Evidence map›Paper›PMID 40944455›Full record

ArticleProtein science : a publication of the Protein Society2025

Tracking Copper sensing operon Repressor (CsoR) oligomerization in solution using Electron Paramagnetic Resonance spectroscopy.

Yasmin Igbaria-Jaber, Alysia Mandato, Lukas Hofmann, Yulia Shenberger, Lada Gevorkyan-Airapetov, Liel Sapir, Sunil Saxena, Sharon Ruthstein

Abstract read
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In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Review
  2. Review
  3. 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

8 authors.

Yasmin Igbaria-JaberDepartment of Chemistry and the Institute of Nanotechnology and Advanced Materials, Faculty of Exact Sciences, Bar Ilan University, Ramat-Gan, Israel.
Alysia MandatoDepartment of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania, USA.
Lukas HofmannDepartment of Chemistry and the Institute of Nanotechnology and Advanced Materials, Faculty of Exact Sciences, Bar Ilan University, Ramat-Gan, Israel.
Yulia ShenbergerDepartment of Chemistry and the Institute of Nanotechnology and Advanced Materials, Faculty of Exact Sciences, Bar Ilan University, Ramat-Gan, Israel.
Lada Gevorkyan-AirapetovDepartment of Chemistry and the Institute of Nanotechnology and Advanced Materials, Faculty of Exact Sciences, Bar Ilan University, Ramat-Gan, Israel.
Liel SapirDepartment of Chemistry and the Institute of Nanotechnology and Advanced Materials, Faculty of Exact Sciences, Bar Ilan University, Ramat-Gan, Israel.ORCID 0000-0001-7652-6541
Sunil SaxenaDepartment of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania, USA.ORCID 0000-0001-9098-6114
Sharon RuthsteinDepartment of Chemistry and the Institute of Nanotechnology and Advanced Materials, Faculty of Exact Sciences, Bar Ilan University, Ramat-Gan, Israel.ORCID 0000-0002-1741-6892

Funding

the Binational Science Foundation 2022103
6 · The paper itself

Abstract

Protein oligomerization is a fundamental biological process that plays a pivotal role in regulating numerous cellular functions. In this study, we investigated the oligomeric state of copper-sensing operon repressor (CsoR), a transcriptional repressor bound to the cso operon in Mycobacterium tuberculosis. Upon copper binding, CsoR dissociates from the promoter region, permitting transcription initiation. Electron paramagnetic resonance (EPR) spectroscopy was employed to investigate the oligomeric state of CsoR as a function of DNA binding. The data indicated that CsoR exists predominantly as a tetramer in equilibrium with some dimer population, independent of DNA binding. Room temperature continuous wave EPR measurements suggested the presence of two components, where the immobile component was related to spin-labeled CsoR dimers within a tetrameric assembly, and the mobile component was associated with the dimeric assembly. Relaxation measurements were used to verify this assignment, and double electron electron resonance experiments were used to characterize the oligomeric state. Using this approach, we showed that although the equilibrium between tetramers and dimers is preserved as a function of DNA binding, the exchange between the different protein units is affected by the presence of DNA, which likely contributes to the transcription regulation.

Indexed as

Bacterial ProteinsCopperMycobacterium tuberculosisProtein MultimerizationRepressor ProteinsElectron Spin Resonance SpectroscopyOperonBacterial ProteinsCopperRepressor ProteinsCsoREPRprotein–DNA interactionprotein oligomerizationtranscription mechanism

Identifiers

PMID40944455
PMCPMC12432415

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Registered trials

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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.