Evidence map›Paper›PMID 25183522›Full record

ArticleNucleic acids research2014

Arabidopsis MRG domain proteins bridge two histone modifications to elevate expression of flowering genes.

Yifeng Xu, Eng-Seng Gan, Jie Zhou, Wan-Yi Wee, Xiaoyu Zhang, Toshiro Ito

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
9.3field-weighted citation impact, top 2% 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

46 citing papers in PubMed, 92 citations in OpenAlex.

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  12. PIF transcription factors-versatile plant epigenome landscapers.Frontiers in epigenetics and epigenomics · 2024
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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

6 authors at 3 institutions in 2 countries.

Yifeng XuTemasek Life Sciences Laboratory, National University of Singapore, Singapore 117604, Republic of Singapore.
Eng-Seng GanTemasek Life Sciences Laboratory, National University of Singapore, Singapore 117604, Republic of Singapore Department of Biological Sciences, National University of Singapore, Singapore 117543, Republic of Singapore.
Jie ZhouTemasek Life Sciences Laboratory, National University of Singapore, Singapore 117604, Republic of Singapore.
Wan-Yi WeeTemasek Life Sciences Laboratory, National University of Singapore, Singapore 117604, Republic of Singapore.
Xiaoyu ZhangDepartment of Plant Biology, University of Georgia, Athens, GA 30602-7271, USA.
Toshiro ItoTemasek Life Sciences Laboratory, National University of Singapore, Singapore 117604, Republic of Singapore Department of Biological Sciences, National University of Singapore, Singapore 117543, Republic of Singapore itot@tll.org.sg.
Temasek Life Sciences Laboratory · SGNational University of Singapore · SGUniversity of Georgia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trimethylation of lysine 36 of histone H3 (H3K36me3) is found to be associated with various transcription events. In Arabidopsis, the H3K36me3 level peaks in the first half of coding regions, which is in contrast to the 3'-end enrichment in animals. The MRG15 family proteins function as 'reader' proteins by binding to H3K36me3 to control alternative splicing or prevent spurious intragenic transcription in animals. Here, we demonstrate that two closely related Arabidopsis homologues (MRG1 and MRG2) are localised to the euchromatin and redundantly ensure the increased transcriptional levels of two flowering time genes with opposing functions, FLOWERING LOCUS C and FLOWERING LOCUS T (FT). MRG2 directly binds to the FT locus and elevates the expression in an H3K36me3-dependent manner. MRG1/2 binds to H3K36me3 with their chromodomain and interact with the histone H4-specific acetyltransferases (HAM1 and HAM2) to achieve a high expression level through active histone acetylation at the promoter and 5' regions of target loci. Together, this study presents a mechanistic link between H3K36me3 and histone H4 acetylation. Our data also indicate that the biological functions of MRG1/2 have diversified from their animal homologues during evolution, yet they still maintain their conserved H3K36me3-binding molecular function.

Indexed as

Gene Expression Regulation, PlantAcetylationArabidopsisArabidopsis ProteinsChromosomal Proteins, Non-HistoneEuchromatinFlowersHistone AcetyltransferasesHistone-Lysine N-MethyltransferaseHistonesMADS Domain ProteinsMutationPhenotypeTranscription, GeneticArabidopsis ProteinsAt5g10140 protein, ArabidopsisChromosomal Proteins, Non-HistoneEuchromatinFT protein, ArabidopsisHistone AcetyltransferasesHistone-Lysine N-MethyltransferaseHistonesLAZ2 protein, ArabidopsisMADS Domain ProteinsMRG1 protein, ArabidopsisMRG2 protein, Arabidopsis

Identifiers

PMID25183522
PMCPMC4176166
OpenAlexW2126599837

What OpenQuestion holds

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Registered trials

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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.