Evidence map›Paper›PMID 25364981›Full record

ArticlePloS one2014

Towards novel amino acid-base contacts in gene regulatory proteins: AraR--a case study.

Isabel Lopes Correia, Irina Saraiva Franco, Isabel de Sá-Nogueira

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 34% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. 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

3 authors at 2 institutions in 1 country.

Isabel Lopes CorreiaDepartamento de Ciências da Vida (DCV), Centro de Recursos Microbiológicos (CREM), Faculdade de Ciências e Tecnologia (FCT-UNL), Caparica, Portugal; Instituto Tecnologia Química e Biológica (ITQB-UNL), Oeiras, Portugal.
Irina Saraiva FrancoInstituto Tecnologia Química e Biológica (ITQB-UNL), Oeiras, Portugal.
Isabel de Sá-NogueiraDepartamento de Ciências da Vida (DCV), Centro de Recursos Microbiológicos (CREM), Faculdade de Ciências e Tecnologia (FCT-UNL), Caparica, Portugal.
Instituto de Biologia Experimental e Tecnológica · PTRede de Química e Tecnologia · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AraR is a transcription factor involved in the regulation of carbon catabolism in Bacillus subtilis. This regulator belongs to the vast GntR family of helix-turn-helix (HTH) bacterial metabolite-responsive transcription factors. In this study, AraR-DNA specific interactions were analysed by an in vitro missing-contact probing and validated using an in vivo model. We show that amino acid E30 of AraR, a highly conserved residue in GntR regulators, is indirectly responsible for the specificity of amino acid-base contacts, and that by mutating this residue it will be possible to achieve new specificities towards DNA contacts. The results highlight the importance in DNA recognition and binding of highly conserved residues across certain families of transcription factors that are located in the DNA-binding domain but not predicted to specifically contact bases on the DNA. These new findings not only contribute to a more detailed comprehension of AraR-operator interactions, but may also be useful for the establishment of a framework of rules governing protein-DNA recognition.

Indexed as

Models, MolecularBacillus subtilisBacterial ProteinsDNA, BacterialEscherichia coliTranscription FactorsBacterial ProteinsDNA, BacterialTranscription Factors

Identifiers

PMID25364981
PMCPMC4218819
OpenAlexW2080483172

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.