Evidence map›Paper›PMID 20334638›Full record

ArticleEpigenetics & chromatin2010

Histone H1 variant-specific lysine methylation by G9a/KMT1C and Glp1/KMT1D.

Thomas Weiss, Sonja Hergeth, Ulrike Zeissler, Annalisa Izzo, Philipp Tropberger, Barry M Zee, Miroslav Dundr, Benjamin A Garcia, Sylvain Daujat, Robert Schneider

Open access · goldAbstract read
In one paragraph

Article in Epigenetics & chromatin, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.9field-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

55 citing papers in PubMed, 97 citations in OpenAlex.

  1. Review
  2. Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins.International journal of molecular sciences · 2024
    Article
  3. Article
  4. Histone variant-specific post-translational modifications.Seminars in cell & developmental biology · 2023
    Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Genes · 2022
    Review
  10. Targets of histone H3 lysine 9 methyltransferases.Frontiers in cell and developmental biology · 2022
    Review
  11. Review
  12. Review
  13. The missing linkGenes & development · 2021
    Review
  14. Molecular and Cellular Functions of the Linker Histone H1.2.Frontiers in cell and developmental biology · 2021
    Review
  15. Histone H1 Post-Translational Modifications: Update and Future Perspectives.International journal of molecular sciences · 2020
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

10 authors at 3 institutions in 2 countries.

Thomas WeissMPI for Immunobiology, Stübeweg 51, 79108 Freiburg, Germany.
Sonja Hergeth
Ulrike Zeissler
Annalisa Izzo
Philipp Tropberger
Barry M Zee
Miroslav Dundr
Benjamin A Garcia
Sylvain Daujat
Robert Schneider
Max Planck Institute of Immunobiology and Epigenetics · DEPrinceton University · USRosalind Franklin University of Medicine and Science · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe linker histone H1 has a key role in establishing and maintaining higher order chromatin structure and in regulating gene expression. Mammals express up to 11 different H1 variants, with H1.2 and H1.4 being the predominant ones in most somatic cells. Like core histones, H1 has high levels of covalent modifications; however, the full set of modifications and their biological role are largely unknown.

resultsIn this study, we used a candidate screen to identify enzymes that methylate H1 and to map their corresponding methylation sites. We found that the histone lysine methyltransferases G9a/KMT1C and Glp1/KMT1D methylate H1.2 in vitro and in vivo, and we mapped this novel site to lysine 187 (H1.2K187) in the C-terminus of H1. This H1.2K187 methylation is variant-specific. The main target for methylation by G9a in H1.2, H1.3, H1.5 and H1.0 is in the C-terminus, whereas H1.4 is preferentially methylated at K26 (H1.4K26me) in the N-terminus. We found that the readout of these marks is different; H1.4K26me can recruit HP1, but H1.2K187me cannot. Likewise, JMJD2D/KDM4 only reverses H1.4K26 methylation, clearly distinguishing these two methylation sites. Further, in contrast to C-terminal H1 phosphorylation, H1.2K187 methylation level is steady throughout the cell cycle.

conclusionsWe have characterised a novel methylation site in the C-terminus of H1 that is the target of G9a/Glp1 both in vitro and in vivo. To our knowledge, this is the first demonstration of variant-specific histone methylation by the same methyltransferases, but with differing downstream readers, thereby supporting the hypothesis of H1 variants having specific functions.

Identifiers

PMID20334638
PMCPMC2860349
OpenAlexW2131592995

What OpenQuestion holds

Textmetadata
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.