Evidence map›Paper›PMID 9171362›Full record

ArticleThe EMBO journal1997

Histone octamer function in vivo: mutations in the dimer-tetramer interfaces disrupt both gene activation and repression.

M S Santisteban, G Arents, E N Moudrianakis, M M Smith

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

38 citing papers in PubMed, 88 citations in OpenAlex.

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  18. High-resolution structure of the native histone octamer.Acta crystallographica. Section F, Structural biology and crystallization communications · 2005
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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

4 authors at 3 institutions in 1 country.

M S SantistebanDepartment of Microbiology and University of Virginia Cancer Center, School of Medicine, Charlottesville 22908, USA.
G Arents
E N Moudrianakis
M M Smith
Johns Hopkins University · USUniversity of Virginia · USUniversity of Virginia Cancer Center

Funding

HISTONE GENE EXPRESSION IN YEASTR01GM028920 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI SMITH, M MITCHELL · 1985 to 2007
$2.7M
NIGMS NIH HHS GM28920
6 · The paper itself

Abstract

Within the core histone octamer each histone H4 interacts with each H2A-H2B dimer subunit through two binding surfaces. Tyrosines play a central role in these interactions with H4 tyrosines 72 and 88 contacting one H2A-H2B dimer subunit, and tyrosine 98 contacting the other. To investigate the roles of these interactions in vivo, we made site-directed amino acid substitutions at each of these tyrosine residues. Elimination of either set of interactions is lethal, suggesting that binding of the tetramer to both dimers is essential. Temperature-sensitive mutants were obtained through single amino acid substitutions at each of the tyrosines. The mutants show both strong positive and negative effects on transcription. Positive effects include Spt- and Sin-phenotypes resulting from mutations at each of the three tyrosines. One allele has a strong negative effect on the expression of genes essential for the G1 cell cycle transition. At restrictive temperature, mutant cells fail to express the CLN1, CLN2, SWI4 and SWI6 genes, and have reduced levels of CLN3 mRNA. These results demonstrate the critical role of histone dimer-tetramer interactions in vivo, and define their essential role in the expression of genes regulating G1 cell cycle progression.

Indexed as

Gene Expression RegulationChromatinCrystallography, X-RayDimerizationDNA, FungalDNA Mutational AnalysisFungal ProteinsG1 PhaseGenes, FungalHistonesModels, MolecularMutagenesis, Site-DirectedNucleosomesPhenotypeProtein ConformationSaccharomyces cerevisiaeChromatinDNA, FungalFungal ProteinsHistonesNucleosomesTyrosine

Identifiers

PMID9171362
PMCPMC1169849
OpenAlexW2005793722

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.