Evidence map›Paper›PMID 9671473›Full record

ArticleMolecular and cellular biology1998

Disruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase III.

C Tse, T Sera, A P Wolffe, J C Hansen

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 216 papers.

0numbers the graph read from it
0cells of the map it votes in
216citing papers in PubMed
12.8field-weighted citation impact, top 1% 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

216 citing papers in PubMed, 567 citations in OpenAlex.

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  19. Epigenetic Links between Microbiota and Gestational Diabetes.International journal of molecular sciences · 2022
    Review
  20. Article

156 more citing papers are in PubMed but not listed here.

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 2 institutions in 4 countries.

C TseDepartment of Biochemistry, The University of Texas Health Science Center at San Antonio, San Antonio, Texas 78284-7760, USA.
T Sera
A P Wolffe
J C Hansen
National Institutes of Health · USThe University of Texas Health Science Center at San Antonio · US

Funding

CHROMATIN STRUCTURE AND STABILITY IN THE SOLUTION STATER01GM045916 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI HANSEN, JEFFREY C · 1996 to 2012
$3.3M
CHROMATIN STRUCTURE AND STABILITY IN THE SOLUTION STATER29GM045916 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI HANSEN, JEFFREY C · 1991 to 1995
–
NIGMS NIH HHS GM45916NIGMS NIH HHS R01 GM045916
6 · The paper itself

Abstract

We have examined the effects of core histone acetylation on the transcriptional activity and higher-order folding of defined 12-mer nucleosomal arrays. Purified HeLa core histone octamers containing an average of 2, 6, or 12 acetates per octamer (8, 23, or 46% maximal site occupancy, respectively) were assembled onto a DNA template consisting of 12 tandem repeats of a 208-bp Lytechinus 5S rRNA gene fragment. Reconstituted nucleosomal arrays were transcribed in a Xenopus oocyte nuclear extract and analyzed by analytical hydrodynamic and electrophoretic approaches to determine the extent of array compaction. Results indicated that in buffer containing 5 mM free Mg2+ and 50 mM KCl, high levels of acetylation (12 acetates/octamer) completely inhibited higher-order folding and concurrently led to a 15-fold enhancement of transcription by RNA polymerase III. The molecular mechanisms underlying the acetylation effects on chromatin condensation were investigated by analyzing the ability of differentially acetylated nucleosomal arrays to fold and oligomerize. In MgCl2-containing buffer the folding of 12-mer nucleosomal arrays containing an average of two or six acetates per histone octamer was indistinguishable, while a level of 12 acetates per octamer completely disrupted the ability of nucleosomal arrays to form higher-order folded structures at all ionic conditions tested. In contrast, there was a linear relationship between the extent of histone octamer acetylation and the extent of disruption of Mg2+-dependent oligomerization. These results have yielded new insight into the molecular basis of acetylation effects on both transcription and higher-order compaction of nucleosomal arrays.

Indexed as

Protein FoldingTranscription, GeneticAcetylationAnimalsHeLa CellsHistonesHumansNucleosomesRNA Polymerase IIISea UrchinsXenopusHistonesNucleosomesRNA Polymerase III

Identifiers

PMID9671473
PMCPMC109049
OpenAlexW2146358743

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.