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Related Concept Videos

The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
Protein Complex Assembly02:41

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.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

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.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Related Experiment Video

Updated: Jun 21, 2026

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

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

Published on: December 17, 2016

Getting to first base in proteasome assembly.

Henrike C Besche1, Andreas Peth, Alfred L Goldberg

  • 1Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.

Cell
|July 15, 2009
PubMed
Summary
This summary is machine-generated.

The 26S proteasome

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Related Experiment Videos

Last Updated: Jun 21, 2026

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
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Published on: December 17, 2016

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The eukaryotic 26S proteasome is a large protein complex essential for cellular protein degradation.
  • Its assembly is a complex process requiring precise regulation of subunit interactions.
  • Understanding the 19S regulatory particle assembly is crucial for comprehending proteasome function.

Purpose of the Study:

  • To elucidate the ordered assembly pathway of the 19S regulatory particle base.
  • To identify novel precursor complexes and chaperones involved in this assembly process.

Main Methods:

  • Proteomic analysis of cellular extracts.
  • Biochemical assays to characterize protein interactions.
  • Genetic manipulation to study chaperone function.

Main Results:

  • Identification of previously unknown precursor complexes in 19S base assembly.
  • Discovery of four dedicated chaperones that facilitate specific assembly steps.
  • Characterization of the sequential order of subunit incorporation.

Conclusions:

  • The assembly of the 19S regulatory particle base is a stepwise process.
  • Dedicated chaperones and specific precursor complexes are critical for ensuring the fidelity of 19S base assembly.
  • This work provides a framework for understanding the intricate assembly of the 26S proteasome.