Evidence map›Paper›PMID 7579709›Full record

ArticleMolecular biology of the cell1995

Phosphorylated and dephosphorylated linker histone H1 reside in distinct chromatin domains in Tetrahymena macronuclei.

M J Lu, S S Mpoke, C A Dadd, C D Allis

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

16 citing papers in PubMed, 41 citations in OpenAlex.

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  10. Spatiotemporal sites of DNA replication in macro- and micronuclei of the ciliate Paramecium caudatum.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2003
    Article
  11. Article
  12. An HP1-like protein is missing from transcriptionally silent micronuclei of Tetrahymena.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  13. Article
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  15. Article
  16. Increased histone H1 phosphorylation and relaxed chromatin structure in Rb-deficient fibroblasts.Proceedings of the National Academy of Sciences of the United States of America · 1996
    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

4 authors at 1 institution in 1 country.

M J LuDepartment of Biology, Syracuse University, New York 13244, USA.
S S Mpoke
C A Dadd
C D Allis
Syracuse University · US

Funding

INFLUENCE OF HISTONE H1 AND HMGS ON GENE EXPRESSIONR01GM040922 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI ALLIS, CHARLES DAVID · 1989 to 2022
$10.0M
NIGMS NIH HHS GM-40922
6 · The paper itself

Abstract

Phosphorylated and dephosphorylated isoforms of Tetrahymena macronuclear H1 were separated from each other by cation-exchange high performance liquid chromatography and used to generate a pairwise set of antisera that discriminate the phosphorylation state of this linker histone. Affinity-purified antibodies from each sera recognize appropriate H1 isoforms and stain macronuclei under appropriate physiological conditions. Immunogold localizations demonstrate that phosphorylated and dephosphorylated H1 localize nonrandomly in distinct subdomains of macronuclear chromatin. Dephosphorylated H1 is strongly enriched in the electron-dense chromatin bodies that punctuate macronuclear chromatin. In contrast, phosphorylated H1 isoforms, as well as an evolutionarily conserved H2A.F/Z-like variant (hv1) believed to function in the establishment of transcriptionally competent chromatin, are modestly enriched at the periphery of chromatin bodies and in the surrounding euchromatin. Using antibodies against TATA-binding protein, we show that transcriptionally active chromatin lies outside of the chromatin bodies in an area relatively devoid of H1. Antibodies against general core histones are more or less evenly distributed across these domains. Together, these data are consistent with a model in which phosphorylation of H1, perhaps in association with hv1, loosens the binding of H1 in chromatin leading to chromatin decondensation as part of a first-step mechanism in gene activation. In contrast, our data support the view that dephosphorylation of this linker histone facilitates or stabilizes condensed, transcriptionally silent chromatin.

Indexed as

AnimalsAntibodies, ProtozoanAntibody SpecificityCell NucleusChromatinDNA-Binding ProteinsGold ColloidHistonesMicroscopy, ImmunoelectronPhosphorylationTATA-Box Binding ProteinTetrahymenaTranscription FactorsTranscription, GeneticAntibodies, ProtozoanChromatinDNA-Binding ProteinsGold ColloidHistonesTATA-Box Binding ProteinTranscription Factors

Identifiers

PMID7579709
PMCPMC301264
OpenAlexW2023275504

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.