Evidence map›Paper›PMID 26455391›Full record

ArticleMolecular cell2015

FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs.

David J Kemble, Laura L McCullough, Frank G Whitby, Tim Formosa, Christopher P Hill

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
9.2field-weighted citation impact, top 2% 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

105 citing papers in PubMed, 171 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Beyond Chaperoning: The Multifaceted Role of FACT in Chromatin Transactions.International journal of molecular sciences · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024
    Review
  16. Facilitates Chromatin Transcription in Breast and Other Cancers.Advances in experimental medicine and biology · 2024
    Review
  17. Article
  18. Article
  19. Article
  20. Review

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

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

5 authors at 1 institution in 1 country.

David J KembleDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA.
Laura L McCulloughDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA.
Frank G WhitbyDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA.
Tim FormosaDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA. Electronic address: tim@biochem.utah.edu.
Christopher P HillDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA. Electronic address: chris@biochem.utah.edu.
University of Utah · US

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 1986 to 2026
$72.6M
X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2007 to 2018
$51.1M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Biochemical, Genetic, and Genomic Analysis of Nucleosome Reorganization by FACTR01GM064649 · NIGMS · UNIVERSITY OF UTAH · PI FORMOSA, TIMOTHY G · 2002 to 2022
$6.4M
Structures of Proteasome ActivatorsR01GM059135 · NIGMS · UNIVERSITY OF UTAH · PI HILL, CHRISTOPHER P. · 1999 to 2012
$3.4M
Nucleosome Reorganizing/Remodeling ComplexesR01GM076242 · NIGMS · UNIVERSITY OF UTAH · PI HILL, CHRISTOPHER P. · 2006 to 2013
$2.2M
NCI NIH HHS P30 CA042014NCI NIH HHS P30CA042014NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393NIGMS NIH HHS P50 GM082545NIGMS NIH HHS R01 GM059135NIGMS NIH HHS R01 GM064649NIGMS NIH HHS R01 GM076242
6 · The paper itself

Abstract

FACT, a heterodimer of Spt16 and Pob3, is an essential histone chaperone. We show that the H2A-H2B binding activity that is central to FACT function resides in short acidic regions near the C termini of each subunit. Mutations throughout these regions affect binding and cause correlated phenotypes that range from mild to lethal, with the largest individual contributions unexpectedly coming from an aromatic residue and a nearby carboxylate residue within each domain. Spt16 and Pob3 bind overlapping sites on H2A-H2B, and Spt16-Pob3 heterodimers simultaneously bind two H2A-H2B dimers, the same stoichiometry as the components of a nucleosome. An Spt16:H2A-H2B crystal structure explains the biochemical and genetic data, provides a model for Pob3 binding, and implies a mechanism for FACT reorganization that we confirm biochemically. Moreover, unexpected similarity to binding of ANP32E and Swr1 with H2A.Z-H2B reveals that diverse H2A-H2B chaperones use common mechanisms of histone binding and regulating nucleosome functions.

Indexed as

Amino Acid MotifsConserved SequenceCrystallography, X-RayDNA-Binding ProteinsGene Expression Regulation, FungalHigh Mobility Group ProteinsHistonesModels, MolecularMolecular Sequence DataNucleosomesProtein BindingProtein MultimerizationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentTranscriptional Elongation FactorsDNA-Binding ProteinsFACT protein, S cerevisiaeHigh Mobility Group ProteinsHistonesNucleosomesPOB3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSPT16 protein, S cerevisiaeTranscriptional Elongation FactorsTranscription Factorscrystal structurehistone bindinghistone chaperonenucleosome reorganizationSpt16-Pob3

Identifiers

PMID26455391
PMCPMC4620744
OpenAlexW1899034947

What OpenQuestion holds

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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.