Evidence map›Paper›PMID 17020925›Full record

ArticleNucleic acids research2006

The Arabidopsis SUVR4 protein is a nucleolar histone methyltransferase with preference for monomethylated H3K9.

Tage Thorstensen, Andreas Fischer, Silje V Sandvik, Sylvia S Johnsen, Paul E Grini, Gunter Reuter, Reidunn B Aalen

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 63 citations in OpenAlex.

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  8. Review
  9. Genome-Wide Identification of Epigenetic Regulators inInternational journal of molecular sciences · 2020
    Article
  10. The function of histone lysine methylation related SET domain group proteins in plants.Protein science : a publication of the Protein Society · 2020
    Review
  11. Article
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  18. SNF2 chromatin remodeler-family proteins FRG1 and -2 are required for RNA-directed DNA methylation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  19. Article
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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

7 authors at 3 institutions in 2 countries.

Tage ThorstensenDepartment of Molecular Biosciences, University of Oslo, P.O. Box 1041 Blindern, N-0316 Oslo, Norway.
Andreas Fischer
Silje V Sandvik
Sylvia S Johnsen
Paul E Grini
Gunter Reuter
Reidunn B Aalen
University of Oslo · NOMartin Luther University Halle-Wittenberg · DEUiT The Arctic University of Norway · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins containing the evolutionarily conserved SET domain are involved in regulation of eukaryotic gene expression and chromatin structure through their histone lysine methyltransferase (HMTase) activity. The Drosophila SU(VAR)3-9 protein and related proteins of other organisms have been associated with gene repression and heterochromatinization. In Arabidopsis there are 10 SUVH and 5 SUVR genes encoding proteins similar to SU(VAR)3-9, and 4 SUVH proteins have been shown to control heterochromatic silencing by its HMTase activity and by directing DNA methylation. The SUVR proteins differ from the SUVH proteins in their domain structure, and we show that the closely related SUVR1, SUVR2 and SUVR4 proteins contain a novel domain at their N-terminus, and a SUVR specific region preceding the SET domain. Green fluorescent protein (GFP)-fusions of these SUVR proteins preferably localize to the nucleolus, suggesting involvement in regulation of rRNA expression, in contrast to other SET-domain proteins studied so far. A novel HMTase specificity was demonstrated for SUVR4, in that monomethylated histone H3K9 is its preferred substrate in vitro.

Indexed as

Alternative SplicingAmino Acid SequenceArabidopsisArabidopsis ProteinsCell NucleolusHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesLysineMethylationMolecular Sequence DataProtein MethyltransferasesProtein Sorting SignalsProtein Structure, TertiarySequence AlignmentSubstrate SpecificityArabidopsis ProteinsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesLysineProtein MethyltransferasesProtein Sorting SignalsSUVR1 protein, ArabidopsisSUVR2 protein, ArabidopsisSUVR4 protein, Arabidopsis

Identifiers

PMID17020925
PMCPMC1636477
OpenAlexW2157604566

What OpenQuestion holds

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LicenceCC BY-NC
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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.