Evidence map›Paper›PMID 31537788›Full record

ArticleNature communications2019

Transcription-dependent targeting of Hda1C to hyperactive genes mediates H4-specific deacetylation in yeast.

So Dam Ha, Seokjin Ham, Min Young Kim, Ji Hyun Kim, Insoon Jang, Bo Bae Lee, Min Kyung Lee, Jin-Taek Hwang, Tae-Young Roh, TaeSoo Kim

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 25% 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, 24 citations in OpenAlex.

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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

10 authors at 3 institutions in 1 country.

So Dam HaDepartment of Life Science and the Research Center for Cellular Homeostasis, Ewha Womans University, Seoul, 03760, Korea.
Seokjin HamDepartment of Life Sciences, Pohang University of Science and Technology (POSTECH), Pohang, 37673, Korea.
Min Young KimDepartment of Life Science and the Research Center for Cellular Homeostasis, Ewha Womans University, Seoul, 03760, Korea.
Ji Hyun KimDepartment of Life Science and the Research Center for Cellular Homeostasis, Ewha Womans University, Seoul, 03760, Korea.
Insoon JangDivision of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology (POSTECH), Pohang, 37673, Korea.ORCID http://orcid.org/0000-0001-9542-6984
Bo Bae LeeDepartment of Life Science and the Research Center for Cellular Homeostasis, Ewha Womans University, Seoul, 03760, Korea.
Min Kyung LeeDepartment of Life Science and the Research Center for Cellular Homeostasis, Ewha Womans University, Seoul, 03760, Korea.
Jin-Taek HwangKorea Food Research Institute, Wanju, 55365, Korea.
Tae-Young RohDepartment of Life Sciences, Pohang University of Science and Technology (POSTECH), Pohang, 37673, Korea. tyroh@postech.edu.ORCID http://orcid.org/0000-0001-5833-0844
TaeSoo KimDepartment of Life Science and the Research Center for Cellular Homeostasis, Ewha Womans University, Seoul, 03760, Korea. tskim@ewha.ac.kr.ORCID http://orcid.org/0000-0002-3902-1058
Ewha Womans University · KRPohang University of Science and Technology · KRKorea Food Research Institute · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In yeast, Hda1 histone deacetylase complex (Hda1C) preferentially deacetylates histones H3 and H2B, and functionally interacts with Tup1 to repress transcription. However, previous studies identified global increases in histone H4 acetylation in cells lacking Hda1, a component of Hda1C. Here, we find that Hda1C binds to hyperactive genes, likely via the interaction between the Arb2 domain of Hda1 and RNA polymerase II. Additionally, we report that Hda1C specifically deacetylates H4, but not H3, at hyperactive genes to partially inhibit elongation. This role is contrast to that of the Set2-Rpd3S pathway deacetylating histones at infrequently transcribed genes. We also find that Hda1C deacetylates H3 at inactive genes to delay the kinetics of gene induction. Therefore, in addition to fine-tuning of transcriptional response via H3-specific deacetylation, Hda1C may modulate elongation by specifically deacetylating H4 at highly transcribed regions.

Indexed as

DNA-Binding ProteinsGene Expression Regulation, FungalHistone DeacetylasesHistonesNuclear ProteinsProtein DomainsRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription, GeneticDNA-Binding ProteinsHDA1 protein, S cerevisiaeHistone DeacetylasesHistonesNuclear ProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsTUP1 protein, S cerevisiae

Identifiers

PMID31537788
PMCPMC6753149
OpenAlexW2973722891

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.