Evidence map›Paper›PMID 21658482›Full record

ReviewBiochimica et biophysica acta2011

One small step for Mot1; one giant leap for other Swi2/Snf2 enzymes?

Ramya Viswanathan, David T Auble

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. 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
  2. Biophysics of Chromatin Remodeling.Annual review of biophysics · 2021
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Swi2/Snf2 remodelers: hybrid views on hybrid molecular machines.Current opinion in structural biology · 2012
    Review
  12. Article
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

2 authors at 1 institution in 1 country.

Ramya ViswanathanDepartment of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, VA 22908, USA.
David T Auble
University 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 GM55763NIGMS NIH HHS R01 GM055763
6 · The paper itself

Abstract

The TATA-binding protein (TBP) is a major target for transcriptional regulation. Mot1, a Swi2/Snf2-related ATPase, dissociates TBP from DNA in an ATP dependent process. The experimental advantages of this relatively simple reaction have been exploited to learn more about how Swi2/Snf2 ATPases function biochemically. However, many unanswered questions remain and fundamental aspects of the Mot1 mechanism are still under debate. Here, we review the available data and integrate the results with structural and biochemical studies of related enzymes to derive a model for Mot1's catalytic action consistent with the broad literature on enzymes in this family. We propose that the Mot1 ATPase domain is tethered to TBP by a flexible, spring-like linker of alpha helical hairpins. The linker juxtaposes the ATPase domain such that it can engage duplex DNA on one side of the TBP-DNA complex. This allows the ATPase to employ short-range, nonprocessive ATP-driven DNA tracking to pull or push TBP off its DNA site. DNA translocation is a conserved property of ATPases in the broader enzyme family. As such, the model explains how a structurally and functionally conserved ATPase domain has been put to use in a very different context than other enzymes in the Swi2/Snf2 family. This article is part of a Special Issue entitled:Snf2/Swi2 ATPase structure and function.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateChromatin Assembly and DisassemblyDNA-Binding ProteinsDNA, FungalProtein Structure, TertiarySaccharomyces cerevisiae ProteinsTATA-Binding Protein Associated FactorsTATA-Box Binding ProteinTranscriptional ActivationTranscription FactorsTranscription Factor TFIIDTranslocation, GeneticAdenosine TriphosphatasesAdenosine TriphosphateBTAF1 protein, humanDNA-Binding ProteinsDNA, FungalMOT1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSNF2 protein, S cerevisiaeTATA-Binding Protein Associated FactorsTATA-Box Binding ProteinTranscription FactorsTranscription Factor TFIID

Identifiers

PMID21658482
PMCPMC3171519
OpenAlexW2055083006

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.