Evidence map›Paper›PMID 23396446›Full record

ArticleNucleic acids research2013

Study of PcaV from Streptomyces coelicolor yields new insights into ligand-responsive MarR family transcription factors.

Jennifer R Davis, Breann L Brown, Rebecca Page, Jason K Sello

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.8field-weighted citation impact, top 4% 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

34 citing papers in PubMed, 67 citations in OpenAlex.

  1. A conservedFrontiers in microbiology · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. The MarR-Type Regulator PA3458 Is Involved in Osmoadaptation Control inInternational journal of molecular sciences · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
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  14. Article
  15. Article
  16. Article
  17. Review
  18. SAV4189, a MarR-Family Regulator inFrontiers in microbiology · 2018
    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

4 authors at 1 institution in 1 country.

Jennifer R DavisDepartment of Molecular Pharmacology and Physiology, Brown University, Providence, RI 02912, USA.
Breann L Brown
Rebecca Page
Jason K Sello
Brown University · US

Funding

X-RAY STRUCTURE OF RIFM PROTEIN FROM THE BIOSYNTHESIS PATHWAY OF THE ANSAMYCIN AP41RR012408 · NCRR · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI ORVILLE, ALLEN M · 1998 to 2011
$32.2M
Macromolecular Crystallography at the National Synchrotron Light SourceP41GM103473 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI SWEET, ROBERT M · 2012 to 2013
$4.9M
CD SPECTROPHOTOMETER: STRUCTURAL BIOL, PROTEIN, MOLECULAR PHARMACOLOGYS10RR020923 · NCRR · BROWN UNIVERSITY · PI MIERKE, DALE F · 2006 to 2006
$105k
Molecular basis for actin reorganization by the neuronal protein SPARF31NS062630 · NINDS · BROWN UNIVERSITY · PI BROWN, BREANN · 2009 to 2011
$86k
NCRR NIH HHS 1S10RR020923NCRR NIH HHS P41RR012408NIGMS NIH HHS P41GM103473NINDS NIH HHS NS062630
6 · The paper itself

Abstract

MarR family proteins constitute a group of >12 000 transcriptional regulators encoded in bacterial and archaeal genomes that control gene expression in metabolism, stress responses, virulence and multi-drug resistance. There is much interest in defining the molecular mechanism by which ligand binding attenuates the DNA-binding activities of these proteins. Here, we describe how PcaV, a MarR family regulator in Streptomyces coelicolor, controls transcription of genes encoding β-ketoadipate pathway enzymes through its interaction with the pathway substrate, protocatechuate. This transcriptional repressor is the only MarR protein known to regulate this essential pathway for aromatic catabolism. In in vitro assays, protocatechuate and other phenolic compounds disrupt the PcaV-DNA complex. We show that PcaV binds protocatechuate in a 1:1 stoichiometry with the highest affinity of any MarR family member. Moreover, we report structures of PcaV in its apo form and in complex with protocatechuate. We identify an arginine residue that is critical for ligand coordination and demonstrate that it is also required for binding DNA. We propose that interaction of ligand with this arginine residue dictates conformational changes that modulate DNA binding. Our results provide new insights into the molecular mechanism by which ligands attenuate DNA binding in this large family of transcription factors.

Indexed as

ArginineBacterial ProteinsBinding SitesDNA, BacterialDNA-Binding ProteinsHydroxybenzoatesLigandsModels, MolecularOperator Regions, GeneticPhenolsProtein BindingProtein ConformationRepressor ProteinsStreptomyces coelicolor3,4-dihydroxybenzoateArginineBacterial ProteinsDNA, BacterialDNA-Binding ProteinsHydroxybenzoatesLigandsPhenolsRepressor Proteins

Identifiers

PMID23396446
PMCPMC3616709
OpenAlexW2039040624

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.