Evidence map›Paper›PMID 17889663›Full record

ArticleMolecular cell2007

Sir2 deacetylates histone H3 lysine 56 to regulate telomeric heterochromatin structure in yeast.

Feng Xu, Qiongyi Zhang, Kangling Zhang, Wei Xie, Michael Grunstein

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
28.0field-weighted citation impact, top 1% 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

111 citing papers in PubMed, 159 citations in OpenAlex.

  1. Article
  2. Review
  3. The star target in SLE: IL-17.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2023
    Review
  4. Telomere maintenance in African trypanosomes.Frontiers in molecular biosciences · 2023
    Review
  5. Article
  6. Article
  7. Article
  8. The Roles of Chromatin Accessibility in Regulating theJournal of fungi (Basel, Switzerland) · 2021
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

51 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 1 country.

Feng XuDepartment of Biological Chemistry, Geffen School of Medicine at UCLA, and the Molecular Biology Institute, Boyer Hall, 611 Young Drive East, Los Angeles, CA 90095, USA.
Qiongyi Zhang
Kangling Zhang
Wei Xie
Michael Grunstein
University of California, Los Angeles · USLoma Linda University · US

Funding

CHROMOSOMAL REPRESSION OF YEAST HETEROCHROMATINR01GM042421 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI GRUNSTEIN, MICHAEL · 1989 to 2010
$4.4M
NIGMS NIH HHS GM42421NIGMS NIH HHS R01 GM042421
6 · The paper itself

Abstract

At telomeric heterochromatin in yeast, the Sir protein complex spreads from Rap1 sites to silence adjacent genes. This cascade is believed to occur when Sir2, an NAD(+)-dependent enzyme, deacetylates histone H3 and H4 N termini, in particular histone H4 K16, enabling more Sir protein binding. Lysine 56 of histone H3 is located at the entry-exit points of the DNA superhelix surrounding the nucleosome, where it may control DNA compaction. We have found that K56 substitutions disrupt silencing severely without decreasing Sir protein binding at the telomere. Our in vitro and in vivo data indicate that Sir2 deacetylates K56 directly in telomeric heterochromatin to compact chromatin and prevent access to RNA polymerase and ectopic bacterial dam methylase. Since the spread of Sir proteins is necessary but not sufficient for silencing, we propose that silencing occurs when Sir2 deacetylates H3 K56 to close the nucleosomal entry-exit gates, enabling compaction of heterochromatin.

Indexed as

AcetylationAmino Acid SubstitutionGenes, FungalHeterochromatinHistone DeacetylasesHistonesLysineMutationProtein BindingSaccharomyces cerevisiaeSilent Information Regulator Proteins, Saccharomyces cerevisiaeSirtuin 2SirtuinsSite-Specific DNA-Methyltransferase (Adenine-Specific)TelomereDam methyltransferaseHeterochromatinHistone DeacetylasesHistonesLysineSilent Information Regulator Proteins, Saccharomyces cerevisiaeSIR2 protein, S cerevisiaeSirtuin 2SirtuinsSite-Specific DNA-Methyltransferase (Adenine-Specific)

Identifiers

PMID17889663
PMCPMC2048486
OpenAlexW1981483360

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.