ArticleGenetics2007
Diverse roles for histone H2A modifications in DNA damage response pathways in yeast.
Article in Genetics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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.
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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.
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Who cites it
25 citing papers in PubMed, 61 citations in OpenAlex.
- Histone Phosphorylation in DNA Damage Response.International journal of molecular sciences · 2025Review
- Senescence: Pathogenic Driver in Chronic Obstructive Pulmonary Disease.Medicina (Kaunas, Lithuania) · 2022Review
- Epigenetic Regulation of Nucleotide Excision Repair.Frontiers in cell and developmental biology · 2022Review
- Article
- Mitochondrial Function Are Disturbed in the Presence of the Anticancer Drug, 3-Bromopyruvate.International journal of molecular sciences · 2021Article
- Modified chromosome structure caused by phosphomimetic H2A modulates the DNA damage response by increasing chromatin mobility in yeast.Journal of cell science · 2021Article
- Effects of Simulated Microgravity on the Proteome and Secretome of the Polyextremotolerant Black FungusFrontiers in genetics · 2021Article
- Article
- Histone H2A isoforms: Potential implications in epigenome plasticity and diseases in eukaryotes.Journal of biosciences · 2020Review
- Distinct roles foreLife · 2019Article
- Choose Your Own Adventure: The Role of Histone Modifications in Yeast Cell Fate.Journal of molecular biology · 2017Review
- Article
- Histone phosphorylation: a chromatin modification involved in diverse nuclear events.Epigenetics · 2012Review
- Implication of posttranslational histone modifications in nucleotide excision repair.International journal of molecular sciences · 2012Review
- Structure of C-terminal tandem BRCT repeats of Rtt107 protein reveals critical role in interaction with phosphorylated histone H2A during DNA damage repair.The Journal of biological chemistry · 2012Article
- Regulation of budding yeast mating-type switching donor preference by the FHA domain of Fkh1.PLoS genetics · 2012Article
- Key functional regions in the histone variant H2A.Z C-terminal docking domain.Molecular and cellular biology · 2011Article
- Functional relevance of the histone gammaH2Ax in the response to DNA damaging agents.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- H2AX post-translational modifications in the ionizing radiation response and homologous recombination.Cell cycle (Georgetown, Tex.) · 2010Article
- Phosphorylation of histone H2A.X by DNA-dependent protein kinase is not affected by core histone acetylation, but it alters nucleosome stability and histone H1 binding.The Journal of biological chemistry · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
There are many types of DNA damage that are repaired by a multiplicity of different repair pathways. All damage and repair occur in the context of chromatin, and histone modifications are involved in many repair processes. We have analyzed the roles of H2A and its modifications in repair by mutagenizing modifiable residues in the N- and C-terminal tails of yeast H2A and by testing strains containing these mutations in multiple DNA repair assays. We show that residues in both tails are important for homologous recombination and nonhomologous end-joining pathways of double-strand break repair, as well as for survival of UV irradiation and oxidative damage. We show that H2A serine 122 is important for repair and/or survival in each of these assays. We also observe a complex pattern of H2A phosphorylation at residues S122, T126, and S129 in response to different damage conditions. We find that overlapping but nonidentical groups of H2A residues in both tails are involved in different pathways of repair. These data suggest the presence of a set of H2A "damage codes" in which distinct patterns of modifications on both tails of H2A may be used to identify specific types of damage or to promote specific repair pathways.
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Registered trials
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.