Evidence map›Paper›PMID 27601672›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Structural mechanism for the recognition and ubiquitination of a single nucleosome residue by Rad6-Bre1.

Laura D Gallego, Medini Ghodgaonkar Steger, Anton A Polyansky, Tobias Schubert, Bojan Zagrovic, Ning Zheng, Tim Clausen, Franz Herzog, Alwin Köhler

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

28 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
  3. Article
  4. Review
  5. Mechanism of histone H2B monoubiquitination by Bre1.Nature structural & molecular biology · 2023
    Article
  6. 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
  7. Review
  8. Article
  9. Article
  10. Review
  11. BRCA1/BARD1 is a nucleosome reader and writer.Trends in biochemical sciences · 2022
    Review
  12. Article
  13. Biochemical insights into Paf1 complex-induced stimulation of Rad6/Bre1-mediated H2B monoubiquitination.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Review
  15. Review
  16. Review
  17. RPA-mediated recruitment of Bre1 couples histone H2B ubiquitination to DNA replication and repair.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. The Bre1/Rad6 machinery: writing the central histone ubiquitin mark on H2B and beyond.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2020
    Review
  19. Review
  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

9 authors at 6 institutions in 3 countries.

Laura D GallegoMax F. Perutz Laboratories, Medical University of Vienna, Vienna Biocenter Campus, 1030 Vienna, Austria;
Medini Ghodgaonkar StegerGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich 81377, Germany;
Anton A PolyanskyMax F. Perutz Laboratories, Department of Structural and Computational Biology, University of Vienna, Vienna Biocenter Campus, 1030 Vienna, Austria;
Tobias SchubertMax F. Perutz Laboratories, Medical University of Vienna, Vienna Biocenter Campus, 1030 Vienna, Austria;
Bojan ZagrovicMax F. Perutz Laboratories, Department of Structural and Computational Biology, University of Vienna, Vienna Biocenter Campus, 1030 Vienna, Austria;
Ning ZhengDepartment of Pharmacology, University of Washington, Seattle, WA 98195; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195;
Tim ClausenResearch Institute of Molecular Pathology, Vienna Biocenter Campus, 1030 Vienna, Austria.
Franz HerzogGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich 81377, Germany;
Alwin KöhlerMax F. Perutz Laboratories, Medical University of Vienna, Vienna Biocenter Campus, 1030 Vienna, Austria; alwin.koehler@mfpl.ac.at.
Max Perutz Labs · ATLudwig-Maximilians-Universität München · DEHoward Hughes Medical Institute · USMassachusetts General Hospital · USResearch Institute of Molecular Pathology · ATVienna Biocenter · AT

Funding

Structural Studies of cullin-based ubiquitin ligasesR01CA107134 · NCI · UNIVERSITY OF WASHINGTON · PI ZHENG, NING · 2004 to 2013
$3.0M
Austrian Science Fund FWF Y 557European Research Council 279408European Research Council 281354NCI NIH HHS R01 CA107134
6 · The paper itself

Abstract

Cotranscriptional ubiquitination of histone H2B is key to gene regulation. The yeast E3 ubiquitin ligase Bre1 (human RNF20/40) pairs with the E2 ubiquitin conjugating enzyme Rad6 to monoubiquitinate H2B at Lys123. How this single lysine residue on the nucleosome core particle (NCP) is targeted by the Rad6-Bre1 machinery is unknown. Using chemical cross-linking and mass spectrometry, we identified the functional interfaces of Rad6, Bre1, and NCPs in a defined in vitro system. The Bre1 RING domain cross-links exclusively with distinct regions of histone H2B and H2A, indicating a spatial alignment of Bre1 with the NCP acidic patch. By docking onto the NCP surface in this distinct orientation, Bre1 positions the Rad6 active site directly over H2B Lys123. The Spt-Ada-Gcn5 acetyltransferase (SAGA) H2B deubiquitinase module competes with Bre1 for binding to the NCP acidic patch, indicating regulatory control. Our study reveals a mechanism that ensures site-specific NCP ubiquitination and fine-tuning of opposing enzymatic activities.

Indexed as

Gene Expression Regulation, EnzymologicHistonesHumansMolecular Docking SimulationNucleosomesProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitinationUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesBre1 protein, S cerevisiaeHistonesNucleosomesRAD6 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesBre1–Rad6cross-linking mass spectrometrynucleosomeRING E3 ligaseubiquitin

Identifiers

PMID27601672
PMCPMC5035881
OpenAlexW2520960958

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.