Evidence map›Paper›PMID 25275495›Full record

ArticlePLoS genetics2014

H2B mono-ubiquitylation facilitates fork stalling and recovery during replication stress by coordinating Rad53 activation and chromatin assembly.

Chia-Yeh Lin, Meng-Ying Wu, Sophie Gay, Lisette Marjavaara, Mong Sing Lai, Wei-Chun Hsiao, Shih-Hsun Hung, Hsin-Yi Tseng, Duncan Edward Wright, Chen-Yi Wang and 4 more

Abstract read
In one paragraph

Article in PLoS genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Histone dynamics during DNA replication stress.Journal of biomedical science · 2021
    Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Monoubiquitylation of histone H2B contributes to the bypass of DNA damage during and after DNA replication.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Article
  19. Article
  20. Review
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

14 authors.

Chia-Yeh LinInstitute of Cellular and Organismic Biology, Academia Sinica, Nankang, Taipei, Taiwan; Graduate Institute of Nutrition and Food Sciences, Fu-Jen Catholic University, Xinzhuang, New Taipei City, Taiwan.
Meng-Ying WuInstitute of Cellular and Organismic Biology, Academia Sinica, Nankang, Taipei, Taiwan.
Sophie GayFondazione Istituto FIRC di Oncologia Molecolare (IFOM), IFOM-IEO Campus, Milan, Italy.
Lisette MarjavaaraDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Mong Sing LaiFondazione Istituto FIRC di Oncologia Molecolare (IFOM), IFOM-IEO Campus, Milan, Italy.
Wei-Chun HsiaoInstitute of Cellular and Organismic Biology, Academia Sinica, Nankang, Taipei, Taiwan.
Shih-Hsun HungInstitute of Cellular and Organismic Biology, Academia Sinica, Nankang, Taipei, Taiwan.
Hsin-Yi TsengInstitute of Cellular and Organismic Biology, Academia Sinica, Nankang, Taipei, Taiwan.
Duncan Edward WrightInstitute of Cellular and Organismic Biology, Academia Sinica, Nankang, Taipei, Taiwan.
Chen-Yi WangInstitute of Cellular and Organismic Biology, Academia Sinica, Nankang, Taipei, Taiwan; Institut de Génétique et de Biologie Moléculaire. CNRS UMR 7104, INSERM U 596, Université Louis Pasteur de Strasbourg, Illkirch, CU de Strasbourg, France.
Guoo-Shyng W HsuGraduate Institute of Nutrition and Food Sciences, Fu-Jen Catholic University, Xinzhuang, New Taipei City, Taiwan.
Didier DevysInstitut de Génétique et de Biologie Moléculaire. CNRS UMR 7104, INSERM U 596, Université Louis Pasteur de Strasbourg, Illkirch, CU de Strasbourg, France.
Andrei ChabesDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Cheng-Fu KaoInstitute of Cellular and Organismic Biology, Academia Sinica, Nankang, Taipei, Taiwan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The influence of mono-ubiquitylation of histone H2B (H2Bub) on transcription via nucleosome reassembly has been widely documented. Recently, it has also been shown that H2Bub promotes recovery from replication stress; however, the underling molecular mechanism remains unclear. Here, we show that H2B ubiquitylation coordinates activation of the intra-S replication checkpoint and chromatin re-assembly, in order to limit fork progression and DNA damage in the presence of replication stress. In particular, we show that the absence of H2Bub affects replication dynamics (enhanced fork progression and reduced origin firing), leading to γH2A accumulation and increased hydroxyurea sensitivity. Further genetic analysis indicates a role for H2Bub in transducing Rad53 phosphorylation. Concomitantly, we found that a change in replication dynamics is not due to a change in dNTP level, but is mediated by reduced Rad53 activation and destabilization of the RecQ helicase Sgs1 at the fork. Furthermore, we demonstrate that H2Bub facilitates the dissociation of the histone chaperone Asf1 from Rad53, and nucleosome reassembly behind the fork is compromised in cells lacking H2Bub. Taken together, these results indicate that the regulation of H2B ubiquitylation is a key event in the maintenance of genome stability, through coordination of intra-S checkpoint activation, chromatin assembly and replication fork progression.

Indexed as

Chromatin Assembly and DisassemblyCell Cycle ProteinsCheckpoint Kinase 2DNA ReplicationHistone-Lysine N-MethyltransferaseHistonesHydroxyureaMolecular ChaperonesMutationNucleosomesProtein Serine-Threonine KinasesRecQ HelicasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationASF1 protein, S cerevisiaeBRE2 protein, S cerevisiaeCell Cycle ProteinsCheckpoint Kinase 2DUN1 protein, S cerevisiaeHistone-Lysine N-MethyltransferaseHistonesHydroxyureaMolecular ChaperonesNucleosomesProtein Serine-Threonine KinasesRAD53 protein, S cerevisiaeRecQ HelicasesSaccharomyces cerevisiae ProteinsSGS1 protein, S cerevisiae

Identifiers

PMID25275495
PMCPMC4183429

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.