Evidence map›Paper›PMID 19822661›Full record

ArticleMolecular and cellular biology2009

Set2-dependent K36 methylation is regulated by novel intratail interactions within H3.

James N Psathas, Suting Zheng, Song Tan, Joseph C Reese

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Histone proteolysis: a proposal for categorization into 'clipping' and 'degradation'.BioEssays : news and reviews in molecular, cellular and developmental biology · 2015
    Review
  7. Article
  8. Article
  9. Article
  10. Understanding the language of Lys36 methylation at histone H3.Nature reviews. Molecular cell biology · 2012
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

4 authors at 1 institution in 1 country.

James N PsathasDepartment of Biochemistry and Molecular Biology, Penn State University, University Park, PA 16802, USA.
Suting Zheng
Song Tan
Joseph C Reese
Pennsylvania State University · US

Funding

REGULATION OF DNA DAMAGE INDUCED GENES BY YEAST TAFIISR01GM058672 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI REESE, JOSEPH C · 1999 to 2019
$6.5M
STRUCTURE AND FUNCTION OF GENE REGULATORY COMPLEXESR01GM060489 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI TAN, SONG · 2000 to 2010
$2.4M
NIGMS NIH HHS GM58627NIGMS NIH HHS R01 GM058672NIGMS NIH HHS R01 GM060489
6 · The paper itself

Abstract

Posttranslational modifications to histones have been studied extensively, but the requirement for the residues within the tails for different stages of transcription is less clear. Using RNR3 as a model, we found that the residues within the N terminus of H3 are predominantly required for steps after transcription initiation and chromatin remodeling. Specifically, deleting as few as 20 amino acids, or substituting glutamines for lysines in the tail, greatly impaired K36 methylation by Set2. The mutations to the tail described here preserve the residues predicted to fill the active site of Set2, and the deletion mimics the recently described cleavage of the H3 tail that occurs during gene activation. Importantly, maintaining the charge of the unmodified tail by arginine substitutions preserves Set2 function in vivo. The H3 tail is dispensable for Set2 recruitment to genes but is required for the catalytic activity of Set2 in vitro. We propose that Set2 activity is controlled by novel intratail interactions which can be influenced by modifications and changes to the structure of the H3 tail to control the dynamics and localization of methylation during elongation.

Indexed as

HistonesAmino Acid SequenceGene Expression Regulation, FungalLysineMethylationMethyltransferasesMolecular Sequence DataMutationOpen Reading FramesPhenotypeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription, GeneticHistonesLysineMethyltransferasesSaccharomyces cerevisiae ProteinsSet2 protein, S cerevisiae

Identifiers

PMID19822661
PMCPMC2786872
OpenAlexW2142005850

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.