Evidence map›Paper›PMID 20048053›Full record

ArticleMolecular and cellular biology2010

Asf1 can promote trimethylation of H3 K36 by Set2.

Ling-Ju Lin, Laura V Minard, Gerald C Johnston, Richard A Singer, Michael C Schultz

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. The determinants of alternative RNA splicing in human cells.Molecular genetics and genomics : MGG · 2017
    Review
  8. Shaping the cellular landscape with Set2/SETD2 methylation.Cellular and molecular life sciences : CMLS · 2017
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Understanding the language of Lys36 methylation at histone H3.Nature reviews. Molecular cell biology · 2012
    Review
  17. Promoter regulation by distinct mechanisms of functional interplay between lysine acetylase Rtt109 and histone chaperone Asf1.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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

5 authors at 2 institutions in 1 country.

Ling-Ju LinDepartment of Biochemistry, University of Alberta, MSB 5-76, Edmonton, Alberta, Canada T6G 2H7.
Laura V Minard
Gerald C Johnston
Richard A Singer
Michael C Schultz
University of Alberta · CADalhousie University · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Asf1 is a conserved histone H3/H4 chaperone that can assemble and disassemble nucleosomes and promote histone acetylation. Set2 is an H3 K36 methyltransferase. The functions of these proteins intersect in the context of transcription elongation by RNA polymerase II: both contribute to the establishment of repressive chromatin structures that inhibit spurious intragenic transcription. Here we characterize further interactions between budding yeast (Saccharomyces cerevisiae) Asf1 and Set2 using assays of intragenic transcription, H3/H4 posttranslational modification, coding region cross-linking of Asf1 and Set2, and cooccurrence of Asf1 and Set2 in protein complexes. We find that at some genes Asf1 and Set2 control chromatin metabolism as components of separate pathways. However, the existence of a low-abundance complex containing both proteins suggests that Asf1 and Set2 can more directly collaborate in chromatin regulation. Consistent with this possibility, we show that Asf1 stimulates Set2 occupancy of the coding region of a highly transcribed gene by a mechanism that depends on Asf1 binding to H3/H4. This function of Asf1 promotes the switch from di- to trimethylation of H3 K36 at that gene. These results support the view that Set2 function in chromatin metabolism can intimately involve histone chaperone Asf1.

Indexed as

Cell CycleCell Cycle ProteinsChromatinDNA DamageDNA, FungalGene DeletionGene Regulatory NetworksGenes, FungalHistonesMethylationMethyltransferasesModels, BiologicalMolecular ChaperonesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription, GeneticASF1 protein, S cerevisiaeCell Cycle ProteinsChromatinDNA, FungalHistonesMethyltransferasesMolecular ChaperonesSaccharomyces cerevisiae ProteinsSet2 protein, S cerevisiae

Identifiers

PMID20048053
PMCPMC2820888
OpenAlexW2168346118

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.