Evidence map›Paper›PMID 15781691›Full record

ArticleGenetics2005

Saccharomyces cerevisiae histone H2A Ser122 facilitates DNA repair.

Anne C Harvey, Stephen P Jackson, Jessica A Downs

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

20 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Article
  3. Histone Phosphorylation in DNA Damage Response.International journal of molecular sciences · 2025
    Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Distinct roles foreLife · 2019
    Article
  11. Protein phosphatases in chromatin structure and function.Biochimica et biophysica acta. Molecular cell research · 2019
    Review
  12. Article
  13. Comprehensive Catalog of Currently Documented Histone Modifications.Cold Spring Harbor perspectives in biology · 2015
    Review
  14. Review
  15. Article
  16. Review
  17. 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

3 authors at 2 institutions in 1 country.

Anne C HarveyDepartment of Biochemistry, University of Cambridge, UK.
Stephen P Jackson
Jessica A Downs
University of Cambridge · GBWellcome/Cancer Research UK Gurdon Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA repair takes place in the context of chromatin. Recently, it has become apparent that proteins that make up and modulate chromatin structure are involved in the detection and repair of DNA lesions. We previously demonstrated that Ser129 in the carboxyl-terminal tail of yeast histone H2A is important for double-strand-break responses. By undertaking a systematic site-directed mutagenesis approach, we identified another histone H2A serine residue (Ser122) that is important for survival in the presence of DNA-damaging agents. We show that mutation of this residue does not affect DNA damage-dependent Rad53 phosphorylation or G(2)/M checkpoint responses. Interestingly, we find that yeast lacking H2A S122 are defective in their ability to sporulate. Finally, we demonstrate that H2A S122 provides a function distinct from that of H2A S129. These data demonstrate a role for H2A S122 in facilitating survival in the presence of DNA damage and suggest a potential role in mediating homologous recombination. The distinct roles of H2A S122 and S129 in mediating these responses suggest that chromatin components can provide specialized functions for distinct DNA repair and survival mechanisms and point toward the possibility of a complex DNA damage responsive histone code.

Indexed as

DNA RepairAmino Acid SequenceBlotting, WesternCell Cycle ProteinsCell DivisionCheckpoint Kinase 2ChromatinChromatin ImmunoprecipitationG2 PhaseHistonesMicrococcal NucleaseMolecular Sequence DataMutationPhosphorylationProtein Serine-Threonine KinasesProtein Structure, TertiaryCell Cycle ProteinsCheckpoint Kinase 2ChromatinHistonesMicrococcal NucleaseProtein Serine-Threonine KinasesRAD53 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSerine

Identifiers

PMID15781691
PMCPMC1450416
OpenAlexW2161675968

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.