Evidence map›Paper›PMID 40768570›Full record

ArticleScience advances2025

Histone acetylation readers Bdf1 and Yaf9 direct SWR1 remodeler to +1 nucleosome.

Anand Ranjan, Ejlal Elalaoui, Xiaona Tang, Justin Cha, Robert K Louder, Kevin Nguyen, Joseph Ye, Muhammad Bennani, Anne M Gardner, Derrick Liu and 2 more

Abstract read
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
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

12 authors.

Anand RanjanDepartment of Biology, Johns Hopkins University, Baltimore, MD, USA.ORCID 0000-0001-6071-6017
Ejlal ElalaouiDepartment of Biology, Johns Hopkins University, Baltimore, MD, USA.ORCID 0000-0003-0842-5647
Xiaona TangDepartment of Biology, Johns Hopkins University, Baltimore, MD, USA.
Justin ChaDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY, USA.
Robert K LouderDepartment of Biology, Johns Hopkins University, Baltimore, MD, USA.ORCID 0000-0002-6944-9346
Kevin NguyenDepartment of Biology, Johns Hopkins University, Baltimore, MD, USA.ORCID 0009-0000-2568-2173
Joseph YeDepartment of Biology, Johns Hopkins University, Baltimore, MD, USA.ORCID 0000-0003-1735-7287
Muhammad BennaniDepartment of Biology, Johns Hopkins University, Baltimore, MD, USA.
Anne M GardnerDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY, USA.ORCID 0000-0001-7095-772X
Derrick LiuDepartment of Biology, Johns Hopkins University, Baltimore, MD, USA.ORCID 0009-0007-8548-8728
B Franklin PughDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY, USA.
Carl WuDepartment of Biology, Johns Hopkins University, Baltimore, MD, USA.ORCID 0000-0001-6933-5763

Funding

HIGH RESOLUTION EPIGENOMIC MAPS OF YEAST IN RESPONSE TO ENVIRONMENTAL STRESSR01ES034353 · NIEHS · CORNELL UNIVERSITY · PI B FRANKLIN PUGH · 2022 to 2026
$3.3M
EPIGENOMIC REGULATION OF GENOMESR35GM145217 · NIGMS · CORNELL UNIVERSITY · PI B FRANKLIN PUGH · 2022 to 2026
$2.8M
NIEHS NIH HHS R01 ES034353NIGMS NIH HHS R35 GM145217
6 · The paper itself

Abstract

The histone variant H2A.Z marking permissive chromatin is deposited by the multicomponent SWR1 chromatin remodeler, which is targeted to nucleosome-free promoters by a DNA length-sensing module. How SWR1 is directed to the flanking acetylated +1 nucleosome, its physiological substrate, has been enigmatic. We show by live-cell, single-molecule tracking that SWR1 subunits Bdf1 and Yaf9 harboring histone acetylation reader domains differentially regulate chromatin binding: Bdf1 promotes SWR1 association, while Yaf9-YEATS slows its dissociation. Notably, single-molecule tracking and genome-wide chromatin immunoprecipitation combined with exonuclease treatment reveal Bdf1 and Yaf9 contributions to global SWR1 targeting and histone exchange at +1 nucleosomes. Our findings highlight the in-cell biochemistry of histone readers and suggest a generalizable, two-stage mechanism wherein acetylated nucleosome interactions initially constrain the three-dimensional diffusion of SWR1 to increase local concentration, followed by stochastic one-dimensional diffusion at nucleosome-depleted regions with directional capture by acetylated +1 nucleosomes.

Indexed as

Adenosine TriphosphatasesChromatin Assembly and DisassemblyHistonesNucleosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsAcetylationProtein BindingAdenosine TriphosphatasesHistonesNucleosomesSaccharomyces cerevisiae ProteinsSwr1 protein, S cerevisiaeTranscription Factors

Identifiers

PMID40768570
PMCPMC12327448

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.