Evidence map›Paper›PMID 27307602›Full record

ArticleNucleic acids research2016

Structural basis of thiol-based regulation of formaldehyde detoxification in H. influenzae by a MerR regulator with no sensor region.

Rafael M Couñago, Nathan H Chen, Chiung-Wen Chang, Karrera Y Djoko, Alastair G McEwan, Bostjan Kobe

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.5field-weighted citation impact, top 15% 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

7 citing papers in PubMed, 11 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

6 authors at 1 institution in 1 country.

Rafael M CouñagoSchool of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Qld 4072, Australia Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, Qld 4072, Australia Institute for Molecular Bioscience, University of Queensland, Brisbane, Qld 4072, Australia rafael.counago@sgc.ox.ac.uk.
Nathan H ChenSchool of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Qld 4072, Australia Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, Qld 4072, Australia.
Chiung-Wen ChangSchool of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Qld 4072, Australia Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, Qld 4072, Australia Institute for Molecular Bioscience, University of Queensland, Brisbane, Qld 4072, Australia.
Karrera Y DjokoSchool of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Qld 4072, Australia Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, Qld 4072, Australia.
Alastair G McEwanSchool of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Qld 4072, Australia Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, Qld 4072, Australia a.mcewan@uq.edu.au.
Bostjan KobeSchool of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Qld 4072, Australia Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, Qld 4072, Australia Institute for Molecular Bioscience, University of Queensland, Brisbane, Qld 4072, Australia b.kobe@uq.edu.au.
University of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pathogenic bacteria such as Haemophilus influenzae, a major cause of lower respiratory tract diseases, must cope with a range of electrophiles generated in the host or by endogenous metabolism. Formaldehyde is one such compound that can irreversibly damage proteins and DNA through alkylation and cross-linking and interfere with redox homeostasis. Its detoxification operates under the control of HiNmlR, a protein from the MerR family that lacks a specific sensor region and does not bind metal ions. We demonstrate that HiNmlR is a thiol-dependent transcription factor that modulates H. influenzae response to formaldehyde, with two cysteine residues (Cys54 and Cys71) identified to be important for its response against a formaldehyde challenge. We obtained crystal structures of HiNmlR in both the DNA-free and two DNA-bound forms, which suggest that HiNmlR enhances target gene transcription by twisting of operator DNA sequences in a two-gene operon containing overlapping promoters. Our work provides the first structural insights into the mechanism of action of MerR regulators that lack sensor regions.

Indexed as

Bacterial ProteinsCrystallography, X-RayDNA, BacterialDNA-Binding ProteinsDNA-Directed RNA PolymerasesFormaldehydeGene Expression Regulation, BacterialHaemophilus influenzaeInactivation, MetabolicKineticsModels, MolecularOperator Regions, GeneticPromoter Regions, GeneticProtein BindingStructure-Activity RelationshipSulfhydryl CompoundsBacterial ProteinsDNA, BacterialDNA-Binding ProteinsDNA-Directed RNA PolymerasesFormaldehydeMerR protein, BacteriaSulfhydryl CompoundsTranscription Factors

Identifiers

PMID27307602
PMCPMC5001606
OpenAlexW2429696056

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.