Evidence map›Paper›PMID 22693636›Full record

ArticlePloS one2012

Med5(Nut1) and Med17(Srb4) are direct targets of mediator histone H4 tail interactions.

Zhongle Liu, Lawrence C Myers

Abstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Cells · 2022
    Review
  2. Article
  3. Article
  4. Article
  5. Transcription regulation by the Mediator complex.Nature reviews. Molecular cell biology · 2018
    Review
  6. Review
  7. Article
  8. Chromatin potentiates transcription.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Mechanisms of Mediator complex action in transcriptional activation.Cellular and molecular life sciences : CMLS · 2013
    Review
  18. The Mediator complex and transcription elongation.Biochimica et biophysica acta · 2013
    Review
  19. The Mediator complex and transcription regulation.Critical reviews in biochemistry and molecular biology
    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

2 authors.

Zhongle LiuDepartment of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire, United States of America.
Lawrence C Myers

Funding

The Role of Yeast Mediator in Transcriptional RegulationR01GM062483 · NIGMS · DARTMOUTH COLLEGE · PI MYERS, LAWRENCE CHRISTOPHER · 2001 to 2012
$2.5M
NIGMS NIH HHS R01 GM062483NIGMS NIH HHS R01 GM62483
6 · The paper itself

Abstract

The Mediator complex transmits activation signals from DNA bound transcription factors to the core transcription machinery. In addition to its canonical role in transcriptional activation, recent studies have demonstrated that S. cerevisiae Mediator can interact directly with nucleosomes, and their histone tails. Mutations in Mediator subunits have shown that Mediator and certain chromatin structures mutually impact each other structurally and functionally in vivo. We have taken a UV photo cross-linking approach to further delineate the molecular basis of Mediator chromatin interactions and help determine whether the impact of certain Mediator mutants on chromatin is direct. Specifically, by using histone tail peptides substituted with an amino acid analog that is a UV activatible crosslinker, we have identified specific subunits within Mediator that participate in histone tail interactions. Using Mediator purified from mutant yeast strains we have evaluated the impact of these subunits on histone tail binding. This analysis has identified the Med5 subunit of Mediator as a target for histone tail interactions and suggests that the previously observed effect of med5 mutations on telomeric heterochromatin and silencing is direct.

Indexed as

HeterochromatinHistonesMediator ComplexNucleosomesProtein BindingSaccharomyces cerevisiae ProteinsHeterochromatinHistonesMediator ComplexNucleosomesNUT1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSRB4 protein, S cerevisiae

Identifiers

PMID22693636
PMCPMC3367926

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.