Evidence map›Paper›PMID 15280549›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Rad6-Bre1-mediated histone H2B ubiquitylation modulates the formation of double-strand breaks during meiosis.

Kentaro Yamashita, Miki Shinohara, Akira Shinohara

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

64 citing papers in PubMed, 118 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Deubiquitinases and Cancer.Journal of pharmacy & bioallied sciences · 2024
    Review
  6. Article
  7. Review
  8. Review
  9. RPA-mediated recruitment of Bre1 couples histone H2B ubiquitination to DNA replication and repair.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. SCFLife science alliance · 2021
    Article
  11. Article
  12. The Bre1/Rad6 machinery: writing the central histone ubiquitin mark on H2B and beyond.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2020
    Review
  13. Article
  14. Review
  15. Article
  16. Expanding Role of Ubiquitin in Translational Control.International journal of molecular sciences · 2020
    Review
  17. Article
  18. Gametogenesis: A journey from inception to conception.Current topics in developmental biology · 2019
    Review
  19. Article
  20. Article

4 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Kentaro YamashitaDepartment of Biology, Graduate School of Science, and Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.
Miki Shinohara
Akira Shinohara
Graduate School USA · USJapan Science and Technology Agency · JPOsaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An E2 ubiquitin-conjugating enzyme, Rad6, working with an E3 ubiquitin ligase Bre1, catalyzes monoubiquitylation of histone H2B on a C-terminal lysine residue. The rad6 mutant of Saccharomyces cerevisiae shows a meiotic prophase arrest. Here, we analyzed meiotic defects of a rad6 null mutant of budding yeast. The rad6 mutant exhibits pleiotropic phenotypes during meiosis. RAD6 is required for efficient formation of double-strand breaks (DSBs) at meiotic recombination hotspots, which is catalyzed by Spo11. The mutation decreases overall frequencies of DSBs in a cell. The effect of the rad6 mutation is local along chromosomes; levels of DSBs at stronger hotspots are particularly reduced in the mutant. The absence of RAD6 has little effect on the formation of ectopic DSBs targeted by Spo11 fusion protein with a Gal4 DNA-binding domain. Furthermore, the disruption of the BRE1 as well as substitution of the ubiquitylation site of histone H2B also reduces some DSB formation similar to the rad6. These results suggest that Rad6-Bre1, through ubiquitylation of histone H2B, is necessary for efficient recruitment and/or stabilization of a DSB-forming machinery containing Spo11. Histone tail modifications might play a role in DSB formation during meiosis.

Indexed as

DNA-Binding ProteinsEndodeoxyribonucleasesEsterasesHistonesMeiosisMeiotic Recombination Protein SPO11MitosisMutationRad51 RecombinaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitinUbiquitin-Conjugating EnzymesBre1 protein, S cerevisiaeDNA-Binding ProteinsEndodeoxyribonucleasesEsterasesGAL4 protein, S cerevisiaeHistonesMeiotic Recombination Protein SPO11RAD51 protein, S cerevisiaeRad51 RecombinaseRAD6 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitinUbiquitin-Conjugating Enzymes

Identifiers

PMID15280549
PMCPMC509210
OpenAlexW2080783893

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.