Evidence map›Paper›PMID 37106137›Full record

ArticleNature structural & molecular biology2023

Structural basis for TBP displacement from TATA box DNA by the Swi2/Snf2 ATPase Mot1.

Stephan Woike, Sebastian Eustermann, James Jung, Simon Josef Wenzl, Götz Hagemann, Joseph Bartho, Katja Lammens, Agata Butryn, Franz Herzog, Karl-Peter Hopfner

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Review
  3. Multiple Roles of dXNP and dADD1-International journal of molecular sciences · 2023
    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

10 authors at 5 institutions in 4 countries.

Stephan WoikeDepartment of Biochemistry, Ludwig-Maximilians-Universität, Munich, Germany.
Sebastian Eustermann *Department of Biochemistry, Ludwig-Maximilians-Universität, Munich, Germany.ORCID http://orcid.org/0000-0002-4439-7770
James Jung *Department of Biochemistry, Ludwig-Maximilians-Universität, Munich, Germany.
Simon Josef WenzlDepartment of Biochemistry, Ludwig-Maximilians-Universität, Munich, Germany.
Götz HagemannDepartment of Biochemistry, Ludwig-Maximilians-Universität, Munich, Germany.ORCID http://orcid.org/0000-0002-1147-7758
Joseph BarthoDepartment of Biochemistry, Ludwig-Maximilians-Universität, Munich, Germany.ORCID http://orcid.org/0000-0003-3853-2347
Katja LammensDepartment of Biochemistry, Ludwig-Maximilians-Universität, Munich, Germany.ORCID http://orcid.org/0000-0002-4438-1381
Agata ButrynDepartment of Biochemistry, Ludwig-Maximilians-Universität, Munich, Germany.ORCID http://orcid.org/0000-0002-5227-4770
Franz HerzogGene Center, Ludwig-Maximilians-Universität, Munich, Germany.ORCID http://orcid.org/0000-0001-8270-1449
Karl-Peter HopfnerDepartment of Biochemistry, Ludwig-Maximilians-Universität, Munich, Germany. hopfner@genzentrum.lmu.de.ORCID http://orcid.org/0000-0002-4528-8357
Ludwig-Maximilians-Universität München · DEEuropean Molecular Biology Laboratory · DEIMC University of Applied Sciences Krems · ATThe Francis Crick Institute · GBThe University of Queensland · AU

Funding

European Research Council 833613
6 · The paper itself

Abstract

The Swi2/Snf2 family transcription regulator Modifier of Transcription 1 (Mot1) uses adenosine triphosphate (ATP) to dissociate and reallocate the TATA box-binding protein (TBP) from and between promoters. To reveal how Mot1 removes TBP from TATA box DNA, we determined cryogenic electron microscopy structures that capture different states of the remodeling reaction. The resulting molecular video reveals how Mot1 dissociates TBP in a process that, intriguingly, does not require DNA groove tracking. Instead, the motor grips DNA in the presence of ATP and swings back after ATP hydrolysis, moving TBP to a thermodynamically less stable position on DNA. Dislodged TBP is trapped by a chaperone element that blocks TBP's DNA binding site. Our results show how Swi2/Snf2 proteins can remodel protein-DNA complexes through DNA bending without processive DNA tracking and reveal mechanistic similarities to RNA gripping DEAD box helicases and RIG-I-like immune sensors.

Indexed as

Saccharomyces cerevisiae ProteinsTATA-Binding Protein Associated FactorsAdenosine TriphosphatasesAdenosine TriphosphateDNATATA BoxTATA-Box Binding ProteinTranscription FactorsAdenosine TriphosphatasesAdenosine TriphosphateDNASaccharomyces cerevisiae ProteinsTATA-Binding Protein Associated FactorsTATA-Box Binding ProteinTranscription Factors

Identifiers

PMID37106137
PMCPMC7615866
OpenAlexW4367321017

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.