Evidence map›Paper›PMID 26534951›Full record

ArticleGenetics2016

Divergent Residues Within Histone H3 Dictate a Unique Chromatin Structure in Saccharomyces cerevisiae.

Kristina L McBurney, Andrew Leung, Jennifer K Choi, Benjamin J E Martin, Nicholas A T Irwin, Till Bartke, Christopher J Nelson, LeAnn J Howe

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

Article in Genetics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. The functional study of human proteins using humanized yeast.Journal of microbiology (Seoul, Korea) · 2020
    Review
  7. Article
  8. 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 3 institutions in 2 countries.

Kristina L McBurneyDepartment of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3.
Andrew LeungDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada V8P 5C2.
Jennifer K ChoiDepartment of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3.
Benjamin J E MartinDepartment of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3.
Nicholas A T IrwinDepartment of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3.
Till BartkeChromatin Biochemistry Group, Medical Research Council Clinical Sciences Centre, Imperial College London, London, W12 0NN, United Kingdom.
Christopher J NelsonDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada V8P 5C2.
LeAnn J HoweDepartment of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3 ljhowe@mail.ubc.ca.
University of British Columbia · CAMedical Research Council · GBUniversity of Victoria · CA

Funding

CIHRMedical Research Council MC_UP_1102/2
6 · The paper itself

Abstract

Histones are among the most conserved proteins known, but organismal differences do exist. In this study, we examined the contribution that divergent amino acids within histone H3 make to cell growth and chromatin structure in Saccharomyces cerevisiae. We show that, while amino acids that define histone H3.3 are dispensable for yeast growth, substitution of residues within the histone H3 α3 helix with human counterparts results in a severe growth defect. Mutations within this domain also result in altered nucleosome positioning, both in vivo and in vitro, which is accompanied by increased preference for nucleosome-favoring sequences. These results suggest that divergent amino acids within the histone H3 α3 helix play organismal roles in defining chromatin structure.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionChromatinHistonesHumansMolecular Sequence DataNucleosomesRecombinant ProteinsSaccharomyces cerevisiaeChromatinHistonesNucleosomesRecombinant ProteinsH3histonenucleosome positioningS. cerevisiae

Identifiers

PMID26534951
PMCPMC4701097
OpenAlexW2230750713

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.