Evidence map›Paper›PMID 16622709›Full record

ArticleMolecular genetics and genomics : MGG2006

Identification of three histone methyltransferases in Drosophila: dG9a is a suppressor of PEV and is required for gene silencing.

Jacek Mis, Sarbjit S Ner, Thomas A Grigliatti

Abstract read
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In one paragraph

Article in Molecular genetics and genomics : MGG, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Heterochromatin-based silencing of a foreign tandem repeat inbioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. SetDB1 and Su(var)3-9 are essential for late stages of larval development of Drosophila melanogaster.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2023
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  6. Biomedicines · 2022
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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

3 authors at 1 institution in 1 country.

Jacek MisDepartment of Zoology, Life Sciences Institute, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, Canada, V6T 1Z3.
Sarbjit S Ner
Thomas A Grigliatti
University of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Organization of chromatin structure and regulation of gene transcription are contingent on histone tail modifications. Regions of the genome packaged with nucleosomes that contain methyl histone H3 at lysine 9 (Me K9H3) strongly correlate with regions that are silenced for transcription. To date Su(var)3-9 is the only K9H3 specific enzyme characterized in Drosophila melanogaster. In this study, we describe the identification of three additional Drosophila genes that potentially encode K9H3 specific methyltransferases (HMTase) with homology to known mammalian proteins. By several criteria, including sequence alignments, phylogenic analyses, and enzyme activity of the protein, one of these is a homologue of the human G9a and hence, we name it dG9a. dG9a catalyzes the transfer of methyl groups to full-length histone H3 and to N-terminal H3 peptides that contain lysine 9, suggesting that the major target for dG9a is K9H3. Chromatin extracts prepared from a P-element insert mutation in dG9a display an altered K9H3 methylation profile. In addition, the dG9a mutant is a dominant suppressor of position-effect variegation (PEV), a heterochromatin-associated gene silencing phenomenon. Su(var)3-9 also suppresses PEV. The combined Su(var)3-9 and dG9a mutations have severe developmental defects suggesting an overlapping role for dG9a and Su(var)3-9 in the packaging of heterochromatin and gene silencing via a K9H3 methylation pathway.

Indexed as

Gene SilencingAmino Acid SequenceAnimalsBase SequenceBlotting, WesternDNA PrimersDrosophila melanogasterHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHumansMolecular Sequence DataProtein MethyltransferasesSequence Homology, Amino AcidDNA PrimersHistone-Lysine N-MethyltransferaseHistone MethyltransferasesProtein Methyltransferases

Identifiers

PMID16622709
OpenAlexW2086574165

What OpenQuestion holds

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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.