Evidence map›Paper›PMID 12130537›Full record

ArticleGenes & development2002

Fission yeast CENP-B homologs nucleate centromeric heterochromatin by promoting heterochromatin-specific histone tail modifications.

Hiromi Nakagawa, Joon-Kyu Lee, Jerard Hurwitz, Robin C Allshire, Jun-Ichi Nakayama, Shiv I S Grewal, Katsunori Tanaka, Yota Murakami

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
–field-weighted citation impact
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

44 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
  2. Revisiting the question: When is a centromere not a kinetochore?Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Genetic and epigenetic regulation of centromeres: a look at HAC formation.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2015
    Review
  15. Article
  16. Article
  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

8 authors at 4 institutions in 3 countries.

Hiromi NakagawaInstitute for Virus Research, Kyoto University, Kyoto 606-8507, Japan.
Joon-Kyu Lee
Jerard Hurwitz
Robin C Allshire
Jun-Ichi Nakayama
Shiv I S Grewal
Katsunori Tanaka
Yota Murakami
Memorial Sloan Kettering Cancer Center · USCold Spring Harbor Laboratory · USKyoto University · JPWestern General Hospital · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heterochromatin is a functionally important chromosomal component, especially at centromeres. In fission yeast, conserved heterochromatin-specific modifications of the histone H3 tail, involving deacetylation of Lys 9 and Lys 14 and subsequent methylation of Lys 9, promote the recruitment of a heterochromatin protein, Swi6, a homolog of the Drosophila heterochromatin protein 1. However, the primary determinants of the positioning of heterochromatin are still unclear. The fission yeast proteins Abp1, Cbh1, and Cbh2 are homologs of the human protein CENP-B that bind to centromeric alpha-satellite DNA and associate with centromeric heterochromatin. We show that the CENP-B homologs are functionally redundant at centromeres, and that Abp1 binds specifically to centromeric heterochromatin. In the absence of Abp1 or Cbh1, the centromeric association of Swi6 is diminished, resulting in a decrease in silencing of the region. CENP-B-homolog double disruptants show a synergistic reduction of Swi6 at centromeric heterochromatin, indicating that the three proteins are functionally redundant in the recruitment of Swi6. Furthermore, using chromatin immunoprecipitation assays, we show that disruption of CENP-B homologs causes a decrease in heterochromatin-specific modifications of histone H3. These results indicate that the CENP-B homologs act as site-specific nucleation factors for the formation of centromeric heterochromatin by heterochromatin-specific modifications of histone tails.

Indexed as

AutoantigensMicrofilament ProteinsSchizosaccharomyces pombe ProteinsBinding SitesCentromereCentromere Protein BChromosomal Proteins, Non-HistoneDNA-Binding ProteinsFungal ProteinsGene SilencingHeterochromatinHistonesMutagenesisMutagenesis, InsertionalPhenotypeSaccharomyces cerevisiae ProteinsABP1 protein, S cerevisiaeAutoantigensCbh2 protein, S pombeCentromere Protein BChromosomal Proteins, Non-HistoneDNA-Binding ProteinsFungal ProteinsHeterochromatinHistonesMicrofilament ProteinsSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsSWI6 protein, S cerevisiaeTranscription Factorsura4 protein, S pombe

Identifiers

PMID12130537
PMCPMC186399
OpenAlexW2171380099

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.