Evidence map›Paper›PMID 10436015›Full record

ArticleMolecular biology of the cell1999

The nuclear actin-related protein of Saccharomyces cerevisiae, Act3p/Arp4, interacts with core histones.

M Harata, Y Oma, S Mizuno, Y W Jiang, D J Stillman, U Wintersberger

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed, 119 citations in OpenAlex.

  1. Envisioning a role for nuclear actin in prophase I spermatocytes.Frontiers in cell and developmental biology · 2023
    Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Nuclear Actin: From Discovery to Function.Anatomical record (Hoboken, N.J. : 2007) · 2018
    Review
  10. Article
  11. Review
  12. Genome maintenance functions of the INO80 chromatin remodeller.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
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  19. Multiple modes of regulation of the human Ino80 SNF2 ATPase by subunits of the INO80 chromatin-remodeling complex.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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 4 institutions in 3 countries.

M HarataLaboratory of Molecular Biology, Department of Molecular and Cell Biology, Division of Life Science, Graduate School of Agricultural Science, Tohoku University, Sendai 981-8555, Japan. mharata@biochem.tohoku.ac.jp
Y Oma
S Mizuno
Y W Jiang
D J Stillman
U Wintersberger
Tohoku University · JPHuntsman Cancer Institute · USUniversity of Utah · USUniversity of Vienna · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Act3p/Arp4, an essential actin-related protein of Saccharomyces cerevisiae located within the nucleus, is, according to genetic data, involved in transcriptional regulation. In addition to the basal core structure of the actin family members, which is responsible for ATPase activity, Act3p possesses two insertions, insertions I and II, the latter of which is predicted to form a loop-like structure protruding from beyond the surface of the molecule. Because Act3p is a constituent of chromatin but itself does not bind to DNA, we hypothesized that insertion II might be responsible for an Act3p-specific function through its interaction with some other chromatin protein. Far Western blot and two-hybrid analyses revealed the ability of insertion II to bind to each of the core histones, although with somewhat different affinities. Together with our finding of coimmunoprecipitation of Act3p with histone H2A, this suggests the in vivo existence of a protein complex required for correct expression of particular genes. We also show that a conditional act3 mutation affects chromatin structure of an episomal DNA molecule, indicating that the putative Act3p complex may be involved in the establishment, remodeling, or maintenance of chromatin structures.

Indexed as

Saccharomyces cerevisiae ProteinsActinsBlotting, WesternChromatinHistonesHybrid CellsMutationNuclear ProteinsSaccharomyces cerevisiaeActinsArp4 protein, S cerevisiaeChromatinHistonesNuclear ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID10436015
PMCPMC25491
OpenAlexW2171857613

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.