ArticleThe Journal of biological chemistry2014
Trimethylation of histone H3 lysine 36 by human methyltransferase PRDM9 protein.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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.
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.
Who cites it
73 citing papers in PubMed, 116 citations in OpenAlex.
- Why recombination hotspots?PLoS genetics · 2026Review
- Assembling Ternary Dead-End Complex for Covalent Trapping of Protein Lysine Methyltransferases.Journal of the American Chemical Society · 2026Article
- Interleukin-38 is a negative regulator of trained immunity-A retrospective multi-omics study.iScience · 2025Article
- Article
- Unveiling the Role of Histone Methyltransferases in Psoriasis Pathogenesis: Insights from Transcriptomic Analysis.International journal of molecular sciences · 2025Article
- Investigation and design of the dual specificity of the PRDM9 protein lysine methyltransferase.Communications biology · 2025Article
- Mechanisms and rationales of SAM homeostasis.Trends in biochemical sciences · 2025Review
- Epigenetic Regulation of CD8European journal of immunology · 2025Article
- Dynamic Changes in Histone Modifications Are Associated with Differential Chromatin Interactions.Genes · 2024Article
- Loss of ZNF408 attenuates STING-mediated immune surveillance in breast carcinogenesis.iScience · 2024Article
- Bridging the gap between the evolutionary dynamics and the molecular mechanisms of meiosis: A model based exploration of the PRDM9 intra-genomic Red Queen.PLoS genetics · 2024Article
- Recent advances in mechanisms ensuring the pairing, synapsis and segregation of XY chromosomes in mice and humans.Cellular and molecular life sciences : CMLS · 2024Review
- Article
- Natural variation in the zinc-finger-encoding exon of Prdm9 affects hybrid sterility phenotypes in mice.Genetics · 2024Article
- SilenceREIN: seeking silencers on anchors of chromatin loops by deep graph neural networks.Briefings in bioinformatics · 2023Article
- Down the Penrose stairs, or how selection for fewer recombination hotspots maintains their existence.eLife · 2023Article
- Biochemical and structural characterization of the first-discovered metazoan DNA cytosine-N4 methyltransferase from the bdelloid rotifer Adineta vaga.The Journal of biological chemistry · 2023Article
- Chromatin Remodeling Enzyme Cluster Predicts Prognosis and Clinical Benefit of Therapeutic Strategy in Breast Cancer.International journal of molecular sciences · 2023Article
- Epigenetic Regulations in Mammalian Cells: Roles and Profiling Techniques.Molecules and cells · 2023Review
- SMYD5 is a histone H3-specific methyltransferase mediating mono-methylation of histone H3 lysine 36 and 37.Biochemical and biophysical research communications · 2022Article
13 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 2 institutions in 1 country.
Funding
Abstract
PRDM9 (PR domain-containing protein 9) is a meiosis-specific protein that trimethylates H3K4 and controls the activation of recombination hot spots. It is an essential enzyme in the progression of early meiotic prophase. Disruption of the PRDM9 gene results in sterility in mice. In human, several PRDM9 SNPs have been implicated in sterility as well. Here we report on kinetic studies of H3K4 methylation by PRDM9 in vitro indicating that PRDM9 is a highly active histone methyltransferase catalyzing mono-, di-, and trimethylation of the H3K4 mark. Screening for other potential histone marks, we identified H3K36 as a second histone residue that could also be mono-, di-, and trimethylated by PRDM9 as efficiently as H3K4. Overexpression of PRDM9 in HEK293 cells also resulted in a significant increase in trimethylated H3K36 and H3K4 further confirming our in vitro observations. Our findings indicate that PRDM9 may play critical roles through H3K36 trimethylation in cells.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.