Evidence map›Paper›PMID 25711831›Full record

ArticleG3 (Bethesda, Md.)2015

A systematic mutational analysis of a histone H3 residue in budding yeast provides insights into chromatin dynamics.

Paige Johnson, Virginia Mitchell, Kelsi McClure, Martha Kellems, Sarah Marshall, Mary K Allison, Harrison Lindley, Hoai-Trang T Nguyen, Jessalyn E Tackett, Andrea A Duina

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in G3 (Bethesda, Md.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

12 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Structure and function of the histone chaperone FACT - Resolving FACTual issues.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018
    Review
  9. Article
  10. Targeted in Situ Mutagenesis of Histone Genes in Budding Yeast.Journal of visualized experiments : JoVE · 2017
    Article
  11. Review
  12. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Paige JohnsonBiology Department, Hendrix College, Conway, Arkansas 72032.
Virginia MitchellBiology Department, Hendrix College, Conway, Arkansas 72032.
Kelsi McClureBiology Department, Hendrix College, Conway, Arkansas 72032.
Martha KellemsBiology Department, Hendrix College, Conway, Arkansas 72032.
Sarah MarshallBiology Department, Hendrix College, Conway, Arkansas 72032.
Mary K AllisonBiology Department, Hendrix College, Conway, Arkansas 72032.
Harrison LindleyBiology Department, Hendrix College, Conway, Arkansas 72032.
Hoai-Trang T NguyenBiology Department, Hendrix College, Conway, Arkansas 72032.
Jessalyn E TackettBiology Department, Hendrix College, Conway, Arkansas 72032.
Andrea A DuinaBiology Department, Hendrix College, Conway, Arkansas 72032 duina@hendrix.edu.ORCID http://orcid.org/0000-0002-6040-6825
Hendrix College · USConway School of Landscape Design · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In previous work using the Saccharomyces cerevisiae model system, a mutant version of histone H3-H3-L61W-was found to confer a variety of abnormal growth phenotypes and defects in specific aspects of the transcription process, including a pronounced alteration in the distribution pattern of the transcription elongation factor Spt16 across transcribed genes and promotion of cryptic transcription initiation within the FLO8 gene. To gain insights into the contribution of the H3-L61 residue to chromatin function, we have generated yeast strains expressing versions of histone H3 harboring all possible natural amino acid substitutions at position 61 (H3-L61X mutants) and tested them in a series of assays. We found that whereas 16 of the 19 H3-L61X mutants support viability when expressed as the sole source of histone H3 in cells, all 19 confer abnormal phenotypes ranging from very mild to severe, a finding that might in part explain the high degree of conservation of the H3-L61 residue among eukaryotes. An examination of the strength of the defects conferred by each H3-L61X mutant and the nature of the corresponding substituted residue provides insights into structural features of the nucleosome required for proper Spt16-gene interactions and for prevention of cryptic transcription initiation events. Finally, we provide evidence that the defects imparted by H3-L61X mutants on Spt16-gene interactions and on repression of intragenic transcription initiation are mechanistically related to each other.

Indexed as

Amino Acid SubstitutionChromatinHistonesMutationNucleosomesPhenotypeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptional Elongation FactorsTranscription Initiation, GeneticChromatinHistonesNucleosomesSaccharomyces cerevisiae ProteinsSPT16 protein, S cerevisiaeTranscriptional Elongation Factorschromatinhistone H3intragenic transcription initiationSpt16transcription elongation

Identifiers

PMID25711831
PMCPMC4426362
OpenAlexW2096103116

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.