Evidence map›Paper›PMID 27605472›Full record

ArticleScientific reports2016

Characterization of a putative NsrR homologue in Streptomyces venezuelae reveals a new member of the Rrf2 superfamily.

John T Munnoch, Ma Teresa Pellicer Martinez, Dimitri A Svistunenko, Jason C Crack, Nick E Le Brun, Matthew I Hutchings

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

21 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Fe-S cluster homeostasis and beyond: The multifaceted roles of IscR.Biochimica et biophysica acta. Molecular cell research · 2024
    Review
  5. Review
  6. Harnessing regulatory networks in Actinobacteria for natural product discovery.Journal of industrial microbiology & biotechnology · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Native Mass Spectrometry of Iron-Sulfur Proteins.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Sensing iron availabilityChemical science · 2017
    Article
  19. Article
  20. 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

6 authors at 3 institutions in 1 country.

John T MunnochSchool of Biological Sciences, University of East Anglia, Norwich, Norwich Research Park, United Kingdom.
Ma Teresa Pellicer MartinezCentre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia,Norwich, Norwich Research Park, United Kingdom.
Dimitri A SvistunenkoSchool of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, United Kingdom.
Jason C CrackCentre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia,Norwich, Norwich Research Park, United Kingdom.
Nick E Le BrunCentre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia,Norwich, Norwich Research Park, United Kingdom.
Matthew I HutchingsSchool of Biological Sciences, University of East Anglia, Norwich, Norwich Research Park, United Kingdom.
University of East Anglia · GBNorwich Research Park · GBUniversity of Essex · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J003247/1
6 · The paper itself

Abstract

Members of the Rrf2 superfamily of transcription factors are widespread in bacteria but their functions are largely unexplored. The few that have been characterized in detail sense nitric oxide (NsrR), iron limitation (RirA), cysteine availability (CymR) and the iron sulfur (Fe-S) cluster status of the cell (IscR). In this study we combined ChIP- and dRNA-seq with in vitro biochemistry to characterize a putative NsrR homologue in Streptomyces venezuelae. ChIP-seq analysis revealed that rather than regulating the nitrosative stress response like Streptomyces coelicolor NsrR, Sven6563 binds to a conserved motif at a different, much larger set of genes with a diverse range of functions, including a number of regulators, genes required for glutamine synthesis, NADH/NAD(P)H metabolism, as well as general DNA/RNA and amino acid/protein turn over. Our biochemical experiments further show that Sven6563 has a [2Fe-2S] cluster and that the switch between oxidized and reduced cluster controls its DNA binding activity in vitro. To our knowledge, both the sensing domain and the putative target genes are novel for an Rrf2 protein, suggesting Sven6563 represents a new member of the Rrf2 superfamily. Given the redox sensitivity of its Fe-S cluster we have tentatively named the protein RsrR for Redox sensitive response Regulator.

Indexed as

Bacterial ProteinsIron-Sulfur ProteinsStreptomycesTranscription FactorsDNA, BacterialNucleotide MotifsProtein BindingSequence Homology, Amino AcidBacterial ProteinsDNA, BacterialIron-Sulfur ProteinsTranscription Factors

Identifiers

PMID27605472
PMCPMC5015018
OpenAlexW2514879434

What OpenQuestion holds

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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.