Evidence map›Paper›PMID 16100335›Full record

ArticleThe Plant cell2005

Monomethyl histone H3 lysine 4 as an epigenetic mark for silenced euchromatin in Chlamydomonas.

Karin van Dijk, Katherine E Marley, Byeong-ryool Jeong, Jianping Xu, Jennifer Hesson, Ronald L Cerny, Jakob H Waterborg, Heriberto Cerutti

Abstract read
In one paragraph

Article in The Plant cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
–field-weighted citation impact
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

43 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. An Improved Top-Down Mass Spectrometry Characterization ofJournal of the American Society for Mass Spectrometry · 2021
    Article
  11. Article
  12. Genes · 2020
    Article
  13. Inhibition of DNA Methylation inFrontiers in genetics · 2020
    Article
  14. Review
  15. Article
  16. Article
  17. RNA-binding protein DUS16 plays an essential role in primary miRNA processing in the unicellular alga Chlamydomonas reinhardtii.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

8 authors.

Karin van DijkDepartment of Plant Pathology and Plant Science Initiative, University of Nebraska, Lincoln, Nebraska 68588-0666, USA.
Katherine E Marley
Byeong-ryool Jeong
Jianping Xu
Jennifer Hesson
Ronald L Cerny
Jakob H Waterborg
Heriberto Cerutti

Funding

ZINC FINGER-INSPIRED FLUORESCENT CHEMOSENSORSP20RR016469 · NCRR · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI TURPEN, JAMES B · 2001 to 2011
$36.2M
RNA-Mediated Silencing: Mechanisms and Biological Roles in ChlamydomonasR01GM062915 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI CERUTTI, HERIBERTO · 2001 to 2009
$2.0M
NCRR NIH HHS P20 RR016469NIGMS NIH HHS GM62915NIGMS NIH HHS R01 GM062915
6 · The paper itself

Abstract

Histone Lys methylation plays an important role in determining chromatin states and is mostly catalyzed by SET domain-containing proteins. The outcome, transcriptional repression or activation, depends on the methylated histone residue, the degree of methylation, and the chromatin context. Dimethylation or trimethylation of histone H3 Lys 4 (H3K4me2 or H3K4me3) has been correlated with transcriptionally competent/active genes. However, H3K4 methylation has also been implicated in gene silencing. This dualistic nature of the H3K4 methyl mark has thus far remained unresolved. In the green alga Chlamydomonas reinhardtii, Mut11p, related to a subunit of trithorax-like methyltransferase complexes, is required for transcriptional silencing. Here, we show that Mut11p interacts with conserved components of H3K4 methyltransferase machineries, and an affinity-purified Mut11p complex(es) methylates histones H3, H2A, and H4. Moreover, a Mut11 mutant showed global loss of monomethylated H3K4 (H3K4me1) and an increase in dimethylated H3K4. By chromatin immunoprecipitation analysis, this strain also displayed substantial reduction in H3K4me1 and enrichment in H3K4me2 associated with transcriptionally derepressed genes, transgenes, and retrotransposons. RNA interference-mediated suppression of Set1, encoding an H3K4 methyltransferase, induced similar phenotypes, but of lower magnitude, and no detectable increase in H3K4me2. Together, our results suggest functional differentiation between dimethyl H3K4 and monomethyl H3K4, with the latter operating as an epigenetic mark for repressed euchromatin.

Indexed as

Gene SilencingAlgal ProteinsAmino Acid SequenceAnimalsChlamydomonas reinhardtiiEpigenesis, GeneticEuchromatinGene Expression Regulation, PlantHistonesLysineMacromolecular SubstancesMethylationMolecular Sequence DataPhylogenyProtein SubunitsProtozoan ProteinsAlgal ProteinsEuchromatinHistonesLysineMacromolecular SubstancesProtein SubunitsProtozoan Proteins

Identifiers

PMID16100335
PMCPMC1197426

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.