Evidence map›Paper›PMID 19651042›Full record

ArticleBiophysical journal2009

Single-molecule study of metalloregulator CueR-DNA interactions using engineered Holliday junctions.

Nesha May Andoy, Susanta K Sarkar, Qi Wang, Debashis Panda, Jaime J Benítez, Aleksandr Kalininskiy, Peng Chen

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2009. 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
0.7field-weighted citation impact, top 26% 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, 28 citations in OpenAlex.

  1. TheGenes · 2026
    Article
  2. The Copper Efflux Regulator (CueR).Sub-cellular biochemistry · 2024
    Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Pathogenic adaptations to host-derived antibacterial copper.Frontiers in cellular and infection microbiology · 2014
    Review
  12. Review
  13. Article
  14. Direct substitution and assisted dissociation pathways for turning off transcription by a MerR-family metalloregulator.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  15. 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

7 authors at 1 institution in 1 country.

Nesha May AndoyDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.
Susanta K Sarkar
Qi Wang
Debashis Panda
Jaime J Benítez
Aleksandr Kalininskiy
Peng Chen
Cornell University · US

Funding

Single-Molecule Study of Dynamics and Mechanisms of Biomacromolecule InteractionsR01GM082939 · NIGMS · CORNELL UNIVERSITY · PI CHEN, PENG · 2008 to 2012
$1.3M
NIGMS NIH HHS GM082939NIGMS NIH HHS R01 GM082939
6 · The paper itself

Abstract

To maintain normal metal metabolism, bacteria use metal-sensing metalloregulators to control transcription of metal resistance genes. Depending on their metal-binding states, the MerR-family metalloregulators change their interactions with DNA to suppress or activate transcription. To understand their functions fundamentally, we study how CueR, a Cu(1+)-responsive MerR-family metalloregulator, interacts with DNA, using an engineered DNA Holliday junction (HJ) as a protein-DNA interaction reporter in single-molecule fluorescence resonance energy transfer measurements. By analyzing the single-molecule structural dynamics of the engineered HJ in the presence of various concentrations of both apo- and holo-CueR, we show how CueR interacts with the two conformers of the engineered HJ, forming variable protein-DNA complexes at different protein concentrations and changing the HJ structures. We also show how apo- and holo-CueR differ in their interactions with DNA, and discuss their similarities and differences with other MerR-family metalloregulators. The surprising finding that holo-CueR binds more strongly to DNA than to apo-CueR suggests functional differences among MerR-family metalloregulators, in particular in their mechanisms of switching off gene transcription after activation. The study also corroborates the general applicability of engineered HJs as single-molecule reporters for protein-DNA interactions, which are fundamental processes in gene replication, transcription, recombination, and regulation.

Indexed as

Base SequenceDNA, CruciformEscherichia coliEscherichia coli ProteinsFluorescence PolarizationFluorescence Resonance Energy TransferKineticsMolecular Sequence DataNucleic Acid ConformationTrans-ActivatorscueR protein, E coliDNA, CruciformEscherichia coli ProteinsTrans-Activators

Identifiers

PMID19651042
PMCPMC2718160
OpenAlexW2064715512

What OpenQuestion holds

Textmetadata
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.