Evidence map›Paper›PMID 15928086›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Nucleosome assembly protein-1 is a linker histone chaperone in Xenopus eggs.

Keishi Shintomi, Mari Iwabuchi, Hideaki Saeki, Kiyoe Ura, Takeo Kishimoto, Keita Ohsumi

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. 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, 90 citations in OpenAlex.

  1. Article
  2. Histone Density and Dynamics Shape Mitotic Chromatid Architecture in Xenopus Egg Extracts.Genes to cells : devoted to molecular & cellular mechanisms · 2026
    Article
  3. Article
  4. Histone Nuclear Import and Beyond: Multifunctional Roles of Importins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Histone variants and chromatin structure, update of advances.Computational and structural biotechnology journal · 2023
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  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

6 authors at 2 institutions in 1 country.

Keishi ShintomiLaboratory of Cell and Developmental Biology, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan. kohsumi@bio.titech.ac.jp
Mari Iwabuchi
Hideaki Saeki
Kiyoe Ura
Takeo Kishimoto
Keita Ohsumi
Osaka University · JPTokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotic cells, genomic DNA is primarily packaged into nucleosomes through sequential ordered binding of the core and linker histone proteins. The acidic proteins termed histone chaperones are known to bind to core histones to neutralize their positive charges, thereby facilitating their proper deposition onto DNA to assemble the core of nucleosomes. For linker histones, however, little has been known about the regulatory mechanism for deposition of linker histones onto the linker DNA. Here we report that, in Xenopus eggs, the linker histone is associated with the Xenopus homologue of nucleosome assembly protein-1 (NAP-1), which is known to be a chaperone for the core histones H2A and H2B in Drosophila and mammalian cells [Ito, T., Bulger, M., Kobayashi, R. & Kadonaga, J. T. (1996) Mol. Cell Biol. 16, 3112-3124; Chang, L., Loranger, S. S., Mizzen, C., Ernst, S. G., Allis, C. D. & Annunziato, A. T. (1997) Biochemistry 36, 469-480]. We show that NAP-1 acts as the chaperone for the linker histone in both sperm chromatin remodeling into nucleosomes and linker histone binding to nucleosome core dimers. In the presence of NAP-1, the linker histone is properly deposited onto linker DNA at physiological ionic strength, without formation of nonspecific aggregates. These results strongly suggest that NAP-1 functions as a chaperone for the linker histone in Xenopus eggs.

Indexed as

Amino Acid SequenceAnimalsCell Cycle ProteinsCell ExtractsChromatin Assembly and DisassemblyDrosophila ProteinsFemaleHistonesMaleMolecular ChaperonesMolecular Sequence DataNuclear ProteinsNucleosome Assembly Protein 1NucleosomesOocytesProteinsCell Cycle ProteinsCell ExtractsDrosophila ProteinsHistonesMolecular ChaperonesNap1 protein, DrosophilaNuclear ProteinsNucleosome Assembly Protein 1NucleosomesProteins

Identifiers

PMID15928086
PMCPMC1149419
OpenAlexW2118169279

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.