Evidence map›Paper›PMID 27615797›Full record

ArticleScientific reports2016

Novel O-GlcNAcylation on Ser(40) of canonical H2A isoforms specific to viviparity.

Mitsuko Hirosawa, Koji Hayakawa, Chikako Yoneda, Daisuke Arai, Hitoshi Shiota, Takehiro Suzuki, Satoshi Tanaka, Naoshi Dohmae, Kunio Shiota

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. ProteinFrontiers in endocrinology · 2022
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  7. Review
  8. Advances in chemical probing of proteinChemical Society reviews · 2021
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  9. Article
  10. Role ofPhysiological reviews · 2021
    Review
  11. Review
  12. Article
  13. Review
  14. Frontiers in genetics · 2020
    Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. 'Molecules (Basel, Switzerland) · 2018
    Review
  20. Article
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

9 authors at 3 institutions in 1 country.

Mitsuko HirosawaLaboratory of Cellular Biochemistry, Department of Animal Resource Sciences/Veterinary Medical Sciences, The University of Tokyo, Tokyo 113-8657, JAPAN.
Koji HayakawaLaboratory of Cellular Biochemistry, Department of Animal Resource Sciences/Veterinary Medical Sciences, The University of Tokyo, Tokyo 113-8657, JAPAN.
Chikako YonedaLaboratory of Cellular Biochemistry, Department of Animal Resource Sciences/Veterinary Medical Sciences, The University of Tokyo, Tokyo 113-8657, JAPAN.
Daisuke AraiWaseda Research Institute for Science and Engineering, Waseda University Tokyo 169-8555, JAPAN.
Hitoshi ShiotaLaboratory of Cellular Biochemistry, Department of Animal Resource Sciences/Veterinary Medical Sciences, The University of Tokyo, Tokyo 113-8657, JAPAN.
Takehiro SuzukiBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Saitama 351-0198, JAPAN.
Satoshi TanakaLaboratory of Cellular Biochemistry, Department of Animal Resource Sciences/Veterinary Medical Sciences, The University of Tokyo, Tokyo 113-8657, JAPAN.
Naoshi DohmaeBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Saitama 351-0198, JAPAN.
Kunio ShiotaLaboratory of Cellular Biochemistry, Department of Animal Resource Sciences/Veterinary Medical Sciences, The University of Tokyo, Tokyo 113-8657, JAPAN.
The University of Tokyo · JPRIKEN Center for Sustainable Resource Science · JPWaseda University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We report here newly discovered O-linked-N-acetylglucosamine (O-GlcNAc) modification of histone H2A at Ser(40) (H2AS40Gc). The mouse genome contains 18 H2A isoforms, of which 13 have Ser(40) and the other five have Ala(40). The combination of production of monoclonal antibody and mass spectrometric analyses with reverse-phase (RP)-high performance liquid chromatography (HPLC) fractionation indicated that the O-GlcNAcylation is specific to the Ser(40) isoforms. The H2AS40Gc site is in the L1 loop structure where two H2A molecules interact in the nucleosome. Targets of H2AS40Gc are distributed genome-wide and are dramatically changed during the process of differentiation in mouse trophoblast stem cells. In addition to the mouse, H2AS40Gc was also detected in humans, macaques and cows, whereas non-mammalian species possessing only the Ala(40) isoforms, such as silkworms, zebrafish and Xenopus showed no signal. Genome database surveys revealed that Ser(40) isoforms of H2A emerged in Marsupialia and persisted thereafter in mammals. We propose that the emergence of H2A Ser(40) and its O-GlcNAcylation linked a genetic event to genome-wide epigenetic events that correlate with the evolution of placental animals.

Indexed as

Biological EvolutionAcetylglucosamineAnimalsAntibodies, MonoclonalBinding SitesBombyxCattleChromatography, High Pressure LiquidEmbryonic Stem CellsHeLa CellsHistonesHumansMacacaMass SpectrometryMiceMice, Inbred C57BLAcetylglucosamineAntibodies, MonoclonalHistonesProtein IsoformsRecombinant ProteinsSerine

Identifiers

PMID27615797
PMCPMC5018834
OpenAlexW2520069674

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.