Evidence map›Paper›PMID 28895528›Full record

ArticleeLife2017

A synthetic biology approach to probing nucleosome symmetry.

Yuichi Ichikawa, Caitlin F Connelly, Alon Appleboim, Thomas Cr Miller, Hadas Jacobi, Nebiyu A Abshiru, Hsin-Jung Chou, Yuanyuan Chen, Upasna Sharma, Yupeng Zheng and 9 more

Abstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Spys Make Asymmetric Chromatin.ACS central science · 2022
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. 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

19 authors.

Yuichi Ichikawa *Department of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, United States.
Caitlin F Connelly *Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, United States.
Alon AppleboimSchool of Computer Science and Engineering, The Hebrew University of Jerusalem, Jerusalem, Israel.
Thomas Cr MillerStructural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
Hadas JacobiSchool of Computer Science and Engineering, The Hebrew University of Jerusalem, Jerusalem, Israel.
Nebiyu A AbshiruNational Resource for Translational and Developmental Proteomics, Northwestern University, Evanston, United States.
Hsin-Jung ChouDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, United States.
Yuanyuan ChenDepartment of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, United States.
Upasna SharmaDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, United States.
Yupeng ZhengNational Resource for Translational and Developmental Proteomics, Northwestern University, Evanston, United States.
Paul M ThomasNational Resource for Translational and Developmental Proteomics, Northwestern University, Evanston, United States.
Hsuiyi V ChenDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, United States.
Vineeta BajajDepartment of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, United States.
Christoph W MüllerStructural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
Neil L KelleherNational Resource for Translational and Developmental Proteomics, Northwestern University, Evanston, United States.ORCID http://orcid.org/0000-0002-8815-3372
Nir FriedmanSchool of Computer Science and Engineering, The Hebrew University of Jerusalem, Jerusalem, Israel.ORCID http://orcid.org/0000-0002-9678-3550
Daniel Na BolonDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, United States.
Oliver J RandoDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, United States.ORCID https://orcid.org/0000-0003-1516-9397
Paul D KaufmanDepartment of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, United States.ORCID http://orcid.org/0000-0003-3089-313X

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Daniela E Matei · 1993 to 2026
$153.9M
TR&D 7: Cell Specific ProteomicsP41GM108569 · NIGMS · NORTHWESTERN UNIVERSITY · PI KELLEHER, NEIL L · 2015 to 2024
$13.6M
Breaking Nucleosomal SymmetryR01GM100164 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KAUFMAN, PAUL D., RANDO, OLIVER J · 2014 to 2017
$1.3M
European Research Council 340712NCI NIH HHS P30 CA060553NIGMS NIH HHS P41 GM108569NIGMS NIH HHS R01 GM100164
6 · The paper itself

Abstract

The repeating subunit of chromatin, the nucleosome, includes two copies of each of the four core histones, and several recent studies have reported that asymmetrically-modified nucleosomes occur at regulatory elements in vivo. To probe the mechanisms by which histone modifications are read out, we designed an obligate pair of H3 heterodimers, termed H3X and H3Y, which we extensively validated genetically and biochemically. Comparing the effects of asymmetric histone tail point mutants with those of symmetric double mutants revealed that a single methylated H3K36 per nucleosome was sufficient to silence cryptic transcription in vivo. We also demonstrate the utility of this system for analysis of histone modification crosstalk, using mass spectrometry to separately identify modifications on each H3 molecule within asymmetric nucleosomes. The ability to generate asymmetric nucleosomes in vivo and in vitro provides a powerful and generalizable tool to probe the mechanisms by which H3 tails are read out by effector proteins in the cell.

Indexed as

HistonesMass SpectrometryNucleosomesProtein Processing, Post-TranslationalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSynthetic BiologyHistonesNucleosomesSaccharomyces cerevisiae ProteinschromatinchromosomesgenesS. cerevisiaesynthetic biologytranscription

Identifiers

PMID28895528
PMCPMC5626479

What OpenQuestion holds

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Registered trials

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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.