Evidence map›Paper›PMID 36010552›Full record

ArticleCells2022

N-Terminal Tails of Histones H2A and H2B Differentially Affect Transcription by RNA Polymerase II In Vitro.

Han-Wen Chang, Alexey V Feofanov, Alexander V Lyubitelev, Grigory A Armeev, Elena Y Kotova, Fu-Kai Hsieh, Mikhail P Kirpichnikov, Alexey K Shaytan, Vasily M Studitsky

Open access · goldAbstract read
In one paragraph

Article in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. 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

9 authors at 3 institutions in 2 countries.

Han-Wen ChangFox Chase Cancer Center, Philadelphia, PA 19111, USA.
Alexey V FeofanovBiology Faculty, Lomonosov Moscow State University, Moscow 119992, Russia.ORCID 0000-0002-1596-9506
Alexander V LyubitelevBiology Faculty, Lomonosov Moscow State University, Moscow 119992, Russia.ORCID 0000-0003-0768-9309
Grigory A ArmeevBiology Faculty, Lomonosov Moscow State University, Moscow 119992, Russia.
Elena Y KotovaFox Chase Cancer Center, Philadelphia, PA 19111, USA.
Fu-Kai HsiehDepartment of Molecular Biology, Harvard Medical School, Boston, MA 02114, USA.
Mikhail P KirpichnikovBiology Faculty, Lomonosov Moscow State University, Moscow 119992, Russia.
Alexey K ShaytanBiology Faculty, Lomonosov Moscow State University, Moscow 119992, Russia.
Vasily M StuditskyFox Chase Cancer Center, Philadelphia, PA 19111, USA.
Lomonosov Moscow State University · RUFox Chase Cancer Center · USHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone N-terminal tails and their post-translational modifications affect various biological processes, often in a context-specific manner; the underlying mechanisms are poorly studied. Here, the role of individual N-terminal tails of histones H2A/H2B during transcription through chromatin was analyzed in vitro. spFRET data suggest that the tail of histone H2B (but not of histone H2A) affects nucleosome stability. Accordingly, deletion of the H2B tail (amino acids 1-31, but not 1-26) causes a partial relief of the nucleosomal barrier to transcribing RNA polymerase II (Pol II), likely facilitating uncoiling of DNA from the histone octamer during transcription. Taken together, the data suggest that residues 27-31 of histone H2B stabilize DNA-histone interactions at the DNA region localized ~25 bp in the nucleosome and thus interfere with Pol II progression through the region localized 11-15 bp in the nucleosome. This function of histone H2B requires the presence of the histone H2A N-tail that mediates formation of nucleosome-nucleosome dimers; however, nucleosome dimerization

Indexed as

HistonesNucleosomesChromatinDNARNA Polymerase IIChromatinDNAHistonesNucleosomesRNA Polymerase IIFACThistone H2Ahistone H2Bhistone tailsmolecular modelingnucleosomeRNA polymerase IIspFRETtranscription

Identifiers

PMID36010552
PMCPMC9406932
OpenAlexW4293777670

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.