Evidence map›Paper›PMID 29248151›Full record

ArticleBiophysical journal2018

Protein Flexibility and Synergy of HMG Domains Underlie U-Turn Bending of DNA by TFAM in Solution.

Anna Rubio-Cosials, Federica Battistini, Alexander Gansen, Anna Cuppari, Pau Bernadó, Modesto Orozco, Jörg Langowski, Katalin Tóth, Maria Solà

Abstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Review
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  11. Review
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  13. Mitochondrial transcription factor A promotes DNA strand cleavage at abasic sites.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Article
  15. Organization of DNA in Mammalian Mitochondria.International journal of molecular sciences · 2019
    Review
  16. Review
  17. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Anna Rubio-CosialsStructural MitoLab, Department of Structural Biology, Molecular Biology Institute Barcelona (IBMB-CSIC), Barcelona, Spain.
Federica BattistiniInstitute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and Technology, Institute for Research in Biomedicine, Barcelona, Spain; Joint BSC-IRB Program in Computational Biology, Institute for Research in Biomedicine, Barcelona, Spain.
Alexander GansenDeutsches Krebsforschungszentrum, Division Biophysics of Macromolecules, Heidelberg, Germany.
Anna CuppariStructural MitoLab, Department of Structural Biology, Molecular Biology Institute Barcelona (IBMB-CSIC), Barcelona, Spain.
Pau BernadóCentre de Biochimie Structurale (CBS), Inserm, CNRS and Université de Montpellier, France.
Modesto OrozcoInstitute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and Technology, Institute for Research in Biomedicine, Barcelona, Spain; Joint BSC-IRB Program in Computational Biology, Institute for Research in Biomedicine, Barcelona, Spain; Department of Biochemistry and Biomedicine, Faculty of Biology, University of Barcelona, Barcelona, Spain.
Jörg LangowskiDeutsches Krebsforschungszentrum, Division Biophysics of Macromolecules, Heidelberg, Germany.
Katalin TóthDeutsches Krebsforschungszentrum, Division Biophysics of Macromolecules, Heidelberg, Germany. Electronic address: kt@dkfz-heidelberg.de.
Maria SolàStructural MitoLab, Department of Structural Biology, Molecular Biology Institute Barcelona (IBMB-CSIC), Barcelona, Spain. Electronic address: maria.sola@ibmb.csic.es.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human mitochondrial transcription factor A (TFAM) distorts DNA into a U-turn, as shown by crystallographic studies. The relevance of this U-turn is associated with transcription initiation at the mitochondrial light strand promoter (LSP). However, it has not been yet discerned whether a tight U-turn or an alternative conformation, such as a V-shape, is formed in solution. Here, single-molecule FRET experiments on freely diffusing TFAM/LSP complexes containing different DNA lengths show that a DNA U-turn is induced by progressive and cooperative binding of the two TFAM HMG-box domains and the linker between them. SAXS studies further show compaction of the protein upon complex formation. Finally, molecular dynamics simulations reveal that TFAM/LSP complexes are dynamic entities, and the HMG boxes induce the U-turn against the tendency of the DNA to adopt a straighter conformation. This tension is resolved by reversible unfolding of the linker, which is a singular mechanism that allows a flexible protein to stabilize a tight bending of DNA.

Indexed as

Mechanical PhenomenaBiomechanical PhenomenaDiffusionDNADNA-Binding ProteinsHumansMitochondrial ProteinsMolecular Dynamics SimulationNucleic Acid ConformationProtein DomainsSolutionsTranscription FactorsDNADNA-Binding ProteinsMitochondrial Proteinsmitochondrial transcription factor ASolutionsTranscription Factors

Identifiers

PMID29248151
PMCPMC6028807

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Registered trials

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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.