Evidence map›Paper›PMID 29136238›Full record

ArticleNucleic acids research2018

Regulation of transcriptional silencing and chromodomain protein localization at centromeric heterochromatin by histone H3 tyrosine 41 phosphorylation in fission yeast.

Bingbing Ren, Hwei Ling Tan, Thi Thuy Trang Nguyen, Ahmed Mahmoud Mohammed Sayed, Ying Li, Yu-Keung Mok, Henry Yang, Ee Sin Chen

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.2field-weighted citation impact, top 43% 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

10 citing papers in PubMed, 12 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 1 country.

Bingbing RenDepartment of Biochemistry, National University of Singapore, Yong Loo Lin School of Medicine, Singapore.
Hwei Ling TanDepartment of Biochemistry, National University of Singapore, Yong Loo Lin School of Medicine, Singapore.
Thi Thuy Trang NguyenDepartment of Biochemistry, National University of Singapore, Yong Loo Lin School of Medicine, Singapore.
Ahmed Mahmoud Mohammed SayedDepartment of Biological Sciences, National University of Singapore.
Ying LiCancer Science Institute, National University of Singapore, Yong Loo Lin School of Medicine, Singapore.
Yu-Keung MokDepartment of Biological Sciences, National University of Singapore.
Henry YangCancer Science Institute, National University of Singapore, Yong Loo Lin School of Medicine, Singapore.
Ee Sin ChenDepartment of Biochemistry, National University of Singapore, Yong Loo Lin School of Medicine, Singapore.
National University of Singapore · SGNational University Health System · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heterochromatin silencing is critical for genomic integrity and cell survival. It is orchestrated by chromodomain (CD)-containing proteins that bind to methylated histone H3 lysine 9 (H3K9me), a hallmark of heterochromatin. Here, we show that phosphorylation of tyrosine 41 (H3Y41p)-a novel histone H3 modification-participates in the regulation of heterochromatin in fission yeast. We show that a loss-of-function mutant of H3Y41 can suppress heterochromatin de-silencing in the centromere and subtelomere repeat regions, suggesting a de-silencing role for H3Y41p on heterochromatin. Furthermore, we show both in vitro and in vivo that H3Y41p differentially regulates two CD-containing proteins without the change in the level of H3K9 methylation: it promotes the binding of Chp1 to histone H3 and the exclusion of Swi6. H3Y41p is preferentially enriched on centromeric heterochromatin during M- to early S phase, which coincides with the localization switch of Swi6/Chp1. The loss-of-function H3Y41 mutant could suppress the hypersensitivity of the RNAi mutants towards hydroxyurea (HU), which arrests replication in S phase. Overall, we describe H3Y41p as a novel histone modification that differentially regulates heterochromatin silencing in fission yeast via the binding of CD-containing proteins.

Indexed as

RNA InterferenceCell Cycle CheckpointsCentromereHeterochromatinHistonesLoss of Function MutationMethylationPhosphorylationSchizosaccharomycesSchizosaccharomyces pombe ProteinsS PhaseTyrosineHeterochromatinHistonesSchizosaccharomyces pombe ProteinsTyrosine

Identifiers

PMID29136238
PMCPMC5758876
OpenAlexW2768039881

What OpenQuestion holds

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LicenceCC BY-NC
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.