA; California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA 94720, USA; Biophysics Graduate Group, University of California, Berkeley, Berkeley, CA 94720, USA.
César Díaz-CelisJason Choy Laboratory of Single Molecule Biophysics, University of California, Berkeley, Berkeley, CA 94704, USA; California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA 94720, USA.
Craig D KaplanDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, CA 15260, USA.
Gary LeRoyHoward Hughes Medical Institute, University of Miami Miller School of Medicine, Miami, FL 33136, USA.
Danny ReinbergHoward Hughes Medical Institute, University of Miami Miller School of Medicine, Miami, FL 33136, USA.
Carlos BustamanteJason Choy Laboratory of Single Molecule Biophysics, University of California, Berkeley, Berkeley, CA 94704, USA; Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94704, USA; California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA 94720, USA; Biophysics Graduate Group, University of California, Berkeley, Berkeley, CA 94720, USA; Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA; Department of Physics, University of California, Berkeley, Berkeley, CA 94720, USA; Molecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; Kavli Energy Nanoscience Institute, University of California Berkeley, Berkeley, CA 94720, USA. Electronic address: carlosb@berkeley.edu.

Funding

THE PHYSICAL CHEMISTRY OF NUCLEIC ACIDSR01GM032543 · NIGMS · UNIVERSITY OF OREGON · PI CARLOS Jose BUSTAMANTE · 1985 to 2026
$6.4M
Repression via Facultative HeterochromatinR01CA199652 · NCI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI REINBERG, DANNY · 2015 to 2025
$4.2M
Mechanisms of RNA Polymerase II transcriptionR35GM144116 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Craig Kaplan · 2022 to 2026
$3.4M
PHYSICAL CHEMISTRY OF NUCLEIC ACIDSR37GM032543 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BUSTAMANTE, CARLOS JOSE · 1999 to 2008
$2.4M
NCI NIH HHS R01 CA199652NIGMS NIH HHS R01 GM032543NIGMS NIH HHS R35 GM144116NIGMS NIH HHS R37 GM032543
6 · The paper itself

Abstract

Transcription of yeast RNA polymerase II through nucleosomes requires the assistance of the histone chaperone FACT (facilitates chromatin transcription). Yet, how FACT modulates the nucleosomal mechanical barrier to affect the polymerase's elongation dynamics is poorly understood. Using high-resolution single-molecule optical tweezers, we show that FACT greatly decreases the magnitude of the barrier by favoring the unwrapping of DNA from the distal H2A-H2B dimer, which, in turn, weakens the contacts near the dyad, significantly reducing the enzyme's crossing time. We show that barrier crossing depends on the asymmetric flexibility of the nucleosome arms, an asymmetry we find across the genome. Mechanical unwrapping of Cy3-H2A nucleosomes reveals that FACT reduces their unwrapping force and stabilizes a hexasome-like intermediate that retains both labeled dimers during successive unwrapping cycles. This intermediate is also observed after transcription. In conclusion, FACT facilitates nucleosomal transcription by weakening the barrier and actively assisting the maintenance of nucleosomal integrity after enzyme passage.

Indexed as

NucleosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptional Elongation FactorsTranscription, GeneticChromosomal Proteins, Non-HistoneDimerizationDNADNA-Binding ProteinsGenomeHigh Mobility Group ProteinsHistonesNuclear ProteinsOptical TweezersRNA Polymerase IIChromosomal Proteins, Non-HistoneDNADNA-Binding ProteinsFACT protein, S cerevisiaeHigh Mobility Group ProteinsHistonesNuclear ProteinsNucleosomesRNA Polymerase IISaccharomyces cerevisiae ProteinsSPT4 protein, S cerevisiaeSPT5 transcriptional elongation factorTranscriptional Elongation FactorsFACThistone chaperonenucleosomal DNA flexibilitynucleosomenucleosome integritynucleosome unwrappingoptical tweezersRNA polymerase IIsingle-molecule fluorescencetranscription

Identifiers

PMID40412388
PMCPMC12204072

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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.