Evidence map›Paper›PMID 25163529›Full record

ArticleNature communications2014

Solution-state conformation and stoichiometry of yeast Sir3 heterochromatin fibres.

Sarah G Swygert, Benjamin J Manning, Subhadip Senapati, Parminder Kaur, Stuart Lindsay, Borries Demeler, Craig L Peterson

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. SIR proteins create compact heterochromatin fibers.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Direct interactions promote eviction of the Sir3 heterochromatin protein by the SWI/SNF chromatin remodeling enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

7 authors at 3 institutions in 1 country.

Sarah G SwygertProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, Massachusetts 01605, USA.
Benjamin J ManningProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, Massachusetts 01605, USA.
Subhadip SenapatiCenter for Single Molecule Biophysics, Biodesign Institute, Arizona State University, PO Box 875001, Tempe, Arizona 85287, USA.
Parminder KaurCenter for Single Molecule Biophysics, Biodesign Institute, Arizona State University, PO Box 875001, Tempe, Arizona 85287, USA.
Stuart LindsayCenter for Single Molecule Biophysics, Biodesign Institute, Arizona State University, PO Box 875001, Tempe, Arizona 85287, USA.
Borries DemelerDepartment of Biochemistry, University of Texas Health Sciences Center, 7703 Floyd Curl Drive, San Antonio, Texas 78229, USA.
Craig L PetersonProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, Massachusetts 01605, USA.
Arizona State University · USUniversity of Massachusetts Chan Medical School · USThe University of Texas at Austin · US

Funding

Trans-NetworkU54CA143862 · NCI · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI MELDRUM, DEIRDRE R. · 2009 to 2013
$8.4M
YEAST CHROMATIN STRUCTURE/FUNCTIONR01GM054096 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI PETERSON, CRAIG L · 1997 to 2017
$5.7M
NCI NIH HHS U54 CA143862NIGMS NIH HHS GM54096NIGMS NIH HHS R01 GM054096
6 · The paper itself

Abstract

Heterochromatin is a repressive chromatin compartment essential for maintaining genomic integrity. A hallmark of heterochromatin is the presence of specialized nonhistone proteins that alter chromatin structure to inhibit transcription and recombination. It is generally assumed that heterochromatin is highly condensed. However, surprisingly little is known about the structure of heterochromatin or its dynamics in solution. In budding yeast, formation of heterochromatin at telomeres and the homothallic silent mating type loci require the Sir3 protein. Here, we use a combination of sedimentation velocity, atomic force microscopy and nucleosomal array capture to characterize the stoichiometry and conformation of Sir3 nucleosomal arrays. The results indicate that Sir3 interacts with nucleosomal arrays with a stoichiometry of two Sir3 monomers per nucleosome. We also find that Sir3 fibres are less compact than canonical magnesium-induced 30 nm fibres. We suggest that heterochromatin proteins promote silencing by 'coating' nucleosomal arrays, stabilizing interactions between nucleosomal histones and DNA.

Indexed as

AlgorithmsHeterochromatinMicroscopy, Atomic ForceMonte Carlo MethodNucleosomesProtein MultimerizationSilent Information Regulator Proteins, Saccharomyces cerevisiaeUltracentrifugationHeterochromatinNucleosomesSilent Information Regulator Proteins, Saccharomyces cerevisiaeSIR3 protein, S cerevisiae

Identifiers

PMID25163529
PMCPMC4151189
OpenAlexW2090439040

What OpenQuestion holds

Textmetadata
LicenceTDM
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.