Evidence map›Paper›PMID 26258880›Full record

ArticleeLife2015

Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1.

Agata Butryn, Jan M Schuller, Gabriele Stoehr, Petra Runge-Wollmann, Friedrich Förster, David T Auble, Karl-Peter Hopfner

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Mot1 regulation of promoter binding by TBP varies with stress and gene expression levels independently of coactivator dependence.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Structures and implications of TBP-nucleosome complexes.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

7 authors at 4 institutions in 2 countries.

Agata ButrynGene Center, Department of Biochemistry, Ludwig Maximilian University, Munich, Germany.
Jan M SchullerDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, , Germany.
Gabriele StoehrGene Center, Department of Biochemistry, Ludwig Maximilian University, Munich, Germany.
Petra Runge-WollmannGene Center, Department of Biochemistry, Ludwig Maximilian University, Munich, Germany.
Friedrich FörsterDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, , Germany.
David T AubleDepartment of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, United States.
Karl-Peter HopfnerGene Center, Department of Biochemistry, Ludwig Maximilian University, Munich, Germany.ORCID http://orcid.org/0000-0002-4528-8357
Ludwig-Maximilians-Universität München · DEMax Planck Institute of Biochemistry · DECenter for Integrated Protein Science Munich · DEUniversity of Virginia Health System · US

Funding

MOLECULAR ANALYSIS OF A YEAST TRANSCRIPTIONAL REGULATORR01GM055763 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI AUBLE, DAVID T. · 1997 to 2021
$6.4M
NIGMS NIH HHS R01 GM055763
6 · The paper itself

Abstract

Swi2/Snf2 ATPases remodel substrates such as nucleosomes and transcription complexes to control a wide range of DNA-associated processes, but detailed structural information on the ATP-dependent remodeling reactions is largely absent. The single subunit remodeler Mot1 (modifier of transcription 1) dissociates TATA box-binding protein (TBP):DNA complexes, offering a useful system to address the structural mechanisms of Swi2/Snf2 ATPases. Here, we report the crystal structure of the N-terminal domain of Mot1 in complex with TBP, DNA, and the transcription regulator negative cofactor 2 (NC2). Our data show that Mot1 reduces DNA:NC2 interactions and unbends DNA as compared to the TBP:DNA:NC2 state, suggesting that Mot1 primes TBP:NC2 displacement in an ATP-independent manner. Electron microscopy and cross-linking data suggest that the Swi2/Snf2 domain of Mot1 associates with the upstream DNA and the histone fold of NC2, thereby revealing parallels to some nucleosome remodelers. This study provides a structural framework for how a Swi2/Snf2 ATPase interacts with its substrate DNA:protein complex.

Indexed as

Crystallography, X-RayDNA, FungalEncephalitozoon cuniculiMicroscopy, ElectronModels, MolecularPhosphoproteinsProtein ConformationTATA-Binding Protein Associated FactorsTATA-Box Binding ProteinTranscription FactorsDNA, Fungaldown-regulator of transcription 1PhosphoproteinsTATA-Binding Protein Associated FactorsTATA-Box Binding ProteinTranscription Factorsbiophysicsencephalitozoon cuniculihybrid methodsMot1NC2structural biologySwi2/Snf2TBPtranscription regulation

Identifiers

PMID26258880
PMCPMC4565979
OpenAlexW2141186869

What OpenQuestion holds

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LicenceCC BY
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.