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Related Experiment Video

Updated: Mar 25, 2026

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Interaction Analysis of a Two-Component System Using Nanodiscs.

Patrick Hörnschemeyer¹, Viktoria Liss¹, Ralf Heermann²

¹Fachbereich Biologie/Chemie, Mikrobiologie, Universität Osnabrück, Barbarastrasse 11, D-49076, Osnabrück, Germany.

|February 17, 2016

Summary

This summary is machine-generated.

This study quantifies interactions of the bacterial membrane protein CpxA with CpxR and CpxP. ATP binding enhances CpxA’s affinity for CpxR, revealing key insights into bacterial signal transduction.

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Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

Area of Science:

Microbiology
Biochemistry
Molecular Biology

Background:

Two-component systems regulate bacterial adaptation to environmental stimuli.
These systems rely on phosphorylation cascades involving histidine kinases and response regulators.
Understanding protein interactions within these systems is crucial for deciphering signal fidelity.

Purpose of the Study:

To analyze the interaction kinetics between the membrane-bound histidine kinase CpxA and its partners, CpxR and CpxP.
To quantify the binding affinities of CpxA with CpxR and CpxP using reconstituted systems.
To elucidate the role of ATP in modulating CpxA-CpxR interactions.

Main Methods:

Reconstitution of full-length membrane-bound histidine kinase CpxA in nanodiscs.
Surface plasmon resonance (SPR) spectroscopy to analyze CpxA-CpxR and CpxA-CpxP interactions.
Microscale thermophoresis (MST) to determine binding affinities.

Main Results:

Quantified the affinity of membrane-embedded CpxA for its cognate response regulator CpxR.
Demonstrated a tenfold increase in CpxA-CpxR affinity in the presence of ATP.
Determined a substantially lower affinity between CpxA and the accessory protein CpxP compared to CpxR.

Conclusions:

The findings provide the first quantitative interaction data for membrane-embedded CpxA with its partners.
Increased affinity for CpxR upon ATP binding suggests stable association of phosphorylated CpxR with CpxA in vivo.
The study enhances the understanding of signal transduction mechanisms in bacterial two-component systems.