Evidence map›Paper›PMID 31381567›Full record

ArticlePLoS genetics2019

Methyl-CpG-binding domain 9 (MBD9) is required for H2A.Z incorporation into chromatin at a subset of H2A.Z-enriched regions in the Arabidopsis genome.

Paja Sijacic, Dylan H Holder, Marko Bajic, Roger B Deal

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
8.7field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 56 citations in OpenAlex.

  1. Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Epigenetics in the modern era of crop improvements.Science China. Life sciences · 2025
    Review
  8. Article
  9. Roles of methyl-CpG-binding-domain (MBD) protiens in regulation of biological processes in plants.Physiology and molecular biology of plants : an international journal of functional plant biology · 2025
    Review
  10. Article
  11. Review
  12. Proteomic profiling ofPhysiology and molecular biology of plants : an international journal of functional plant biology · 2024
    Article
  13. Review
  14. Review
  15. Review
  16. Review
  17. Interactome of Arabidopsis Thaliana.Plants (Basel, Switzerland) · 2022
    Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Paja SijacicDepartment of Biology, Emory University, Atlanta, GA, United States of America.ORCID 0000-0003-1966-2365
Dylan H HolderDepartment of Biology, Emory University, Atlanta, GA, United States of America.ORCID 0000-0003-4043-2724
Marko BajicDepartment of Biology, Emory University, Atlanta, GA, United States of America.ORCID 0000-0002-8566-5153
Roger B DealDepartment of Biology, Emory University, Atlanta, GA, United States of America.ORCID 0000-0003-1289-688X
Emory University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM008490 · NIGMS · EMORY UNIVERSITY · PI BOSS, JEREMY M. · 1993 to 2022
$8.0M
NIGMS NIH HHS T32 GM008490
6 · The paper itself

Abstract

The SWR1 chromatin remodeling complex, which deposits the histone variant H2A.Z into nucleosomes, has been well characterized in yeast and animals, but its composition in plants has remained uncertain. We used the conserved SWR1 subunit ACTIN RELATED PROTEIN 6 (ARP6) as bait in tandem affinity purification experiments to isolate associated proteins from Arabidopsis thaliana. We identified all 11 subunits found in yeast SWR1 and the homologous mammalian SRCAP complexes, demonstrating that this complex is conserved in plants. We also identified several additional proteins not previously associated with SWR1, including Methyl-CpG-BINDING DOMAIN 9 (MBD9) and three members of the Alfin1-like protein family, all of which have been shown to bind modified histone tails. Since mbd9 mutant plants were phenotypically similar to arp6 mutants, we explored a potential role for MBD9 in H2A.Z deposition. We found that MBD9 is required for proper H2A.Z incorporation at thousands of discrete sites, which represent a subset of the genomic regions normally enriched with H2A.Z. We also discovered that MBD9 preferentially interacts with acetylated histone H4 peptides, as well as those carrying mono- or dimethylated H3 lysine 4, or dimethylated H3 arginine 2 or 8. Considering that MBD9-dependent H2A.Z sites show a distinct histone modification profile, we propose that MBD9 recognizes particular nucleosome modifications via its PHD- and Bromo-domains and thereby guides SWR1 to these sites for H2A.Z deposition. Our data establish the SWR1 complex as being conserved across eukaryotes and suggest that MBD9 may be involved in targeting the complex to specific genomic sites through nucleosomal interactions. The finding that MBD9 does not appear to be a core subunit of the Arabidopsis SWR1 complex, along with the synergistic phenotype of arp6;mbd9 double mutants, suggests that MBD9 also has important roles beyond H2A.Z deposition.

Indexed as

Chromatin Assembly and DisassemblyArabidopsisArabidopsis ProteinsChromatinGenome, PlantHistonesMutationNucleosomesPlants, Genetically ModifiedArabidopsis ProteinsAT1G52740 protein, ArabidopsisChromatinHistonesNucleosomes

Identifiers

PMID31381567
PMCPMC6695207
OpenAlexW2964684026

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.