Evidence map›Paper›PMID 25965993›Full record

ArticleScientific reports2015

Dot1 histone methyltransferases share a distributive mechanism but have highly diverged catalytic properties.

Iris J E Stulemeijer, Dirk De Vos, Kirsten van Harten, Onkar K Joshi, Olga Blomberg, Tibor van Welsem, Marit Terweij, Hanneke Vlaming, Erik L de Graaf, A F Maarten Altelaar and 2 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

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  9. Epigenetic Control of a Local Chromatin Landscape.International journal of molecular sciences · 2020
    Review
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  14. Review
  15. 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

12 authors at 2 institutions in 1 country.

Iris J E StulemeijerDivision of Gene Regulation, Netherlands Cancer Institute, Amsterdam, 1066 CX, The Netherlands.
Dirk De VosDepartment of Biology, University of Antwerp, Antwerp, 2020, Belgium.
Kirsten van HartenDivision of Gene Regulation, Netherlands Cancer Institute, Amsterdam, 1066 CX, The Netherlands.
Onkar K JoshiDivision of Gene Regulation, Netherlands Cancer Institute, Amsterdam, 1066 CX, The Netherlands.
Olga BlombergDivision of Gene Regulation, Netherlands Cancer Institute, Amsterdam, 1066 CX, The Netherlands.
Tibor van WelsemDivision of Gene Regulation, Netherlands Cancer Institute, Amsterdam, 1066 CX, The Netherlands.
Marit TerweijDivision of Gene Regulation, Netherlands Cancer Institute, Amsterdam, 1066 CX, The Netherlands.
Hanneke VlamingDivision of Gene Regulation, Netherlands Cancer Institute, Amsterdam, 1066 CX, The Netherlands.
Erik L de GraafBiomolecular Mass Spectrometry and Proteomics Group, The Netherlands Proteomics Centre, Utrecht University, Utrecht, 3584 CH, The Netherlands.
A F Maarten AltelaarBiomolecular Mass Spectrometry and Proteomics Group, The Netherlands Proteomics Centre, Utrecht University, Utrecht, 3584 CH, The Netherlands.
Barbara M BakkerDepartment of Pediatrics, Systems Biology Centre for Energy Metabolism and Ageing, Center for Liver, Digestive and Metabolic Diseases, University of Groningen, University Medical Center Groningen, Groningen, 9713 GZ, The Netherlands.
Fred van LeeuwenDivision of Gene Regulation, Netherlands Cancer Institute, Amsterdam, 1066 CX, The Netherlands.
The Netherlands Cancer Institute · NLOncode Institute · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The conserved histone methyltransferase Dot1 establishes an H3K79 methylation pattern consisting of mono-, di- and trimethylation states on histone H3 via a distributive mechanism. This mechanism has been shown to be important for the regulation of the different H3K79 methylation states in yeast. Dot1 enzymes in yeast, Trypanosoma brucei (TbDot1A and TbDot1B, which methylate H3K76) and human (hDot1L) generate very divergent methylation patterns. To understand how these species-specific methylation patterns are generated, the methylation output of the Dot1 enzymes was compared by expressing them in yeast at various expression levels. Computational simulations based on these data showed that the Dot1 enzymes have highly distinct catalytic properties, but share a distributive mechanism. The mechanism of methylation and the distinct rate constants have implications for the regulation of H3K79/K76 methylation. A mathematical model of H3K76 methylation during the trypanosome cell cycle suggests that temporally-regulated consecutive action of TbDot1A and TbDot1B is required for the observed regulation of H3K76 methylation states.

Indexed as

Models, BiologicalCatalysisCell CycleHistone-Lysine N-MethyltransferaseHistonesHumansMethylationNuclear ProteinsProtozoan ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpecies SpecificityTrypanosoma brucei bruceiDot1 protein, S cerevisiaeHistone-Lysine N-MethyltransferaseHistonesNuclear ProteinsProtozoan ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID25965993
PMCPMC4650758
OpenAlexW1848123587

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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.