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Related Experiment Video

Updated: Feb 7, 2026

Author Spotlight: Optimizing CFPS Systems for Synthetic Cell Construction

Author Spotlight: Optimizing CFPS Systems for Synthetic Cell Construction

Published on: April 19, 2024

How do our cells build their protein interactome?

Benoit Coulombe^1,2, Philippe Cloutier³, Marie-Soleil Gauthier³

¹Translational Proteomics Research Unit, Montreal Clinical Research Institute, Montreal, H2W 1R7, QC, Canada. benoit.coulombe@ircm.qc.ca.

Nature Communications

|July 29, 2018

Summary

The PAQosome, a co-chaperone, organizes protein complexes by using different subunits and adaptors. This mechanism allows multiple protein clients to bind simultaneously for assembly and maturation.

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Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing

Published on: October 3, 2018

Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

Chaperones assist in protein folding and complex assembly.
Co-chaperones enhance chaperone specificity and function.
The PAQosome (Particle for Arrangement of Quaternary structure) is a co-chaperone complex involved in proteome organization.

Purpose of the Study:

To characterize the PAQosome complex and elucidate its role in protein homeostasis.
To understand how the PAQosome facilitates the assembly of protein complexes and networks.

Main Methods:

Biochemical characterization of the PAQosome complex.
Analysis of subunit composition and adaptor interactions.
Investigating the binding of client proteins to the PAQosome.

Main Results:

The PAQosome utilizes alternative subunit compositions for diverse client interactions.
Adaptor proteins confer specificity, directing clients to the PAQosome.
The PAQosome provides a platform for simultaneous client binding, aiding complex maturation.

Conclusions:

The PAQosome is a key co-chaperone that organizes the proteome by managing multiple client proteins.
Differential PAQosome assembly and adaptor usage enable precise control over protein complex formation.
This study provides insights into the fundamental mechanisms of protein complex assembly and quality control.