Evidence map›Paper›PMID 23816883›Full record

ArticleMolecular and cellular biology2013

Histone variant H2A.Z functions in sister chromatid cohesion in Saccharomyces cerevisiae.

Upasna Sharma, Dessislava Stefanova, Scott G Holmes

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 30 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Histone dynamics during DNA replication stress.Journal of biomedical science · 2021
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Point centromere activity requires an optimal level of centromeric noncoding RNA.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Article
  15. Review
  16. Binding, sliding, and function of cohesin during transcriptional activation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Determinants of Sir2-Mediated, Silent Chromatin Cohesion.Molecular and cellular biology · 2016
    Article
  18. Review
  19. Review
  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

3 authors at 1 institution in 1 country.

Upasna SharmaDepartment of Molecular Biology and Biochemistry, Wesleyan University, Middletown, Connecticut, USA.
Dessislava Stefanova
Scott G Holmes
Wesleyan University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

H2A.Z is a highly conserved variant of histone H2A with well-characterized roles in transcriptional regulation. We previously reported that H2A.Z and Mcd1, a subunit of the cohesin complex, regulate the establishment of transcriptional silencing at telomeres in Saccharomyces cerevisiae and that H2A.Z broadly dissociated from chromatin during the anaphase-to-telophase transition, coincident with the dissociation of Mcd1 from chromosomes and dissolution of cohesion. In this study, we show that depletion of H2A.Z causes precocious loss of sister chromatid cohesion in yeast without loss of Mcd1 from chromosomes. H2A.Z is deposited into chromatin by the SWR1 complex and is subject to acetylation of its four N-terminal tail lysine residues by the NuA4 and SAGA histone acetyltransferase complexes. We found that cells compromised for function of the SWR1 complex were defective in cohesion, as were cells expressing a form of H2A.Z not subject to acetylation. Finally, inactivation of H2A.Z in metaphase-blocked cells led immediately to cohesion defects, suggesting a direct role for H2A.Z in the maintenance of sister chromatid cohesion.

Indexed as

AcetylationAdenosine TriphosphatasesCell Cycle ProteinsChromatidsChromosomal Proteins, Non-HistoneGene DeletionHistone AcetyltransferasesHistonesMutationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesCell Cycle ProteinsChromosomal Proteins, Non-HistoneHistone AcetyltransferasesHistonesMCD1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSwr1 protein, S cerevisiae

Identifiers

PMID23816883
PMCPMC3753853
OpenAlexW2166081348

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.