Evidence map›Paper›PMID 26912860›Full record

ArticleScience (New York, N.Y.)2016

Structural basis for histone H2B deubiquitination by the SAGA DUB module.

Michael T Morgan, Mahmood Haj-Yahya, Alison E Ringel, Prasanthi Bandi, Ashraf Brik, Cynthia Wolberger

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers.

0numbers the graph read from it
0cells of the map it votes in
152citing papers in PubMed
18.5field-weighted citation impact, top 1% 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

152 citing papers in PubMed, 248 citations in OpenAlex.

  1. Article
  2. Substrate biasing in UCHL5 proteoforms.bioRxiv : the preprint server for biology · 2026
    Article
  3. A Chromatin Biology Assessment of AlphaFold3.bioRxiv : the preprint server for biology · 2026
    Article
  4. Structure and molecular function of the BCL7 proteins.Biochemical Society transactions · 2026
    Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Research progress of DUB enzyme in breast cancer.Clinical and experimental medicine · 2025
    Review
  16. Article
  17. Article
  18. Haspin kinase binds to a nucleosomal DNA supergroove.Nature structural & molecular biology · 2025
    Article
  19. Article
  20. Review

92 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 2 countries.

Michael T MorganDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Mahmood Haj-YahyaDepartment of Chemistry, Ben-Gurion University of the Negev, Beer Sheva 8410501, Israel.
Alison E RingelDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Prasanthi BandiDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Ashraf BrikSchulich Faculty of Chemistry, Technion-Israel Institute of Technology, Haifa 3200008, Israel.
Cynthia WolbergerDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. cwolberg@jhmi.edu.
Johns Hopkins Medicine · USJohns Hopkins University · USBen-Gurion University of the Negev · ILTechnion – Israel Institute of Technology · IL

Funding

Translational Research Central ServicesP30CA006973 · NCI · JOHNS HOPKINS UNIVERSITY · PI Rosalie Wollett · 1985 to 2026
$208.6M
PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
Structure and Function of the SAGA Deubiquitinating ModuleR01GM095822 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WOLBERGER, CYNTHIA · 2011 to 2018
$2.7M
NCI NIH HHS P30 CA006973NCI NIH HHS Y01 CO001020NCI NIH HHS Y1-CO-1020NIGMS NIH HHS GM-095822NIGMS NIH HHS R01 GM095822NIGMS NIH HHS T32 GM008403NIGMS NIH HHS Y01 GM001104NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

Monoubiquitinated histone H2B plays multiple roles in transcription activation. H2B is deubiquitinated by the Spt-Ada-Gcn5 acetyltransferase (SAGA) coactivator, which contains a four-protein subcomplex known as the deubiquitinating (DUB) module. The crystal structure of the Ubp8/Sgf11/Sus1/Sgf73 DUB module bound to a ubiquitinated nucleosome reveals that the DUB module primarily contacts H2A/H2B, with an arginine cluster on the Sgf11 zinc finger domain docking on the conserved H2A/H2B acidic patch. The Ubp8 catalytic domain mediates additional contacts with H2B, as well as with the conjugated ubiquitin. We find that the DUB module deubiquitinates H2B both in the context of the nucleosome and in H2A/H2B dimers complexed with the histone chaperone, FACT, suggesting that SAGA could target H2B at multiple stages of nucleosome disassembly and reassembly during transcription.

Indexed as

UbiquitinationAnimalsCatalytic DomainCrystallography, X-RayEndopeptidasesHistone AcetyltransferasesHistonesNuclear ProteinsNucleosomesProtein MultimerizationProtein Structure, SecondaryRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscriptional ActivationTranscription FactorsEndopeptidasesHistone AcetyltransferasesHistonesNuclear ProteinsNucleosomesRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSAGA complex, S cerevisiaeSGF11 protein, S cerevisiaeSgf73 protein, S cerevisiaeSus1 protein, S cerevisiaeTrans-ActivatorsTranscription FactorsUbiquitinUBP8 protein, S cerevisiae

Identifiers

PMID26912860
PMCPMC4863942
OpenAlexW2287689805

What OpenQuestion holds

Textmetadata
LicenceTDM
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.