Evidence map›Paper›PMID 37378428›Full record

ArticleNucleic acids research2023

Structural insights into the DNA recognition mechanism by the bacterial transcription factor PdxR.

Ida Freda, Cécile Exertier, Anna Barile, Antonio Chaves-Sanjuan, Mirella Vivoli Vega, Michail N Isupov, Nicholas J Harmer, Elena Gugole, Paolo Swuec, Martino Bolognesi and 7 more

Abstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Promoter DNA recognition by theFrontiers in molecular biosciences · 2023
    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

17 authors.

Ida FredaDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza, University of Rome, Rome 00185, Italy.
Cécile ExertierInstitute of Molecular Biology and Pathology, National Research Council, Rome 00185, Italy.
Anna BarileInstitute of Molecular Biology and Pathology, National Research Council, Rome 00185, Italy.
Antonio Chaves-SanjuanDepartment of Biosciences, Pediatric Clinical Research Center Romeo ed Enrica Invernizzi and NOLIMITS, University of Milano, Milano 20133, Italy.ORCID 0000-0003-3287-9024
Mirella Vivoli VegaSchool of Biochemistry, University of Bristol, University Walk, BS8 1TD Bristol, UK.
Michail N IsupovGeoffrey Pope Building, University of Exeter, Stocker Road, Exeter EX4 4QD, UK.
Nicholas J HarmerLiving Systems Institute, University of Exeter, Stocker Road, Exeter EX4 4QD, UK.ORCID 0000-0002-4073-0505
Elena GugoleInstitute of Molecular Biology and Pathology, National Research Council, Rome 00185, Italy.
Paolo SwuecCryo-Electron Microscopy Core Facility, Human Technopole, Milano 20157, Italy.
Martino BolognesiDepartment of Biosciences, Pediatric Clinical Research Center Romeo ed Enrica Invernizzi and NOLIMITS, University of Milano, Milano 20133, Italy.ORCID 0000-0002-9253-5170
Anita ScipioniDepartment of Chemistry, Sapienza, University of Rome, Rome 00185, Italy.
Carmelinda SavinoInstitute of Molecular Biology and Pathology, National Research Council, Rome 00185, Italy.
Martino Luigi Di SalvoDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza, University of Rome, Rome 00185, Italy.
Roberto ContestabileDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza, University of Rome, Rome 00185, Italy.ORCID 0000-0002-5235-9993
Beatrice ValloneDepartment of Biochemical Sciences "A. Rossi Fanelli", Sapienza, University of Rome, Rome 00185, Italy.
Angela TramontiInstitute of Molecular Biology and Pathology, National Research Council, Rome 00185, Italy.
Linda Celeste MontemiglioInstitute of Molecular Biology and Pathology, National Research Council, Rome 00185, Italy.ORCID 0000-0002-4253-7493

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Specificity in protein-DNA recognition arises from the synergy of several factors that stem from the structural and chemical signatures encoded within the targeted DNA molecule. Here, we deciphered the nature of the interactions driving DNA recognition and binding by the bacterial transcription factor PdxR, a member of the MocR family responsible for the regulation of pyridoxal 5'-phosphate (PLP) biosynthesis. Single particle cryo-EM performed on the PLP-PdxR bound to its target DNA enabled the isolation of three conformers of the complex, which may be considered as snapshots of the binding process. Moreover, the resolution of an apo-PdxR crystallographic structure provided a detailed description of the transition of the effector domain to the holo-PdxR form triggered by the binding of the PLP effector molecule. Binding analyses of mutated DNA sequences using both wild type and PdxR variants revealed a central role of electrostatic interactions and of the intrinsic asymmetric bending of the DNA in allosterically guiding the holo-PdxR-DNA recognition process, from the first encounter through the fully bound state. Our results detail the structure and dynamics of the PdxR-DNA complex, clarifying the mechanism governing the DNA-binding mode of the holo-PdxR and the regulation features of the MocR family of transcription factors.

Indexed as

Bacterial ProteinsTranscription FactorsBacillus clausiiBacteriaDNAProtein BindingPyridoxal PhosphateBacterial ProteinsDNAPyridoxal PhosphateTranscription Factors

Identifiers

PMID37378428
PMCPMC10450172

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.