Evidence map›Paper›PMID 29556010›Full record

ArticleNature communications2018

The MerR-like protein BldC binds DNA direct repeats as cooperative multimers to regulate Streptomyces development.

Maria A Schumacher, Chris D den Hengst, Matthew J Bush, T B K Le, Ngat T Tran, Govind Chandra, Wenjie Zeng, Brady Travis, Richard G Brennan, Mark J Buttner

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 37 citations in OpenAlex.

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  20. When is a transcription factor a NAP?Current opinion in microbiology · 2020
    Review
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

10 authors at 2 institutions in 2 countries.

Maria A SchumacherDepartment of Biochemistry, Duke University School of Medicine, Durham, NC, 27710, USA. maria.schumacher@duke.edu.
Chris D den HengstDepartment of Molecular Microbiology, John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, UK.
Matthew J BushDepartment of Molecular Microbiology, John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, UK.
T B K LeDepartment of Molecular Microbiology, John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, UK.ORCID http://orcid.org/0000-0003-4764-8851
Ngat T TranDepartment of Molecular Microbiology, John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, UK.
Govind ChandraDepartment of Molecular Microbiology, John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, UK.
Wenjie ZengDepartment of Biochemistry, Duke University School of Medicine, Durham, NC, 27710, USA.
Brady TravisDepartment of Biochemistry, Duke University School of Medicine, Durham, NC, 27710, USA.
Richard G BrennanDepartment of Biochemistry, Duke University School of Medicine, Durham, NC, 27710, USA. richard.brennan@duke.edu.
Mark J ButtnerDepartment of Molecular Microbiology, John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, UK. mark.buttner@jic.ac.uk.
John Innes Centre · GBDuke University · US

Funding

Deciphering fundamental biological processes involving protein-nucleic acid interactions at the molecular levelR35GM130290 · NIGMS · DUKE UNIVERSITY · PI Maria Schumacher · 2019 to 2026
$4.9M
Complete atomic dissection of the B. subtilis nitrogen regulatory pathwayR01GM115547 · NIGMS · DUKE UNIVERSITY · PI SCHUMACHER, MARIA · 2015 to 2018
$1.2M
Biotechnology and Biological Sciences Research Council BB/H006125/1Biotechnology and Biological Sciences Research Council BBS/E/J/00000015NIGMS NIH HHS R01 GM115547NIGMS NIH HHS R35 GM130290
6 · The paper itself

Abstract

Streptomycetes are notable for their complex life cycle and production of most clinically important antibiotics. A key factor that controls entry into development and the onset of antibiotic production is the 68-residue protein, BldC. BldC is a putative DNA-binding protein related to MerR regulators, but lacks coiled-coil dimerization and effector-binding domains characteristic of classical MerR proteins. Hence, the molecular function of the protein has been unclear. Here we show that BldC is indeed a DNA-binding protein and controls a regulon that includes other key developmental regulators. Intriguingly, BldC DNA-binding sites vary significantly in length. Our BldC-DNA structures explain this DNA-binding capability by revealing that BldC utilizes a DNA-binding mode distinct from MerR and other known regulators, involving asymmetric head-to-tail oligomerization on DNA direct repeats that results in dramatic DNA distortion. Notably, BldC-like proteins radiate throughout eubacteria, establishing BldC as the founding member of a new structural family of regulators.

Indexed as

Bacterial ProteinsBase SequenceBinding SitesDNA, BacterialDNA-Binding ProteinsGene Expression Regulation, BacterialGene Expression Regulation, DevelopmentalGenes, BacterialModels, MolecularNucleic Acid ConformationPromoter Regions, GeneticProtein Structure, QuaternaryRegulonRepetitive Sequences, Nucleic AcidRepressor ProteinsStatic ElectricityBacterial ProteinsDNA, BacterialDNA-Binding ProteinsMerR protein, BacteriaRepressor ProteinswhiL protein, Streptomyces coelicolor

Identifiers

PMID29556010
PMCPMC5859096
OpenAlexW2792576316

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.