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Related Experiment Video

Updated: Jan 18, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

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

Yasmin Igbaria-Jaber¹, Alysia Mandato², Lukas Hofmann¹

¹Department of Chemistry and the Institute of Nanotechnology and Advanced Materials, Faculty of Exact Sciences, Bar Ilan University, Ramat-Gan, Israel.

Protein Science : a Publication of the Protein Society

|September 13, 2025

Summary

This summary is machine-generated.

Mycobacterium tuberculosis copper-sensing repressor (CsoR) exists as a tetramer in equilibrium with dimers. DNA binding affects protein exchange, influencing transcription regulation.

Keywords:

CsoR EPR protein oligomerization protein–DNA interaction transcription mechanism

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Last Updated: Jan 18, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Protein oligomerization is crucial for cellular functions.
Copper-sensing operon repressor (CsoR) regulates the cso operon in Mycobacterium tuberculosis.
CsoR dissociation from DNA upon copper binding enables transcription.

Purpose of the Study:

To investigate the oligomeric state of Mycobacterium tuberculosis CsoR.
To determine how DNA binding affects CsoR's oligomeric state and dynamics.
To elucidate the role of CsoR oligomerization in transcriptional regulation.

Main Methods:

Electron paramagnetic resonance (EPR) spectroscopy, including continuous wave and double electron-electron resonance (DEER).
Site-directed spin labeling to probe protein structure and dynamics.
Analysis of EPR data to determine oligomeric states and inter-spin distances.

Main Results:

CsoR exists predominantly as a tetramer in equilibrium with a dimer population, irrespective of DNA binding.
EPR data revealed distinct mobile (dimer) and immobile (tetramer) components.
DNA binding did not alter the tetramer-dimer equilibrium but affected the exchange rate between protein units.

Conclusions:

CsoR maintains a dynamic equilibrium between tetrameric and dimeric states.
DNA interaction modulates CsoR protein exchange dynamics, contributing to transcriptional control.
Understanding CsoR oligomerization provides insights into bacterial gene regulation mechanisms.