Evidence map›Paper›PMID 25294883›Full record

ArticleThe Journal of biological chemistry2014

Sumoylated human histone H4 prevents chromatin compaction by inhibiting long-range internucleosomal interactions.

Abhinav Dhall, Sijie Wei, Beat Fierz, Christopher L Woodcock, Tae-Hee Lee, Champak Chatterjee

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

51 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
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  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Regulation of SUMOylation on RNA metabolism in cancers.Frontiers in molecular biosciences · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. The solid and liquid states of chromatin.Epigenetics & chromatin · 2021
    Review
  16. Review
  17. Histone sumoylation and chromatin dynamics.Nucleic acids research · 2021
    Review
  18. Review
  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

6 authors at 4 institutions in 2 countries.

Abhinav DhallFrom the Department of Chemistry, University of Washington, Seattle, Washington 98195.
Sijie Weithe Department of Chemistry, Pennsylvania State University, University Park, Pennsylvania 16802.
Beat Fierzthe Institute of Chemical Sciences and Engineering, Ecole polytechnique fédérale de Lausanne, CH-1015 Lausanne, Switzerland, and.
Christopher L Woodcockthe Department of Biology, University of Massachusetts, Amherst, Massachusetts 01003 chris@bio.umass.edu.
Tae-Hee Leethe Department of Chemistry, Pennsylvania State University, University Park, Pennsylvania 16802, txl18@psu.edu.
Champak ChatterjeeFrom the Department of Chemistry, University of Washington, Seattle, Washington 98195, chatterjee@chem.washington.edu.
Pennsylvania State University · USUniversity of Washington · USÉcole Polytechnique Fédérale de Lausanne · CHUniversity of Massachusetts Amherst · US

Funding

Chemical Strategies to Investigate Gene Regulation By Histone SumoylationR01GM110430 · NIGMS · UNIVERSITY OF WASHINGTON · PI CHATTERJEE, CHAMPAK · 2014 to 2022
$2.5M
Dynamics of nucleosome assembly/disassembly affected by chromatin modificationsR01GM097286 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI LEE, TAE-HEE · 2011 to 2015
$1.4M
Acquisition of Analytical Ultracentrifuge at UWS10RR027217 · NCRR · UNIVERSITY OF WASHINGTON · PI KLEVIT, RACHEL E · 2010 to 2010
$313k
NCRR NIH HHS S10 RR027217NIGMS NIH HHS GM097286NIGMS NIH HHS GM110430-01NIGMS NIH HHS R01 GM097286NIGMS NIH HHS R01 GM110430
6 · The paper itself

Abstract

The structure of eukaryotic chromatin directly influences gene function, and is regulated by chemical modifications of the core histone proteins. Modification of the human histone H4 N-terminal tail region by the small ubiquitin-like modifier protein, SUMO-3, is associated with transcription repression. However, the direct effect of sumoylation on chromatin structure and function remains unknown. Therefore, we employed a disulfide-directed strategy to generate H4 homogenously and site-specifically sumoylated at Lys-12 (suH4ss). Chromatin compaction and oligomerization assays with nucleosomal arrays containing suH4ss established that SUMO-3 inhibits array folding and higher order oligomerization, which underlie chromatin fiber formation. Moreover, the effect of sumoylation differed from that of acetylation, and could be recapitulated with the structurally similar protein ubiquitin. Mechanistic studies at the level of single nucleosomes revealed that, unlike acetylation, the effect of SUMO-3 arises from the attenuation of long-range internucleosomal interactions more than from the destabilization of a compacted dinucleosome state. Altogether, our results present the first insight on the direct structural effects of histone H4 sumoylation and reveal a novel mechanism by which SUMO-3 inhibits chromatin compaction.

Indexed as

Protein Processing, Post-TranslationalAcetylationChromatin Assembly and DisassemblyDisulfidesEscherichia coliHistonesHumansKineticsLysineModels, MolecularNucleosomesRecombinant ProteinsSignal TransductionSumoylationTranscription, GeneticUbiquitinDisulfidesHistonesLysineNucleosomesRecombinant ProteinsUbiquitinAcetylationChemical ModificationChromatin StructureDisulfideHistoneInteinLigationPost-translational Modification (PTM)Small Ubiquitin-like Modifier (SUMO)Sumoylation

Identifiers

PMID25294883
PMCPMC4256319
OpenAlexW2078374423

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.