Evidence map›Paper›PMID 15713643›Full record

ArticleMolecular and cellular biology2005

A motif within SET-domain proteins binds single-stranded nucleic acids and transcribed and supercoiled DNAs and can interfere with assembly of nucleosomes.

Wladyslaw A Krajewski, Tatsuya Nakamura, Alexander Mazo, Eli Canaani

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

47 citing papers in PubMed, 75 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. PRC2 is high maintenance.Genes & development · 2019
    Review
  6. Article
  7. Article
  8. Transcription-associated events affecting genomic integrity.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  9. Ctf4-related protein recruits LHP1-PRC2 to maintain H3K27me3 levels in dividing cells inProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Cell discovery · 2017
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. R-loop: an emerging regulator of chromatin dynamics.Acta biochimica et biophysica Sinica · 2016
    Review
  16. Review
  17. Structural analysis of an active fungal PRC2.Nucleus (Austin, Tex.) · 2016
    Article
  18. Article
  19. Article
  20. 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

4 authors at 2 institutions in 3 countries.

Wladyslaw A KrajewskiDepartment of Biochemistry, Institute of Developmental Biology, Russian Academy of Sciences, Vavilova Str. 26, 117808 Moscow, Russia. wkrajewski@hotmail.com
Tatsuya Nakamura
Alexander Mazo
Eli Canaani
Thomas Jefferson University · USWeizmann Institute of Science · IL

Funding

THE MURINE ALL-1 GENE--TUMORIGENESIS AND DEVELOPMENTP01CA050507 · NCI · THOMAS JEFFERSON UNIVERSITY · PI CROCE, CARLO M · 1994 to 2004
$5.6M
NCI NIH HHS CA50507NCI NIH HHS P01 CA050507
6 · The paper itself

Abstract

The evolutionary conserved SET domain is present in many eukaryotic chromatin-associated proteins, including some members of the trithorax (TrxG) group and the polycomb (PcG) group of epigenetic transcriptional regulators and modifiers of position effect variegation. All SET domains examined exhibited histone lysine methyltransferase activity, implicating these proteins in the generation of epigenetic marks. However, the mode of the initial recruitment of SET proteins to target genes and the way that their association with the genes is maintained after replication are not known. We found that SET-containing proteins of the SET1 and SET2 families contain motifs in the pre-SET region or at the pre-SET-SET and SET-post-SET boundaries which very tightly bind single-stranded DNA (ssDNA) and RNA. These motifs also bind stretches of ssDNA generated by superhelical tension or during the in vitro transcription of duplex DNA. Importantly, such binding withstands nucleosome assembly, interfering with the formation of regular nucleosomal arrays. Two representatives of the SUV39 SET family, SU(VAR)3-9 and G9a, did not bind ssDNA. The trxZ11 homeotic point mutation, which is located within TRX SET and disrupts embryonic development, impairs the ssDNA binding capacity of the protein. We suggest that the motifs described here may be directly involved in the biological function(s) of SET-containing proteins. The binding of single-stranded nucleic acids might play a role in the initial recruitment of the proteins to target genes, in the maintenance of their association after DNA replication, or in sustaining DNA stretches in a single-stranded configuration to allow for continuous transcription.

Indexed as

Amino Acid MotifsAnimalsChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDNA, Single-StrandedDNA, SuperhelicalEscherichia coli ProteinsHumansMutationNucleosomesPeptidesProtein Structure, TertiaryRNATranscription FactorsTranscription, GeneticChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDNA, Single-StrandedDNA, SuperhelicalEscherichia coli ProteinsNucleosomesPeptidesRNASSB protein, E coliTranscription Factors

Identifiers

PMID15713643
PMCPMC549386
OpenAlexW2127414497

What OpenQuestion holds

Textmetadata
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.