Evidence map›Paper›PMID 32009151›Full record

ArticleNucleic acids research2020

Biphasic unbinding of a metalloregulator from DNA for transcription (de)repression in Live Bacteria.

Won Jung, Kushal Sengupta, Brian M Wendel, John D Helmann, Peng Chen

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Microbial metal physiology: ions to ecosystems.Nature reviews. Microbiology · 2025
    Review
  4. Article
  5. Article
  6. Memory effects of transcription regulator-DNA interactions in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. 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

5 authors at 1 institution in 1 country.

Won JungDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Kushal SenguptaDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Brian M WendelDepartment of Microbiology, Cornell University, Ithaca, NY 14853, USA.
John D HelmannDepartment of Microbiology, Cornell University, Ithaca, NY 14853, USA.
Peng ChenDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Cornell University · US

Funding

Bacillus subtilis Stress ResponsesR35GM122461 · NIGMS · CORNELL UNIVERSITY · PI John D Helmann · 2017 to 2026
$7.6M
Unusual mechanisms of metal regulation in bacteria: from single molecules to single cells to cell communitiesR01GM109993 · NIGMS · CORNELL UNIVERSITY · PI Peng Chen · 2014 to 2026
$3.9M
NIGMS NIH HHS R01 GM109993NIGMS NIH HHS R35 GM122461
6 · The paper itself

Abstract

Microorganisms use zinc-sensing regulators to alter gene expression in response to changes in the availability of zinc, an essential micronutrient. Under zinc-replete conditions, the Fur-family metalloregulator Zur binds to DNA tightly in its metallated repressor form to Zur box operator sites, repressing the transcription of zinc uptake transporters. Derepression comes from unbinding of the regulator, which, under zinc-starvation conditions, exists in its metal-deficient non-repressor forms having no significant affinity with Zur box. While the mechanism of transcription repression by Zur is well-studied, little is known on how derepression by Zur could be facilitated. Using single-molecule/single-cell measurements, we find that in live Escherichia coli cells, Zur's unbinding rate from DNA is sensitive to Zur protein concentration in a first-of-its-kind biphasic manner, initially impeded and then facilitated with increasing Zur concentration. These results challenge conventional models of protein unbinding being unimolecular processes and independent of protein concentration. The facilitated unbinding component likely occurs via a ternary complex formation mechanism. The impeded unbinding component likely results from Zur oligomerization on chromosome involving inter-protein salt-bridges. Unexpectedly, a non-repressor form of Zur is found to bind chromosome tightly, likely at non-consensus sequence sites. These unusual behaviors could provide functional advantages in Zur's facile switching between repression and derepression.

Indexed as

Gene Expression Regulation, BacterialTranscription, GeneticBinding SitesChromosomes, BacterialDNA, BacterialDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsKineticsProtein BindingProtein MultimerizationSingle-Cell AnalysisZincDNA, BacterialDNA-Binding ProteinsEscherichia coli ProteinsZincZur protein, E coli

Identifiers

PMID32009151
PMCPMC7049717
OpenAlexW3004695264

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.