Evidence map›Paper›PMID 30759223›Full record

ArticleNucleic acids research2019

Set1-catalyzed H3K4 trimethylation antagonizes the HIR/Asf1/Rtt106 repressor complex to promote histone gene expression and chronological life span.

Qianyun Mei, Chen Xu, Madelaine Gogol, Jie Tang, Wanping Chen, Xilan Yu, Jerry L Workman, Shanshan Li

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 36 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

8 authors at 2 institutions in 2 countries.

Qianyun MeiState Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences, Hubei University, Wuhan, Hubei 430062, China.
Chen XuState Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences, Hubei University, Wuhan, Hubei 430062, China.
Madelaine GogolStowers Institute for Medical Research, 1000 E. 50th Street, Kansas City, MO 64110, USA.
Jie TangState Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences, Hubei University, Wuhan, Hubei 430062, China.
Wanping ChenState Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences, Hubei University, Wuhan, Hubei 430062, China.
Xilan YuState Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences, Hubei University, Wuhan, Hubei 430062, China.
Jerry L WorkmanStowers Institute for Medical Research, 1000 E. 50th Street, Kansas City, MO 64110, USA.
Shanshan LiState Key Laboratory of Biocatalysis and Enzyme Engineering, School of Life Sciences, Hubei University, Wuhan, Hubei 430062, China.
Hubei University · CNStowers Institute for Medical Research · US

Funding

Transcription regulation in chromatinR35GM118068 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI JERRY L WORKMAN · 2016 to 2026
$4.2M
NIGMS NIH HHS R35 GM118068
6 · The paper itself

Abstract

Aging is the main risk factor for many prevalent diseases. However, the molecular mechanisms regulating aging at the cellular level are largely unknown. Using single cell yeast as a model organism, we found that reducing yeast histone proteins accelerates chronological aging and increasing histone supply extends chronological life span. We sought to identify pathways that regulate chronological life span by controlling intracellular histone levels. Thus, we screened the histone H3/H4 mutant library to uncover histone residues and posttranslational modifications that regulate histone gene expression. We discovered 15 substitution mutations with reduced histone proteins and 5 mutations with increased histone proteins. Among these mutations, we found Set1 complex-catalyzed H3K4me3 promotes histone gene transcription and maintains normal chronological life span. Unlike the canonical functions of H3K4me3 in gene expression, H3K4me3 facilitates histone gene transcription by acting as a boundary to restrict the spread of the repressive HIR/Asf1/Rtt106 complex from histone gene promoters. Collectively, our study identified a novel mechanism by which H3K4me3 antagonizes the HIR/Asf1/Rtt106 repressor complex to promote histone gene expression and extend chronological life span.

Indexed as

Cell Cycle ProteinsChromosomal Proteins, Non-HistoneDNA-Binding ProteinsGene Expression Regulation, FungalHistone-Lysine N-MethyltransferaseHistonesLongevityMolecular ChaperonesNuclear ProteinsProtein Processing, Post-TranslationalRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsASF1 protein, S cerevisiaeCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHIR1 protein, S cerevisiaehistone H3 trimethyl Lys4Histone-Lysine N-MethyltransferaseHistonesMolecular ChaperonesNuclear ProteinsRepressor ProteinsRtt106 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSET1 protein, S cerevisiae

Identifiers

PMID30759223
PMCPMC6468302
OpenAlexW2911237750

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.