Evidence map›Paper›PMID 29145618›Full record

ArticleNucleic acids research2018

The histone variant H2A.Z promotes initiation of meiotic recombination in fission yeast.

Shintaro Yamada, Kazuto Kugou, Da-Qiao Ding, Yurika Fujita, Yasushi Hiraoka, Hiroshi Murakami, Kunihiro Ohta, Takatomi Yamada

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 33 citations in OpenAlex.

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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

8 authors at 4 institutions in 1 country.

Shintaro YamadaDepartment of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Tokyo 153-8902, Japan.
Kazuto KugouDepartment of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Tokyo 153-8902, Japan.
Da-Qiao DingAdvanced ICT Research Institute Kobe, National Institute of Information and Communications Technology, Kobe 651-2492, Japan.
Yurika FujitaDepartment of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Tokyo 153-8902, Japan.
Yasushi HiraokaAdvanced ICT Research Institute Kobe, National Institute of Information and Communications Technology, Kobe 651-2492, Japan.
Hiroshi MurakamiDepartment of Biological Sciences, Faculty of Science and Engineering, Chuo University, Tokyo 112-8551, Japan.
Kunihiro OhtaDepartment of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Tokyo 153-8902, Japan.
Takatomi YamadaDepartment of Biological Sciences, Faculty of Science and Engineering, Chuo University, Tokyo 112-8551, Japan.
The University of Tokyo · JPChuo University · JPNational Institute of Information and Communications Technology · JPTokyo University of the Arts · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Meiotic recombination is initiated by programmed formation of DNA double strand breaks (DSBs), which are mainly formed at recombination hotspots. Meiotic DSBs require multiple proteins including the conserved protein Spo11 and its cofactors, and are influenced by chromatin structure. For example, local chromatin around hotspots directly impacts DSB formation. Moreover, DSB is proposed to occur in a higher-order chromatin architecture termed 'axis-loop', in which many loops protrude from cohesin-enriched axis. However, still much remains unknown about how meiotic DSBs are generated in chromatin. Here, we show that the conserved histone H2A variant H2A.Z promotes meiotic DSB formation in fission yeast. Detailed investigation revealed that H2A.Z is neither enriched around hotspots nor axis sites, and that transcript levels of DSB-promoting factors were maintained without H2A.Z. Moreover, H2A.Z appeared to be dispensable for chromatin binding of meiotic cohesin. Instead, in H2A.Z-lacking mutants, multiple proteins involved in DSB formation, such as the fission yeast Spo11 homolog and its regulators, were less associated with chromatin. Remarkably, nuclei were more compact in the absence of H2A.Z. Based on these, we propose that fission yeast H2A.Z promotes meiotic DSB formation partly through modulating chromosome architecture to enhance interaction between DSB-related proteins and cohesin-loaded chromatin.

Indexed as

DNA Breaks, Double-StrandedRecombinational DNA RepairChromatinChromosomes, FungalDNA, FungalEndodeoxyribonucleasesHistonesHomologous RecombinationMeiosisMeiotic Recombination Protein SPO11SchizosaccharomycesSchizosaccharomyces pombe ProteinsChromatinDNA, FungalEndodeoxyribonucleasesHistonesMeiotic Recombination Protein SPO11Schizosaccharomyces pombe Proteins

Identifiers

PMID29145618
PMCPMC5778600
OpenAlexW2770354681

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.