Evidence map›Paper›PMID 22095079›Full record

ArticleGenetics2012

The double-bromodomain proteins Bdf1 and Bdf2 modulate chromatin structure to regulate S-phase stress response in Schizosaccharomyces pombe.

Mikael V Garabedian, Chiaki Noguchi, Melissa A Ziegler, Mukund M Das, Tanu Singh, Logan J Harper, Adam R Leman, Lyne Khair, Bettina A Moser, Toru M Nakamura and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

23 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  5. A meiotic driver hijacks an epigenetic reader to disrupt mitosis in noncarrier offspring.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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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

11 authors at 2 institutions in 1 country.

Mikael V GarabedianDepartment of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania 19102, USA.
Chiaki Noguchi
Melissa A Ziegler
Mukund M Das
Tanu Singh
Logan J Harper
Adam R Leman
Lyne Khair
Bettina A Moser
Toru M Nakamura
Eishi Noguchi
Drexel University · USUniversity of Illinois Chicago · US

Funding

Studies of the Swi1-Swi3 Replication Fork Protection ComplexR01GM077604 · NIGMS · DREXEL UNIVERSITY · PI NOGUCHI, EISHI · 2008 to 2012
$1.6M
NIGMS NIH HHS GM077604NIGMS NIH HHS R01 GM077604NIGMS NIH HHS R01GM077604-S1
6 · The paper itself

Abstract

Bromodomain proteins bind acetylated histones to regulate transcription. Emerging evidence suggests that histone acetylation plays an important role in DNA replication and repair, although its precise mechanisms are not well understood. Here we report studies of two double bromodomain-containing proteins, Bdf1 and Bdf2, in fission yeast. Loss of Bdf1 or Bdf2 led to a reduction in the level of histone H4 acetylation. Both bdf1Δ and bdf2Δ cells showed sensitivity to DNA damaging agents, including camptothecin, that cause replication fork breakage. Consistently, Bdf1 and Bdf2 were important for recovery of broken replication forks and suppression of DNA damage. Surprisingly, deletion of bdf1 or bdf2 partially suppressed sensitivity of various checkpoint mutants including swi1Δ, mrc1Δ, cds1Δ, crb2Δ, chk1Δ, and rad3Δ, to hydroxyurea, a compound that stalls replication forks and activates the Cds1-dependent S-phase checkpoint. This suppression was not due to reactivation of Cds1. Instead, we found that bdf2 deletion alleviates DNA damage accumulation caused by defects in the DNA replication checkpoint. We also show that hydroxyurea sensitivity of mrc1Δ and swi1Δ was suppressed by mutations in histone H4 acetyltransferase subunits or histone H4. These results suggest that the double bromodomain-containing proteins modulate chromatin structure to coordinate DNA replication and S-phase stress response.

Indexed as

AcetylationCell Cycle CheckpointsCell Cycle ProteinsCheckpoint Kinase 2ChromatinChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDNA DamageDNA ReplicationGene DeletionHistonesHydroxyureaMutationProtein Serine-Threonine KinasesSchizosaccharomycesSchizosaccharomyces pombe ProteinsBdf1 protein, S pombeCds1 protein, S pombeCell Cycle ProteinsCheckpoint Kinase 2ChromatinChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHistonesHydroxyureaMRC1 protein, S pombeProtein Serine-Threonine KinasesSchizosaccharomyces pombe Proteinsswi1 protein, S pombe

Identifiers

PMID22095079
PMCPMC3276636
OpenAlexW2154032810

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.