Evidence map›Paper›PMID 28276514›Full record

ArticleScientific reports2017

The human mitochondrial transcription factor A is a versatile G-quadruplex binding protein.

Sébastien Lyonnais, Aleix Tarrés-Solé, Anna Rubio-Cosials, Anna Cuppari, Reicy Brito, Joaquim Jaumot, Raimundo Gargallo, Marta Vilaseca, Cristina Silva, Anton Granzhan and 3 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 51 citations in OpenAlex.

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  11. Evaluation of Ectopic Mitochondrial DNA in HeLa Cells.Current issues in molecular biology · 2022
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 5 institutions in 2 countries.

Sébastien LyonnaisStructural MitoLab, Structural Biology Unit, Molecular Biology Institute of Barcelona (CSIC), Barcelona, 08028, Spain.
Aleix Tarrés-SoléStructural MitoLab, Structural Biology Unit, Molecular Biology Institute of Barcelona (CSIC), Barcelona, 08028, Spain.
Anna Rubio-CosialsStructural MitoLab, Structural Biology Unit, Molecular Biology Institute of Barcelona (CSIC), Barcelona, 08028, Spain.
Anna CuppariStructural MitoLab, Structural Biology Unit, Molecular Biology Institute of Barcelona (CSIC), Barcelona, 08028, Spain.
Reicy BritoStructural MitoLab, Structural Biology Unit, Molecular Biology Institute of Barcelona (CSIC), Barcelona, 08028, Spain.
Joaquim JaumotDepartment of Chemical Engineering and Analytical Chemistry, University of Barcelona, Barcelona, 08028, Spain.
Raimundo GargalloDepartment of Chemical Engineering and Analytical Chemistry, University of Barcelona, Barcelona, 08028, Spain.
Marta VilasecaMass Spectrometry Core Facility, Institute for Research in Biomedicine, IRB Barcelona, 08028 Barcelona, Spain.
Cristina SilvaStructural MitoLab, Structural Biology Unit, Molecular Biology Institute of Barcelona (CSIC), Barcelona, 08028, Spain.
Anton GranzhanCNRS UMR9187, INSERM U1196, Institut Curie, Université Paris-Sud, 91405 Orsay, France.
Marie-Paule Teulade-FichouCNRS UMR9187, INSERM U1196, Institut Curie, Université Paris-Sud, 91405 Orsay, France.
Ramon EritjaIQAC-CSIC, CIBER-BBN, Barcelona, E-08034, Spain.
Maria SolàStructural MitoLab, Structural Biology Unit, Molecular Biology Institute of Barcelona (CSIC), Barcelona, 08028, Spain.
Institut de Biologia Molecular de Barcelona · ESInstitut Curie · FRUniversitat de Barcelona · ESInstitute for Research in Biomedicine · ESInstitute of Advanced Chemistry of Catalonia · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ability of the guanine-rich strand of the human mitochondrial DNA (mtDNA) to form G-quadruplex structures (G4s) has been recently highlighted, suggesting potential functions in mtDNA replication initiation and mtDNA stability. G4 structures in mtDNA raise the question of their recognition by factors associated with the mitochondrial nucleoid. The mitochondrial transcription factor A (TFAM), a high-mobility group (HMG)-box protein, is the major binding protein of human mtDNA and plays a critical role in its expression and maintenance. HMG-box proteins are pleiotropic sensors of DNA structural alterations. Thus, we investigated and uncovered a surprising ability of TFAM to bind to DNA or RNA G4 with great versatility, showing an affinity similar than to double-stranded DNA. The recognition of G4s by endogenous TFAM was detected in mitochondrial extracts by pull-down experiments using a G4-DNA from the mtDNA conserved sequence block II (CSBII). Biochemical characterization shows that TFAM binding to G4 depends on both the G-quartets core and flanking single-stranded overhangs. Additionally, it shows a structure-specific binding mode that differs from B-DNA, including G4-dependent TFAM multimerization. These TFAM-G4 interactions suggest functional recognition of G4s in the mitochondria.

Indexed as

G-QuadruplexesDNADNA-Binding ProteinsDNA, MitochondrialHeLa CellsHumansMitochondrial ProteinsProtein BindingRNATranscription FactorsDNADNA-Binding ProteinsDNA, MitochondrialMitochondrial ProteinsRNATFAM protein, humanTranscription Factors

Identifiers

PMID28276514
PMCPMC5343656
OpenAlexW2591797841

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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.