Evidence map›Paper›PMID 34385316›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Biochemical insights into Paf1 complex-induced stimulation of Rad6/Bre1-mediated H2B monoubiquitination.

Feilong Chen, Beibei Liu, Lu Guo, Xuan Ge, Wei Feng, De-Feng Li, Hao Zhou, Jiafu Long

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. 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
1.5field-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, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
  8. Article
  9. Facilitates Chromatin Transcription in Breast and Other Cancers.Advances in experimental medicine and biology · 2024
    Review
  10. Article
  11. Article
  12. Paf1 complex subunit Rtf1 stimulates H2B ubiquitylation by interacting with the highly conserved N-terminal helix of Rad6.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The Paf1 complex is required for RNA polymerase II removal in response to DNA damage.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. 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

8 authors at 2 institutions in 1 country.

Feilong ChenState Key Laboratory of Medicinal Chemical Biology, Tianjin Key Laboratory of Protein Science, Nankai University, Tianjin 300071, China.ORCID 0000-0002-6678-4966
Beibei LiuState Key Laboratory of Medicinal Chemical Biology, Tianjin Key Laboratory of Protein Science, Nankai University, Tianjin 300071, China.
Lu GuoState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Xuan GeNational Laboratory of Biomacromolecules, Chinese Academy of Sciences Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Wei FengNational Laboratory of Biomacromolecules, Chinese Academy of Sciences Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
De-Feng LiState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; jflong@nankai.edu.cn haozhou@nankai.edu.cn lidefeng@im.ac.cn.ORCID 0000-0002-8683-019X
Hao ZhouState Key Laboratory of Medicinal Chemical Biology, Tianjin Key Laboratory of Protein Science, Nankai University, Tianjin 300071, China; jflong@nankai.edu.cn haozhou@nankai.edu.cn lidefeng@im.ac.cn.
Jiafu LongState Key Laboratory of Medicinal Chemical Biology, Tianjin Key Laboratory of Protein Science, Nankai University, Tianjin 300071, China; jflong@nankai.edu.cn haozhou@nankai.edu.cn lidefeng@im.ac.cn.ORCID 0000-0002-6625-0147
Chinese Academy of Sciences · CNNankai University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The highly conserved multifunctional polymerase-associated factor 1 (Paf1) complex (PAF1C), composed of five core subunits Paf1, Leo1, Ctr9, Cdc73, and Rtf1, participates in all stages of transcription and is required for the Rad6/Bre1-mediated monoubiquitination of histone H2B (H2Bub). However, the molecular mechanisms underlying the contributions of the PAF1C subunits to H2Bub are not fully understood. Here, we report that Ctr9, acting as a hub, interacts with the carboxyl-terminal acidic tail of Rad6, which is required for PAF1C-induced stimulation of H2Bub. Importantly, we found that the Ras-like domain of Cdc73 has the potential to accelerate ubiquitin discharge from Rad6 and thus facilitates H2Bub, a process that might be conserved from yeast to humans. Moreover, we found that Rtf1 HMD stimulates H2Bub, probably through accelerating ubiquitin discharge from Rad6 alone or in cooperation with Cdc73 and Bre1, and that the Paf1/Leo1 heterodimer in PAF1C specifically recognizes the histone H3 tail of nucleosomal substrates, stimulating H2Bub. Collectively, our biochemical results indicate that intact PAF1C is required to efficiently stimulate Rad6/Bre1-mediated H2Bub.

Indexed as

Cell Cycle ProteinsCloning, MolecularEscherichia coliGene Expression Regulation, FungalHistonesNuclear ProteinsNucleosomesProtein SubunitsRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTATA-Box Binding ProteinTranscriptional Elongation FactorsUbiquitin-Conjugating EnzymesBre1 protein, S cerevisiaeCDC73 protein, S cerevisiaeCell Cycle ProteinsCTR9 protein, S cerevisiaeHistonesLeo1 protein, S cerevisiaeNuclear ProteinsNucleosomesPAF1 protein, S cerevisiaeProtein SubunitsRAD6 protein, S cerevisiaeRNA-Binding ProteinsRTF1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTATA-Box Binding ProteinTranscriptional Elongation FactorsUbiquitin-Conjugating EnzymescooperationH2B monoubiquitinationPaf1 complexRad6/Bre1ubiquitin discharge

Identifiers

PMID34385316
PMCPMC8379938
OpenAlexW3189069144

What OpenQuestion holds

Textmetadata
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.