Evidence map›Paper›PMID 29339748›Full record

ArticleNature communications2018

Dot1 regulates nucleosome dynamics by its inherent histone chaperone activity in yeast.

Soyun Lee, Seunghee Oh, Kwiwan Jeong, Hyelim Jo, Yoonjung Choi, Hogyu David Seo, Minhoo Kim, Joonho Choe, Chang Seob Kwon, Daeyoup Lee

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

29 citing papers in PubMed, 43 citations in OpenAlex.

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  8. Enhanced oxidative stress resistance in Ustilago maydis and its implications on the virulence.International microbiology : the official journal of the Spanish Society for Microbiology · 2024
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  18. Signals for antigen-independent differentiation of memory CD8Cellular and molecular life sciences : CMLS · 2021
    Review
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  20. 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

10 authors at 3 institutions in 1 country.

Soyun LeeDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Republic of Korea.
Seunghee OhDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Republic of Korea.
Kwiwan JeongBiocenter, Gyeonggi Business & Science Accelerator, Suwon, Gyeonggi-do, 16229, Republic of Korea.
Hyelim JoDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Republic of Korea.
Yoonjung ChoiDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Republic of Korea.
Hogyu David SeoDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Republic of Korea.
Minhoo KimDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Republic of Korea.
Joonho ChoeDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Republic of Korea.
Chang Seob KwonDepartment of Chemistry and Biology, Korea Science Academy of KAIST, Busan, 47162, Republic of Korea.
Daeyoup LeeDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Republic of Korea. daeyoup@kaist.ac.kr.
Korea Advanced Institute of Science and Technology · KRBio-Medical Science (South Korea) · KRKorean Academy of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dot1 (disruptor of telomeric silencing-1, DOT1L in humans) is the only known enzyme responsible for histone H3 lysine 79 methylation (H3K79me) and is evolutionarily conserved in most eukaryotes. Yeast Dot1p lacks a SET domain and does not methylate free histones and thus may have different actions with respect to other histone methyltransferases. Here we show that Dot1p displays histone chaperone activity and regulates nucleosome dynamics via histone exchange in yeast. We show that a methylation-independent function of Dot1p is required for the cryptic transcription within transcribed regions seen following disruption of the Set2-Rpd3S pathway. Dot1p can assemble core histones to nucleosomes and facilitate ATP-dependent chromatin-remodeling activity through its nucleosome-binding domain, in vitro. Global analysis indicates that Dot1p appears to be particularly important for histone exchange and chromatin accessibility on the transcribed regions of long-length genes. Our findings collectively suggest that Dot1p-mediated histone chaperone activity controls nucleosome dynamics in transcribed regions.

Indexed as

ChromatinGene Expression Regulation, FungalHistone ChaperonesHistone-Lysine N-MethyltransferaseHistonesLysineMutationNuclear ProteinsNucleosomesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription, GeneticChromatinDot1 protein, S cerevisiaeHistone ChaperonesHistone-Lysine N-MethyltransferaseHistonesLysineNuclear ProteinsNucleosomesSaccharomyces cerevisiae Proteins

Identifiers

PMID29339748
PMCPMC5770421
OpenAlexW2782621646

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.