Evidence map›Paper›PMID 24336483›Full record

ArticleScientific reports2013

Structural basis of a nucleosome containing histone H2A.B/H2A.Bbd that transiently associates with reorganized chromatin.

Yasuhiro Arimura, Hiroshi Kimura, Takashi Oda, Koichi Sato, Akihisa Osakabe, Hiroaki Tachiwana, Yuko Sato, Yasuha Kinugasa, Tsuyoshi Ikura, Masaaki Sugiyama and 2 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.1field-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

41 citing papers in PubMed, 72 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 1 country.

Yasuhiro ArimuraLaboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, 2-2 wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan.
Hiroshi Kimura1] Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan [2] JST, CREST, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Takashi OdaGraduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
Koichi SatoLaboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, 2-2 wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan.
Akihisa OsakabeLaboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, 2-2 wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan.
Hiroaki TachiwanaLaboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, 2-2 wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan.
Yuko Sato1] Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan [2] JST, CREST, 1-3 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Yasuha KinugasaGraduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan.
Tsuyoshi IkuraDepartment of Mutagenesis, Division of Chromatin Regulatory Network, Radiation Biology Center, Kyoto University, Yoshidakonoe, Sakyo-ku, Kyoto 606-8501, Japan.
Masaaki SugiyamaResearch Reactor Institute, Kyoto University, Kumatori, Osaka, 590-0494, Japan.
Mamoru Sato1] Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan [2] RIKEN SPring-8 Center, 1-1-1 koto, Sayo, Hyogo 679-5148, Japan.
Hitoshi KurumizakaLaboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, 2-2 wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan.
Kyoto University Research Reactor Institute · JPOsaka University · JPYokohama City University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human histone H2A.B (formerly H2A.Bbd), a non-allelic H2A variant, exchanges rapidly as compared to canonical H2A, and preferentially associates with actively transcribed genes. We found that H2A.B transiently accumulated at DNA replication and repair foci in living cells. To explore the biochemical function of H2A.B, we performed nucleosome reconstitution analyses using various lengths of DNA. Two types of H2A.B nucleosomes, octasome and hexasome, were formed with 116, 124, or 130 base pairs (bp) of DNA, and only the octasome was formed with 136 or 146 bp DNA. In contrast, only hexasome formation was observed by canonical H2A with 116 or 124 bp DNA. A small-angle X-ray scattering analysis revealed that the H2A.B octasome is more extended, due to the flexible detachment of the DNA regions at the entry/exit sites from the histone surface. These results suggested that H2A.B rapidly and transiently forms nucleosomes with short DNA segments during chromatin reorganization.

Indexed as

Cell CycleCell LineChromatinChromatin Assembly and DisassemblyDNADNA RepairDNA ReplicationGene ExpressionGenes, ReporterHistonesHumansModels, MolecularNucleosomesProtein BindingProtein ConformationProtein TransportChromatinDNAHistonesNucleosomesSolutions

Identifiers

PMID24336483
PMCPMC3863819
OpenAlexW2110550015

What OpenQuestion holds

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LicenceCC BY
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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.