Evidence map›Paper›PMID 40764940›Full record

ArticleEpigenetics & chromatin2025

Bromodomain proteins IBD1 and IBD2 link histone acetylation to SWR1- and INO80-mediated H2A.Z regulation in Tetrahymena.

Jyoti Garg, Alejandro Saettone, Syed Nabeel-Shah, Steven Dang, Abdul Hadi Khalid, Jérémy Loehr, Alexandra Petrova, James D Burns, Peter Karabatsos, Sherin Shibin and 5 more

Abstract read
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Article in Epigenetics & chromatin, 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

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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

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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.

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4 · The record

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5 · Who and what money

Authors and funding

15 authors.

Jyoti Garg *Department of Chemistry and Biology, Toronto Metropolitan University, Toronto, Canada.
Alejandro Saettone *Department of Chemistry and Biology, Toronto Metropolitan University, Toronto, Canada.
Syed Nabeel-Shah *Department of Molecular Genetics, University of Toronto, Toronto, Canada.
Steven DangDepartment of Chemistry and Biology, Toronto Metropolitan University, Toronto, Canada.
Abdul Hadi KhalidDepartment of Chemistry and Biology, Toronto Metropolitan University, Toronto, Canada.
Jérémy LoehrEndocrinology and Nephrology Research Program, CHU de Québec-Université Laval Research Center, Quebec City, Canada.
Alexandra PetrovaDepartment of Chemistry and Biology, Toronto Metropolitan University, Toronto, Canada.
James D BurnsDepartment of Molecular Genetics, University of Toronto, Toronto, Canada.
Peter KarabatsosDepartment of Chemistry and Biology, Toronto Metropolitan University, Toronto, Canada.
Sherin ShibinDepartment of Chemistry and Biology, Toronto Metropolitan University, Toronto, Canada.
Suzanne WahabDepartment of Chemistry and Biology, Toronto Metropolitan University, Toronto, Canada.
Sean D TavernaDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Jack F GreenblattDepartment of Molecular Genetics, University of Toronto, Toronto, Canada.
Jean-Philippe LambertEndocrinology and Nephrology Research Program, CHU de Québec-Université Laval Research Center, Quebec City, Canada. Jean-Philippe.Lambert@crchudequebec.ulaval.ca.
Jeffrey FillinghamDepartment of Chemistry and Biology, Toronto Metropolitan University, Toronto, Canada. jeffrey.fillingham@torontomu.ca.

Funding

CIHR Foundation Grant FDN-154338Natural Sciences and Engineering Research Council of Canada RGPIN-2020-07036NSERC RGPIN-2024-04260NSERC Alliance Grant ALLRP 571480 - 21
6 · The paper itself

Abstract

backgroundINO80 and SWR1 are evolutionarily related ATP-dependent chromatin remodeling complexes that regulate the chromatin occupancy of the histone variant H2A.Z, playing critical roles in transcriptional regulation, genome replication, and DNA repair. While the H2A.Z-related functions of INO80 and SWR1 are well characterized in budding yeast and metazoans, much less is known about their composition and chromatin-targeting mechanisms outside of the Opisthokonts. We previously found that a distinct bromodomain-containing protein, IBD1, is involved in multiple chromatin-related complexes, including the SWR1-complex, in the ciliate protozoan Tetrahymena thermophila.

resultsHere, we report that a closely related bromodomain-containing protein, IBD2, functions as an acetyl lysine reader module within a putative INO80 complex. Through iterative proteomic analyses, we show that the Tetrahymena INO80 complex retains several conserved subunits found in its yeast and metazoan counterparts. In vitro binding assays reveal that recombinant IBD2 preferentially recognizes acetylated histone H3 tails. Chromatin immunoprecipitation followed by high-throughput sequencing (ChIP-seq) demonstrates that IBD2 is enriched near transcription start sites and promoter regions. Notably, the IBD1 and IBD2 genomic binding profiles strongly correlate with that of H2A.Z (Hv1), supporting their functional association with the SWRI- and INO80-complexes.

conclusionsTogether, our findings support a model in which H2A.Z chromatin dynamics are modulated by SWR1- and INO80-complexes that are differentially recruited to chromatin via distinct bromodomain proteins that recognize specific histone acetylation marks.

Indexed as

HistonesProtozoan ProteinsTetrahymena thermophilaAcetylationChromatin Assembly and DisassemblyHistonesProtozoan ProteinsBromodomainsChromatin remodelingH2A.ZINO80cSWR1cTranscription

Identifiers

PMID40764940
PMCPMC12326766

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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.