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Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Related Experiment Video

Updated: Jan 25, 2026

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

Dissecting protein-protein interactions in proteasome assembly: Implication to its self-assembly.

Smita P Pilla¹, Babu R¹, Ranjit P Bahadur¹

¹Computational Structural Biology Laboratory, Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur, India.

Journal of Molecular Recognition : JMR

|May 3, 2019

Summary

The 26S proteasome

Keywords:

20S core particle evolutionary conservation interaction network proteasome assembly protein-protein interfaces

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Area of Science:

Proteasome structure and function
Molecular and cellular biology
Protein-protein interactions

Background:

The 26S proteasome maintains cellular homeostasis by degrading damaged proteins.
It comprises a 20S core particle (CP) and 19S regulatory particles.
The 20S CP is formed by stacked alpha and beta subunits.

Purpose of the Study:

To understand the structure-function relationship of the 20S proteasome core particle.
To analyze the structural and physiochemical properties of protein-protein interfaces within the 20S CP.
To investigate the evolutionary conservation of the 20S CP.

Main Methods:

Dissection of protein-protein interfaces within the 20S proteasome core particle.
Analysis of structural and physiochemical properties (size, hydrophobicity, polarity, salt-bridge density).
Comparative analysis of evolutionary conservation across alpha and beta subunits and different domains of life.

Main Results:

Intra-alpha interfaces are larger and more hydrophobic; inter-beta interfaces are well-packed, polar, and have high salt-bridge density.
Beta subunit residues are more conserved than alpha subunits during proteasome assembly; multi-interface residues are the most conserved.
Eukaryotic proteasome interfaces are larger and better packed than archaeal and bacterial ones.

Conclusions:

Structural and physiochemical properties of interfaces dictate 20S proteasome assembly.
Glycine is a highly conserved residue at alpha and beta subunit interfaces.
Findings provide a structural basis for 20S core particle assembly across all domains of life.