Evidence map›Paper›PMID 11296235›Full record

ArticleThe EMBO journal2001

MOT1-catalyzed TBP-DNA disruption: uncoupling DNA conformational change and role of upstream DNA.

R P Darst, D Wang, D T Auble

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

R P DarstDepartment of Biochemistry and Molecular Genetics, University of Virginia Health Science Center, Charlottesville, VA 22908-0733, USA.
D Wang
D T Auble
University of Virginia · 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

SNF2/SWI2-related ATPases employ ATP hydrolysis to disrupt protein-DNA interactions, but how ATP hydrolysis is coupled to disruption is not understood. Here we examine the mechanism of action of MOT1, a yeast SNF2/SWI2-related ATPase that uses ATP hydrolysis to remove TATA binding protein (TBP) from DNA. MOT1 function requires a 17 bp DNA 'handle' upstream of the TATA box, which must be double stranded. Remarkably, MOT1-catalyzed disruption of TBP-DNA does not appear to require DNA strand separation, DNA bending or twisting of the DNA helix. Thus, TBP-DNA disruption is accomplished in a reaction apparently not driven by a change in DNA structure. MOT1 action is supported by DNA templates in which the handle is connected to the TATA box via single-stranded DNA, indicating that the upstream duplex DNA can be conformationally uncoupled from the TATA box. Combining these results with proposed similarities between SNF2/SWI2 ATPases and helicases, we suggest that MOT1 uses ATP hydrolysis to translocate along the handle and thereby disrupt interactions between TBP and DNA.

Indexed as

Saccharomyces cerevisiae ProteinsTATA-Binding Protein Associated FactorsAdenosine TriphosphatasesDNADNA-Binding ProteinsDNA HelicasesFungal ProteinsGene Expression RegulationModels, GeneticNucleic Acid ConformationNucleoproteinsProtein BindingTATA BoxTATA-Box Binding ProteinTranscription FactorsAdenosine TriphosphatasesDNADNA-Binding ProteinsDNA HelicasesFungal ProteinsMOT1 protein, S cerevisiaeNucleoproteinsSaccharomyces cerevisiae ProteinsTATA-Binding Protein Associated FactorsTATA-Box Binding ProteinTranscription Factors

Identifiers

PMID11296235
PMCPMC125425
OpenAlexW2079747909

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.